###################################################### ##### Sequences and other information for the C2 Domain ##### Prepared as a part of MeTaDoR (http://proteomics.bioengr.uic.edu/metador) ##### By Nitin Bhardwaj (Dr Hui Lu's Lab at the Univ of Illinois at Chicago) ##### As of May 2007 ###################################################### ###################################################### ##### README ##### First column contains the name of the host-protein ##### Second column contains the species name. 'Human', 'Yeast' and ##### 'Mouse' Have been indicated and others have been indicated by 'Others' ##### Third column indicates membrane-binding (indicated by 1) or ##### non-membrane-binding (indicated by 0) behavior of the protein. ##### Fourth and fifth columns state the function and subcellular location ##### of the protein as given in the Swiss-Prot/Uniprot database, respectively (wherever available). ##### Sixth and subsequent columns provide the sequences of all occurrence of ##### the domain in the host protein. ###################################################### DOC2B_HUMAN Human 1 " FUNCTION: May be involved in constitutive membrane trafficking including dynein-dependent intracellular vesicle transport. In vitro, binds calcium and phospholipids (By similarity)." SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). GTLDFSLLYDQENNALHCTITKAKGLKPMDHNGLADPYVKLHLLPGASKANKLRTKTLRNTLNPTWNETLTYYGITDEDMIRKTLRISVCDEDKFRHNEFIGETR DOC2B_MOUSE Mouse 1 " FUNCTION: May be involved in constitutive membrane trafficking including dynein-dependent intracellular vesicle transport. In vitro, binds calcium and phospholipids." SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). GTLDFSLLYDQENNALHCTISKAKGLKPMDHNGLADPYVKLHLLPGASKANKLRTKTLRNTLNPSWNETLTYYGITDEDMVRKTLRISVCDEDKFRHNEFIGETR GRLSVRCHYEAAEQRLAVEVLHAADLLPLDANGLSDPFVIVELGPPHLFPLVRSQRTQVKTRTLHPVYDELFYFSVPAEACRRRAACVLFTVMDHDWLSTNDFAGEAA DOC2B_RAT Others 1 " FUNCTION: May be involved in constitutive membrane trafficking including dynein-dependent intracellular vesicle transport. In vitro, binds calcium and phospholipids (By similarity)." SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. GTLDFSLLYDQENNALHCTISKAKGLKPMDHNGLADPYVKLHLLPGASKANKLRTKTLRNTLNPSWNETLTYYGITDEDMIRKTLRISVCDEDKFRHNEFIGETR GRLTVRCHYEAAEQRLAVEVLHAADLLPLDANGLSDPFVIVELGPPHLFPLVRSQRTQVKARTLHPVYDELFHFSVPAEACRRRGACVLFTVMDHDWLSTNDFAGEAA KPC1B_CAEEL Others 1 " FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. Associated with membranes and the cytoskeleton. MLFTGTVRVRVLEARQLRPTEWSRRFRQDEAATAAIDSYVNVDWDEYHIGKTQVRPKTNEPRWNEEFTASGVHQGKAIGFSVFHSCVMPPDDFVANTR KPC2_APLCA Others 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters (By similarity)." SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. MSRRAKMVFNGSVKIKVCEAVDLKPTDFSLRLQKGSTKEKASQMIEPYVNIDVDEVYIAKTTTKPKSVKPQWVWNEDFTSEVHNGQNVNLTVFHDAAIPPDEFVANCT KPCB_BOVIN Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). LIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLS VEARNLDKKDFLGKSDPFLEFFRQGDGKWHLVYRSEVIKNNLNPTWKRFSVPVQHFCGGNPSTPIQVQCSDYDSDGSHDLIGTFH KPCB_HUMAN Human 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). LIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLS VEARNLDKKDFLGKSDPFLEFFRQGDGKWQLAYRTEVVKNNLNPTWKRFSVSLQHFCGGDLSTPIQVRCSDYDSDGSHDLIGTFH KPCB_MOUSE Mouse 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). LIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLS KGLITIAAQELSDNRVITLSLAGRRLDKKDLFGKSDPFLEFYKPGDDGKWMLVHRTEVIKYTLDPVWKPFTVPLVSLCDGDMEKPIQVMCYDYDNDGGHDFIGEFQ KPCB_RABIT Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). LIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLS KGVITIAAQELSDNRVITLSLAGRKLDKKDLFGKSDPFLEFYKPGDDGKWMLVHRTEVIKYTLDPVWKPFTVPLVSLCDGDLEKPIQVMCYDYDSNGGHDFIGEFQ KPCB_RAT Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May be considered as a novel component of the NF-kappa-B signaling axis responsible for the survival and activation of B-cells after BCR cross-linking." SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. LIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLS KGSITISAEEIKDNRVVLFEMEARKLDNKDLFGKSDPYLEFHKQTSDGNWLMVHRTEVVKNNLNPVWRPFKISLNSLCYGDMDKTIKVECYDYDNDGSHDLIGTFQ PLCB3_HUMAN Human 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. DPFTEVIVDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGKFVGHRI KGSITISAEEIKDNRVVLFEMEARKLDNKDLFGKSDPYLEFHKQTSDGHWLMVHRTEVIKNNLNPMWKPFKISLNSLCYGDMDKTIKVECYDYDNDGSHDLIGTFQ PLDB1_ARATH Mouse 1 " FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Can use phosphatidylserine or N-acylphosphatidylethanolamine as substrates." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). LFGKGSLKVLLSHGNLDIWIYHAKNLPNMDMFHKTLGDMFGRLPGKIEGQLTSKITSDPYVSVSVAGAVIGRTYVMSNSENPVWMQHFYVPVAHHAAEVHFVVKDSDVVGSQLIGLVT KGSITISAEEIKDNRVVLFEMEARKPDNKDLFGKSDPYLEFHKQTSDGNWLMVHRTEVVKNNLNPVWRPFKISLNSLCYGDMDKTIKVECYDYDNDGSHDLIGTFQ PLDB2_ARATH Mouse 1 " FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Can use phosphatidylserine or N-acylphosphatidylethanolamine as substrates." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). PFGKASLKVLLLHGNLDIWVSCANNLPNLDLFHKTLGVVFGGMTNMIEGQLSKKITSDPYVSISVAGAVIGRTYVISNSENPVWQQHFYVPVAHHAAEVHFVVKDSDAVGSQLIGIVT SSITVIAEELSGNDDYVELAFNARKLDDKDFFSKSDPFLEIFRMNDDATQQLVHRTEVVMNNLSPAWKSFKVSVNSLCSGDPDRRLKCIVWDWDSNGKHDFIGEFT PLDD1_ARATH Mouse 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. May be involved in phosphatidic acid accumulation in the dehydration stress response and in the transduction of hormonal and environmental signals to the microtubules cytoskeleton. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. Colocalization with cortical microtubules also occurs. DMFSEHLRRLFTACNACARPTDTDDVDPRDKGEFGDKNIRSHRKVITSDPYVTVVVPQATLARTRVLKNSQEPLWDEKFNISIAHPFAYLEFQVKDDDVFGAQIIGTAK SSITVIAEELSGNDDYVELAFNARKLDDKDFFSKSDPFLEIFRMNDDATQQLVHRTEVVMNNLSPAWKSFKVSVNSLCSGDPDRRLKCIVWDWDSNGKHDFIGEFT PUB1_SCHPO Yeast 1 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Regulates ubiquitination of cdc25. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. Cytoplasm. ADGLYKRDVFRFPDPF KPMPAVSNGGVPGKKCGTIILSAEELSNCRDVATMQFCANKLDKKDFFGKSDPFLVFYRSNEDGTFTICHKTEVMKNTLNPVWQTFSIPVRALCNGDYDRTIKVEVYDWDRDGSHDFIGEFT RFIP2_HUMAN Human 1 " FUNCTION: A Rab11 effector protein acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Binds preferentially to phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA)." SUBCELLULAR LOCATION: Cell membrane; peripheral membrane protein. Endosome; recycling endosome; recycling endosomal membrane; peripheral membrane protein. Translocates with RAB11A from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. MMLSEQAQKWFPTHVQVTVLQAKDLKPKGKSGTNDTYTIIQLGKEKYSTSVAEKTLEPVWKEEASFELPGLLIQGSPEKYILFLIVMHRSLVGLDKFLGQVA KPMPAVSNGGVPGKKCGTIILSAEELSNCRDVATMQFCANKLDKKDFFGKSDPFLVFYRSNEDGTFTICHKTEVMKNTLNPVWQTFSIPVRALCNGDYDRTIKVEVYDWDRDGSHDFIGEFT RFIP5_HUMAN Human 1 FUNCTION: Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane. SUBCELLULAR LOCATION: Cytoplasm. Endosome; recycling endosome; recycling endosomal membrane; peripheral membrane protein. Mitochondrion; mitochondrial membrane; peripheral membrane protein. GAEPAAGPSRWLPTHVQVTVLRARGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTHGCPEWREECSFELPPGALDGLLRAQEADAGPAPWAASSAAACELVLTTMHRSLIGVDKFLGQAT STITIVAEEVSGTNDYVQLTFRAYKLDNKDLFSKSDPFMEIYKTNEDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDVHRPLKFLVYDYDSSGKHDFIGEFT RFIP5_MOUSE Mouse 1 FUNCTION: Rab effector involved in protein trafficking from apical recycling endosomes to the apical plasma membrane (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Endosome; recycling endosome; recycling endosomal membrane; peripheral membrane protein (By similarity). Mitochondrion; mitochondrial membrane; peripheral membrane protein (By similarity). DPEPAAGSSRWLPTHVQVTVLRASGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTQGCPEWCEECSFELPPGALDGLLRAQEADAGPAPWASGPNAACELVLTTMHRSLIGVDKFLGRAT STITIVAEEVSGTNDYVQLTFRAHKLDNKDLFSKSDPFMEIYKTNGDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDIHRPLKFLVYDYDSSGKHDFIGEFT RIMS1_RAT Others 1 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short- term synaptic plasticity (By similarity). SUBCELLULAR LOCATION: Cell membrane; peripheral membrane protein. Associated with plasma membranes from synaptic junctions. Not detected in synaptic vesicles. Detected in presynaptic nerve terminals close to the active zone. Detected in synaptic ribbons of ribbon synapses of retinal photoreceptor cells. GQLSVKLWYDKVGHQLIVNVLQATDLPPRVDGRPRNPYVKMYFLPDRSDKSKRRTKTVKKLLEPKWNQTFVYSHVHRRDFRERMLEITVWDQPRVQDEESEFLGEIL STITIVAEEVSGTNDYVQLTFRAYKLDNKDPFSKSDPFMEIYKTNEDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDVHRPLKFLVYDYDSSGKHDFIGEFT SYTL1_HUMAN Human 1 " FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking (By similarity). Binds phosphatidylinositol 3,4,5-triphosphate." SUBCELLULAR LOCATION: Cell membrane; peripheral membrane protein; cytoplasmic side. Peripheral membrane protein tightly bound to the cytoplasmic side of cellular membranes. GSVHFALHYEPGAAELRVHVIQCQGLAAARRRRSDPYVKSYLLPDKQSKRKTAVKKRNLNPVFNETLRYSVPQAELQGRVLSLSVWHRESLGRNIFLGEVE RARKLDDKDLFSKSDPFLELYRVNDDQGLQLVYRTEVVKNNLNPVWEAFKVSLSSLCSCEETRPLKCLVWDYDSRGKHDFIGEFS SYTL1_MOUSE Mouse 1 " FUNCTION: Binds phosphatidylinositol 3,4,5-triphosphate (By similarity). May act as Rab effector protein and play a role in vesicle trafficking." SUBCELLULAR LOCATION: Cytoplasmic; peripheral membrane protein. GSVLFSLHYEPGTSELRVQVIQCQGLAAARRRRSDPYVKSYLLPDKQSKRKTSVKKRNLNPIFNETLRHSVQQADLPGRVLSLSVWHRESLGRNIFLGEVE GTIILTAEELNCCRDAVLMQFCANKLDKKDFFGKSDPFLVFYRSNEDGSFTICHKTEVVKNTLNPVWQAFKISVRALCNGDYDRTIKVEVYDWDRDGSHDFIGEFT SYTL2_HUMAN Human 1 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking (By similarity). SUBCELLULAR LOCATION: Cytoplasmic; peripheral membrane protein. Bound to melanosomes (By similarity). FVAQCKDLAAADVKKQRSDPYVKAYLLPDKGKMGKKKTLVVKKTLNPVYNEILRYKIEKQILKTQKLNLSIWHRDTFKRNSFLGEVELDLETWDWDNKQNKQLRW GTIILTAEELNCCRDAVLMQFCANKLDKKDFFGKSDPFLVFYRSNEDGSFTICHKTEVVKNTLNPVWQAFKISVRALCNGDYDRTIKVEVYDWDRDGSHDFIGEFT SYTL2_MOUSE Mouse 1 FUNCTION: May act as Rab effector protein and play a role in melanosome transport and vesicle trafficking. Isoform 1 controls melanosome distribution in the cell periphery and regulates melanocyte morphology. SUBCELLULAR LOCATION: Cytoplasmic; peripheral membrane protein. Bound to melanosomes. Isoform 1 is localized mainly on peripheral melanomes but not on less mature melanosomes around the nucleus. GSVQFALDYVESLKELHVFVAQCKDLAAADVKKQRSDPYVKTYLLPDKGKMGKKKTLVVKKTLNPVYNEILRYKIERQFLKTQKLNLSVWHRDTFKRNSFLGEVE GRILLSLSYSSRRRGLLVGILRCAHLAAMDVNGYSDPYVKTYLRPDVDKKSKHKTCVKKKTLNPEFNEEFFYEIELSTLATKTLEVTVWDYDIGKSNDFIGGVS SYTL3_MOUSE Mouse 1 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids in the presence of calcium ions. SUBCELLULAR LOCATION: Cytoplasmic; peripheral membrane protein. GEIEFAIHYCVKSCSLEICIKTCKNLAYGEEKKRKCNPYVKTYLLPDRSSQGKRKTRVQKNTLDPTFEETLKYQVDPGQLMTRRLQVSVWHLGTLARRVFLGEVI GRILLSLSYSSRRHGLLVGIVRCAHLAAMDVNGYSDPYVKTYLRPDVDKKSKHKTCVKKKTLNPEFNEEFFYEIELSTLATKTLEVTVWDYDIGKSNDFIGGVS SYTL5_HUMAN Human 1 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). GEILLHISYCYKTGGLYIFVKNCRNLAIGDEKKQRTDAYVKSYLLPDKSRNNKRKTKIRTGTNPEFNETLKYTISHTQLETRTLQLSVWHYDRFGRNSFLGEVE GRILLSLSYSSRRHGLLVGIVRCAHLAAMDVNGYSDPYVKTYLRPDVDKKSKHKTCVKKKTLNPEFNEEFFYEMELSTLATKTLEVTVWDYDIGKSNDFIGGVS SYTL5_MOUSE Mouse 1 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). GEILLHISYCYKTGGLYIFVKSCRNLATGDEKKQRTDAYVKSYLLPDKSRNNKRKTKIRTGTNPEFNETLKYTISHTQLETRTLQLSVWHYDRFGRNSFLGEVE GRILISLKYSSQKQGLLVGIVRCAHLAAMDANGYSDPYVKTYLRPDVDKKSKHKTAVKKKTLNPEFNEEFCYEIKHGDLAKKSLEVTVWDYDIGKSNDFIGGVV SYTL5_RAT Others 1 FUNCTION: May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids (By similarity). SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). GEILLHISYCYKTGGLYIFVKNCRNLAIGDEKKQRTDAYVKSYLLPDKTRNNKRKTKIRTGTNPEFNETLKYTISHTQLETRTLQLSVWHYDRFGRNSFLGEVE GRILISLKYSSQKQGLLVGIVRCAHLAAMDANGYSDPYVKTYLKPDVDKKSKHKTAVKKKTLNPEFNEEFCYEIKHGDLAKKTLEVTVWDYDIGKSNDFIGGVV UN13A_HUMAN Human 1 FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity- depending refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses (By similarity). Involved in secretory granule priming in insulin secretion (By similarity). SUBCELLULAR LOCATION: Cell membrane; peripheral membrane protein (By similarity). Localized to the active zone of presynaptic density. Translocated to the plasma membrane as response to phorbol ester binding (By similarity). VKQSVLDGTSKWSAKISITVVCAQGLQAKDKTGSSDPYVTVQVGKTKKRTKTIYGNLNPVWEENFHFECHNSSDRIKVRVWDEDDDIKSRVKQRFKRESDDFLGQTI GRILISLKYSSQKQGLLVGIVRCAHLAAMDANGYSDPYVKTYLKPDVDKKSKHKTAVKKKTLNPEFNEEFCYEIKHGDLAKKTLEVTVWDYDIGKSNDFIGGVV UN13A_RAT Others 1 FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity- depending refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. Involved in secretory granule priming in insulin secretion (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Cell membrane. Localized to the active zone of presynaptic density. Translocated to the plasma membrane in response to phorbol ester binding. VKQSVLDGTSKWSAKISITVVCAQGLQAKDKTGSSDPYVTVQVGKTKKRTKTIYGNLNPVWEENFHFECHNSSDRIKVRVLDEDDDIKSRVKQRFKRESDDFLGQTI GRILLSLCYSSERGGLLVGVLRCVHLAPMDANGYSDPFVRLFLHPSSGKKSKYKTSVRRKTLNPEFNEEFFYAGHREELAQKALLVSVWDYDLGTADDFIGGVQ UN13B_HUMAN Human 1 FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity- depending refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in a subset of excitatory/glutamatergic but not inhibitory/GABA-mediated synapses (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). Cell membrane (By similarity). Localized to synapses. Translocated to the plasma membrane in response to phorbol ester binding (By similarity). VKQSVLDGTSKWSAKITITVVCAQGLQAKDKTGSSDPYVTVQVSKTKKRTKTIFGNLNPVWEEKFHFECHNSSDRIKVRVWDEDDDIKSRVKQRLKRESDDFLGQTI PTSRKLLSDKPQDFQIRVQVIEGRQLPGVNIKPVVKVTAAGQTKRTRIHKGNSPLFNETLFFNLFDSPGELFDEPIFITVVDSRSLRTDALLGEFR SNLLRPTGVALRGAHFCLKVFRAEDLPQMDDAVMDNVKQIFGFESNKKNLVDPFVEVSFAGKMLCSKILEKTANPQWNQNITLPAMFPSMCEKMRIRIIDWDRLTHNDIVATTY RPTISCIFDYGNRYHLRCYMYQARDLAAMDKDSFSDPYAIVSFLHQSQKTVVVKNTLNPTWDQTLIFYEIEIFGEPATVAEQPPSIVVELYDHDTYGADEFMGRCI RQFHQLAAQGPQECLVRIYIVRAFGLQPKDPNGKCDPYIKISIGKKSVSDQDNYIPCTLEPVFGKMFELTCTLPLEKDLKITLYDYDLLSKDEKIGETV UN13B_MOUSE Mouse 1 FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity- depending refilling of readily releasable vesicle pool (RRP) (By similarity). Essential for synaptic vesicle maturation in a subset of excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Golgi apparatus. Localized to synapses (By similarity). Translocates to the Golgi in response to phorbol ester binding. VKQSVLDGTSKWSAKITITVVCAQGLQAKDKTGSSDPYVTVQVGKTKKRTKTIFGNLNPVWEEKFHFECHNSSDRIKVRVWDEDDDIKSRVKQRLKRESDDFLGQTI APPRKLLSDKPQDFQIRVQVIEGRQLPGVNIKPVVKVTAAGQTKRTRIQKGNSPLFNETLFFNVFDSPLELFDEPIFITVVDSRSLRTDALLGEFR GNLLRPTGVALRGAHFCLKVFRAEDLPQMDDAVMDNVKQIFGFDSNKKNLVDPFVEVSSAGKMLCSKILEKTANPQWNQNITLPAMFPSMCEKMRIRVMDWDRLTHNDTVATTYLGMSK RPTISCIFDYGNRYHLRCYLYQARDLPAMDKDSFSDPYSIVSFLHQSQKTVVEKNTLNPTWDQTLIFYEIEIFGEPASIAEHPPCIVVELYDHDTYGADEFMGRCI RQFHQLAAQGPQECLVRIYIVRAFGLQPKDPNGKCDPYIKISIGKKSVSDQDNYIPCTLEPVFGKMFELTCTLPLEKDLKITLYDYDLLSKDEKIGETV UN13B_RAT Others 1 " FUNCTION: Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity- depending refilling of readily releasable vesicle pool (RRP), Essential for synaptic vesicle maturation in a subset of excitatory/glutamatergic but not inhibitory/GABA-mediated synapses (By similarity)." SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Cell membrane. Localized to synapses. Translocated to the plasma membrane in response to phorbol ester binding. VKQSVLDGTSKWSAKITITVVCAQGLQAKDKTGSSDPYVTVQVGKTKKRTKTIFGNLNPVWEEKFHFECHNSSDRIKVRVWDEDDDIKSRVKQRLKRESDDFLGQTI UN13C_HUMAN Human 1 FUNCTION: Probably plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Probably is involved in neurotransmitter release. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). Localized to presynaptic structures (By similarity). AKQSVLDGTSKWSAKITITVVSAQGLQAKDKTGSSDPYVTVQVGKNKRRTKTIFGNLNPVWDEKFYFECHNSTDRIKVRVWDEDDDIKSRVKQHFKKESDDFLGQTI UN13C_MOUSE Mouse 1 FUNCTION: Probably plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Probably is involved in neurotransmitter release. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). Localized to presynaptic structures (By similarity). AKQSVLDGTSKWSAKITITVVSAQGLQAKDKTGSSDPYVTVQVGKNKRRTKTIFGNLNPVWDEKFFFECHNSTDRIKVRVWDEDDDIKSRVKQHFKKESDDFLGQTI NWGVSSRPDPPSAAILVVYLDRAQDLPLKKGNKEPNPMVQLSIQDVTQESKAVYSTNCPVWEEAFRFFLQDPQSQELDVQVKDDSRALTLGALT PCHTTPDSQFGTEHVLRIHVLEAQDLIAKDRFLGGLVKGKSDPYVKLKLAGRSFRSHVVREDLNPRWNEVFEVIVTSVPGQELEVEVFDKDLDKDDFLGRCK SLIQTQKSAELAAALLSIYMERAEDLPLRKGTKHLSPYATLTVGDSSHKTKTISQTSAPVWDESASFLIRKPHTESLELQVRGEGTGVLGSLS LGQVKLTLWYYSEERKLVSIVHGCRSLRQNGRDPPDPYVSLLLLPDKNRGTKRRTSQKKRTLSPEFNERFEWELPLDEAQRRKLDVSVKSNSSFMSRERELLGKVQ UN13D_HUMAN Human 1 FUNCTION: Seems to play a role in vesicle maturation during exocytosis. Is involved in regulation of cytolytic granules secretion. SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Colocalizes with cytotoxic granules at the plasma membrane. QTLQRVRELEKPIFCLKATVKQAKGILGKDVSGFSDPYCLLGIEQGVGVPGGSPGSRHRQKAVVRHTIPEEETHRTQVITQTLNPVWDETFILEFEDITNASFHLDMWDLDTVESVRQKLGELT NRGITSRPEPPSAAILVVYLDRAQDLPLKKGNKEPNPMVQLSVQDVTRESKATYSTNSPVWEEAFRFFLQDPRSQELDVQVKDDSRALTLGALT PYHTTPNSHFGTENVLRIHVLEAQDLIAKDRFLGGLVKGKSDPYVKLKVAGKSFRTHVVREDLNPRWNEVFEVIVTSIPGQELEIEVFDKDLDKDDFLGRYK SLIQTQKSSELAAALLSVFLERAEDLPLRKGTKPPSPYATITVGETSHKTKTVSQSSAPVWEESASFLIRKPHAESLELQVRGEGTGTLGSVS DSPSEAPVGPLGQVKLTVWYHSDEQKLISIIHSCRALRQNGRDLPDPYVSVLLLPDKNRSTKRKTPQKKRTLNPEFNERFEWDLPLDGTLRRKLDVSVKSNSSFMSRERELLGKVQ UN13D_RAT Others 1 FUNCTION: Seems to play a role in vesicle maturation during exocytosis. Is involved in regulation of cytolytic granules secretion (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). Colocalizes with cytotoxic granules at the plasma membrane (By similarity). QMLQRVRELEKPIFCLKATVKQAKGILGKDVSGFSDPYCLLGIEQKVGVPEGSPVSRRRQKAVVRHTIPEEETHRTQVKTQTLNPVWDETFILEFEDITNASFHLDMWDLDTVESVRHKLGELT NQGVSSRPEPPSAAILVVYLDRAQDLPLKKGNKEPNPMVQLSIQDVTQESKAVYSTNCPVWEEAFRFFLQDPQSQELDVQVKDDSRALTLGALT PCHTTPDSQFGTEHVLRIHVLEAQDLIAKDRFLGGLVKGKSDPYVKLKLAGRSFRSHVVREDLNPRWNEVFEVIVTSVPGQELEVEVFDKDLDKDDFLGRCK SLIQTQKSAELAAALLSIYMERAEDLPLRKGTKHPSPYATLTVGDTSHKTKTVSQTSAPVWDESASFLIRKPHTENLELQVRGEGTGVLGSLS LGQVKLTVWYYSEERKLVSIVHGCRALRQNGRDPPDPYVSLLLLPDKNRGTKRKTSQKKRTLSPEFNERFEWELPLDEAQRRKLDVSVKSNPSFMSRERELLGKVQ KPCD_CANFA Others 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May play a role in antigen-dependent control of B-cell function (By similarity)." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). MAPFLRIAFTSYELGSLQAADEASQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPMSEVTVGVSV NRGITSRPEPPSAAILVVYLDRAQDLPLKKGNKEPNPMVQLSVQDVTQESKATYSTNCPVWEEAFRFFLQDPRSQELDVQVKDDSRALTLGALT PYHTTPNSHFGTENVLRIHVLEAQDLIAKDRFLGGLVKGKSDPYVKLKVAGRSLRTHVVREDLNPRWNEVFEVIVTSIPGQELDIEVFDKDLDKDDFLGRYK SLIQTQKSSELAAALLSVYLERSEDLPLRKGTKPPSPYAILTVGETSHKTKTVSQTSAPIWEESASFLIRKPHAESLELQVRGEGTGTLGSIS LGQVKLTVWYHSDEQKLISIIHSCRALRQNGRDLPDPYVSVLLLPDKNRGTKRKTSQKKRTLNPEFNERFEWDLPLDGTLRRKLDVSVKSNSSFMSRERELLGKVQ KPCD_HUMAN Human 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May play a role in antigen-dependent control of B-cell function." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSV LVRVYIIEANGLISNARKGRVDSYVKLHCGKQNVNLKKNYRSECCDPIFGERVDMTVTIPLEKDLKITVMGKRRILSDQEIGSTTIDLENRLLTKWRATG KPCD_MOUSE Mouse 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May play a role in antigen-dependent control of B-cell function." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). MAPFLRISFNSYELGSLQVEDEASQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKTTFDAHIYEGRVIQIVLMRAAEDPVSEVTVGVSV VTIKVPACVDLAKKQGTCDPFVVCTAHYSNKHQVTRRTKQRKKTVDPEFDEAMYFDLHIDADAGSTNTTGSNKSAGSLESSANKGYSIYPVGGADLVEIVVSVWHDAHGAMSDKVFLGEVR KPCD_RAT Others 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters. May play a role in antigen-dependent control of B-cell function. Truncated isoform 2 is inactive." SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. MAPFLRISFNSYELGSLQAEDDASQPFCAVKMKEALTTDRGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEDPMSEVTVGVSV P3C2G_HUMAN Human 1 " FUNCTION: In vitro, phosphorylates PtdIns and PtdIns4P but not PtdIns(4,5)P2 (By similarity)." SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). KLTILVKHMKNIHLPDGSAPSAHVEFYLLPYPSEVLRRKTKSVPKCTDPTYNEIVVYDEVTELQGHVLMLIVKSKTVFVGAINIRLCSVPLDKEKWYP P3C2G_MOUSE Mouse 1 " FUNCTION: In vitro, phosphorylates PtdIns and PtdIns4P but not PtdIns(4,5)P2." SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. RLTILVKHLKNIHLPDGSVPSAHVEIYLLPHPSEVRRKKTKCVPKCTDPTYNEIVVYDEVLGLQGHVLMLIVKSKTVFVGAVNIQLCSVPLNEEKWYP P3C2G_RAT Others 1 " FUNCTION: In vitro, phosphorylates PtdIns and PtdIns4P but not PtdIns(4,5)P2." SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By similarity). KLTILVKHLKNIHLPDGSAPSAHVEIYLLPHPSEVRRKKTKCVPKCTDPTYNEIVVYDDVSGLQGHVLMLIVKSKTVFVGAVNIQLCSVPLNEEKWYP PLDA1_BRAOC Others 1 " FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). MAQHLLHGTLHATIYEVDDLHTGGLRSGFFGKILANVEETIGVGKGETQLYATIDLQRARVGRTRKIKDEAKNPKWYESFHIYCAHLASDIIFTVKDDNPIGATLIGRAY PLDA1_RICCO Others 1 " FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). Vacuole. Endoplasmic reticulum. Plastid. Cell membrane. MAQISLHGTLHVTIYEVDKLHSGGGPHFFRKLVENIEETVGFGKGVSKLYATIDLEKARVGRTRILENEQSNPRWYESFHVYCAHQASNVIFTVKDDNPIGATLIGRAY PLDA2_BRAOC Others 1 " FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). MAQHLLHGTLHATIYEVDALHTGGLRSAGFLGKIISNVEETIGFGKGETQLYATIDLQKARVGRTRKITDEPKNPKWYESFHIYCAHMASDIIFTVKDDNPIGATLIGRAY PLDE1_ARATH Mouse 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). TLEITIFDATPFSPPFPFNCICTKPKAAYVTIKINKKKVAKTSSEYDRIWNQTFQILCAHPVTDTTITITLKTRCSVLGRFRISAEQILTSNSAVIN PLDZ1_ARATH Mouse 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; peripheral membrane protein (By similarity). MTEQLLLHGTLEVKIYRIDKLHQRSRFNLCGKGNKEPTGKKTQSQIKRLTDSCTSLFGGHLYATIDLDRSRVARTMMRRHPKWLQSFHVYTAHSISKIIFTVKEDEPVSASLIGRAY PUB2_SCHPO Yeast 1 FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Has a role in the G2/M transition. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. Cytoplasm. Predominantly found at the cell surface of the polar regions. VQLTILHVEGLWKNGLLRSLKPYLLISVDDDQFIKTNVASGTLRLSWGFTQKLTVSPQSIILLQLFDEKQKNETSDGFVGLGA SYGP1_RAT Others 1 FUNCTION: Inhibitory regulator of the Ras-cAMP pathway. Member of the NMDAR signaling complex in excitatory synapses it may play a role in NMDAR-dependent control of AMPAR potentiation and synaptic plasticity. SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. Mostly in excitatory glutamatergic synapses. LKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRSASGDTVFWGEHFEFNNLPAVRALRLHLYRDSDKKRKKDKAGYVG CPNE1_HUMAN Human 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties. MAHCVTLVQLSISCDHLIDKDIGSKSDPLCVLLQDVGGGSWAELGRTERVRNCSSPEFSKTLQLEYRFETVQKLRFGIYDIDNKTPELRDDDFLGGAE CPNE1_MOUSE Mouse 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties. MAHCVTLVQLSVSCEHLIDKDIGSKSDPLCVLLQDVGGAWAELCRTERVRNCSSPEFSKTLQIEYHFETVQKLRFGIYDIDNKTPELGDDDFLGGAE CPNE3_HUMAN Human 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). Seems to have a protein kinase activity. MAAQCVTKVALNVSCANLLDKDIGSKSDPLCVLFLNTSGQQWYEVERTERIKNCLNPQFSKTFIIDYYFEVVQKLKFGVYDIDNKTIELSDDDFLGECE CPNE3_MOUSE Mouse 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). MAAQCVTKVELNVSCNNLLDADVTSKSDPLCVLFLNTSGHQWYEVERTERIKNSLNPKFSKTFVIDYYFEVVQKLKFGIYDIDNKTIELSDDDFLGECE CPNE3_PONPY Others 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). MAAQCVTKVALNVSCANLLDKDIGSKSDPLCVLFLNTSGQQWYEVERTERIKNCLNPQFSKTFIIDYYFEVVQKLKFGVYDIDNKTIELSDDDFLGECE CPNE4_HUMAN Human 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). TKVELRVACKGISDRDALSKPDPCVILKMQSHGQWFEVDRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDISSNHNGLKEADFLGGMECTLGQIVSQRKLSKS CPNE4_MOUSE Mouse 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). TKVELRVACKGISDRDALSKPDPCVILKMQSHGQWFEVDRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDISSNHNGLKEADFLGGMECTLGQIVSQRKLSKS CPNE5_HUMAN Human 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). VSCRNLLDKDMFSKSDPLCVMYTQGMENKQWREFGRTEVIDNTLNPDFVRKFIVDYFFEEKQNLRFDLYDVDSKSPDLSKHDFLGQAF CPNE5_MOUSE Mouse 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). SLSEFDSLAGSIPATKVEITVSCRNLLDKDMFSKSDPLCVMYTQGMENKQWREFGRTEVIDNTLNPDFVRKFIVDYFFEEKQNLRFDLYDVDSKSPDLSKHDFLGQAF CPNE6_HUMAN Human 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties. May have a role in synaptic plasticity (By similarity). LRVSCHGLLDRDTLTKPHPCVLLKLYSDEQWVEVERTEVLRSCSSPVFSRVLALEYFFEEKQPLQFHVFDAEDGATSPRNDTFLGSTE CPNE6_MOUSE Mouse 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). May have a role in synaptic plasticity. LRVSCHGLLDRDTLTKPHPCVLLKLYSDEQWVEVERTEVLRSCSSPVFSRVLAIEYFFEEKQPLQFHVFDAEDGATSPSSDTFLGSTE CPNE6_PONPY Others 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties. May have a role in synaptic plasticity (By similarity). LRVSCHGLLDRDTLTKPHPCVLLKLYSDEQWVEVERTEVLRSCSSPVFSRVLALEYFFEEKQPLQFHVFDAEDGATSPRNDTFLGSTE CPNE7_HUMAN Human 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). LSCRHLLDRDPLTKSDPSVALLQQAQGQWVQVGRTEVVRSSLHPVFSKVFTVDYYFEEVQRLRFEVYDTHGPSGFSCQEDDFLGGME CPNE8_HUMAN Human 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). GIGDLNQLSAAIPATRVEVSVSCRNLLDRDTFSKSDPICVLYVQGVGNKEWREFGRTEVIDNTLNPDFVRKFILDYFFEERENLRFDLYDVDSKSPNLSKHDFLGQVF CPNE8_MOUSE Mouse 1 FUNCTION: May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties (By similarity). GIGDLNQLSAAIPATRVEVSVSCRNLLDRDTFSKSDPICVLYTQAVGNKEWREFGRTEVIDNTLNPDFVRKFILDYFFEERENLRFDLYDVDSKSPNLSKHDFLGQVF DOC2A_HUMAN Human 1 " FUNCTION: May be involved in calcium dependent neurotransmitter release through the interaction with UNC13A. May be involved in dynein-dependent intracellular vesicle transport. In vitro, binds calcium and phospholipids." SUBCELLULAR LOCATION: Membrane-associated (Probable). Colocalizes to synaptic vesicles. GTLEFDLLYDRASCTLHCSILRAKGLKPMDFNGLADPYVKLHLLPGACKANKLKTKTQRNTLNPVWNEDLTYSGITDDDITHKVLRIAVCDEDKLSHNEFIGEIR DOC2A_MOUSE Mouse 1 " FUNCTION: May be involved in calcium dependent neurotransmitter release through the interaction with UNC13A. May be involved in dynein-dependent intracellular vesicle transport. In vitro, binds calcium and phospholipids." SUBCELLULAR LOCATION: Membrane-associated. Colocalizes to synaptic vesicles (By similarity). GTLEFDLLYDQASCMLHCRILRAKGLKPMDFNGLADPYVKLHLLPGACKANKLKTKTQRNTLNPVWNEELTYSGITDDDITHKVLRISVCDEDKLSHNEFIGEIR DOC2A_RAT Others 1 " FUNCTION: May be involved in calcium dependent neurotransmitter release through the interaction with UNC13A. May be involved in dynein-dependent intracellular vesicle transport. In vitro, binds calcium and phospholipids." SUBCELLULAR LOCATION: Membrane-associated. Colocalizes to synaptic vesicles (By similarity). GTLEFDLLYDQASCMLHCRILRAKGLKPMDFNGLADPYVKLHLLPGACKANKLKTKTQRNTLNPVWNEELTYSGITDDDITHKVLRISVCDEDKLSHNEFIGEIR ERG1_ORYSA Others 1 FUNCTION: May play a role in plant defense signaling. Isoform 2 binds to phospholipids in a Ca(2+)-dependent manner in response to pathogen elicitors. SUBCELLULAR LOCATION: Cytoplasmic. Partially translocated to plasma membrane upon elicitor treatment. MAGSGVLEVHLVDAKGLTGNDFLGEIGKIDPYVVVQYRSQERKSSVARDQGKNPSWNEVFKFQINSTAATGQHKLFLRLMDHDTFSRDDFLGEAT ITSN1_HUMAN Human 1 FUNCTION: Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. Isoform 1 could be involved in brain-specific synaptic vesicle recycling. SUBCELLULAR LOCATION: Cytoplasmic; membrane-associated protein. Enriched in synaptosomes (By similarity). KAYLVRSQRATGIGRLMVNVVEGIELKPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTE ITSN1_MOUSE Mouse 1 FUNCTION: Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. SUBCELLULAR LOCATION: Cytoplasmic; membrane-associated protein. Enriched in synaptosomes (By similarity). KAYLVRSQRATGIGRLMVNVVEGIELKPCRSHGKSNPYCEVTMGSQCHITKTIQDTLNPKWNSNCQFFIRDLEQEVLCITVFERDQFSPDDFLGRTE ITSN2_HUMAN Human 1 FUNCTION: Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. SUBCELLULAR LOCATION: Cytoplasm. KAYQARSQKTSGIGRLMVHVIEATELKACKPNGKSNPYCEISMGSQSYTTRTIQDTLNPKWNFNCQFFIKDLYQDVLCLTLFDRDQFSPDDFLGRTE ITSN2_MOUSE Mouse 1 FUNCTION: Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. SUBCELLULAR LOCATION: Cytoplasm (By similarity). KAYQARSQKTSGIGRLMVHVIEATELKACKPNGKSNPYCEVSMGSQSYTTRTLQDTLNPKWNFNCQFFIKDLYQDVLCLTMFDRDQFSPDDFLGRTE KPC1_APLCA Others 1 " FUNCTION: This is calcium-dependent, phospholipid-dependent, serine- and threonine-specific enzyme. Activation of PKC by serotonin results in presynaptic facilitation of depressed sensory-to-motor neuron synapses, which is thought to underlie behavioral dishabituation. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters (By similarity)." SUBCELLULAR LOCATION: Cytoplasmic; translocated to neuronal membranes. VLVEILEAKNLCPMDPNGLADPYVKVKLIPYDAHKLKLKTKTIKASLNPVWNESFTVDIGPEDNSKRLSLEVWDWDRTSRNDFMGSLS KPC1_DROME Others 1 " FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." LTVQIKEGRNLIPMDPNGLSDPYVKVKLIPDDKDQSKKKTRTIKACLNPVWNETLTYDLKPEDKDRRILIEVWDWDRTSRNDFMGALS KNSRRMLSNKPQDFQIRVRVIEGRQLSGNNIRPVVKVHVCGQTHRTRIKRGNNPFFDELFFYNVNMTPSELMDEIISIRVYNSHSLRADCLMGEFK SNLLLPAGIALRWVTFLLKIYRAEDIPQMDDAFSQTVKEIFGGNADKKNLVDPFVEVSFAGKKVCTNIIEKNANPEWNQVVNLQIKFPSVCEKIKLTIYDWDRLTKNDVVGTTY TPIVSCNFDRVYIYHLRCYVYQARNLLALDKDSFSDPYAHICFLHRSKTTEIIHSTLNPTWDQTIIFDEVEIYGEPQTVLQNPPKVIMELFDNDQVGKDEFLGRSI PPRQFRELPDSVPQECTVRIYIVRGLELQPQDNNGLCDPYIKITLGKKVIEDRDHYIPNTLNPVFGRMYELSCYLPQEKDLKISVYDYDTFTRDEKVGETI KPC1_LYTPI Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme (By similarity). FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters (By similarity)." LQVTVAEAKNLIPMDPNGLSDPFVKLKLIPDQKRETKKKTRTIKGSLNPTWGESFDFNLEDTDRNRRLLVEVWDWDRATRNDFMGALS KPC2_CAEEL Others 1 " FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." KRGRLRIEAHIENDQLTIKILEAKNLIPMDPNGLSDPYVKCKLIPEDSGCKSKQKTKTLRATLNPQWNETFTYKLLPGDKDRRLSIEVWDWDRTSRNDFMGSLS KPC2_DROME Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. This isozyme is a negative regulator of the visual transduction cascade and has been shown to be required for photoreceptor cell inactivation and light adaptation. Negative regulation is dependent on interaction with scaffolding protein inaD." NNLKVDIKEAANLIPMDTNGFSDPYIAVQMHPDRSGRTKKKTKTIQKNLNPVFNETFTFELQPQDRDKRLLIEVWDWDRTSRNDFMGSFS KPCA_BOVIN Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. May play a role in cell motility by phosphorylating CSPG4 (By similarity). FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." KLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPRWDESFTFKLKPSDKDRRLSEEIWDWDRTTRNDFMGSLS KPCA_HUMAN Human 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. May play a role in cell motility by phosphorylating CSPG4. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." KLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLS KPCA_MOUSE Mouse 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. May play a role in cell motility by phosphorylating CSPG4 (By similarity). FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." KLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSNLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLS KPCA_RABIT Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. May play a role in cell motility by phosphorylating CSPG4 (By similarity). FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." KLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLS KPCA_RAT Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. May play a role in cell motility by phosphorylating CSPG4 (By similarity). FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." KLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLS LLLPEGVPPERQWARFYVKIYRAEGLPRMNTSLMANVKKAFIGENKDLVDPYVQVFFAGQKGKTSVQKSSYEPLWNEQVVFTDLFPPLCKRMKVQIRDSDKVNDVAIGTHF FPPVSLVYTKKQAFQLRAHMYQARSLFAADSSGLSDPFARVFFINQSQCTEVLNETLCPTWDQMLVFDNLELYGEAHELRDDPPIIVIEIYDQDSMGKADFMGRTF GMFQGIPSNDPINVLVRVYVVRATDLHPADINGKADPYIAIRLGKTDIRDKENYISKQLNPVFGKSFDIEASFPMESMLTVAVYDWDLVGTDDLIGETK KPCE_HUMAN Human 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCT LLLPEGVPPERQWARFYVKIYRAEGLPRMNTSLMANVKKAFIGENKDLVDPYVQVFFAGQKGKTSVQKSSYEPLWNEQVVFTDLFPPLCKRMKVQIRDSDKVNDVAIGTHF FPPISLVYTKKQAFQLRAHMYQARSLFAADSSGLSDPFARVFFINQSQCTEVLNETLCPTWDQMLVFDNLELYGEAHELRDDPPIIVIEIYDQDSMGKADFMGRTF GMFQGIPSNDPINVLVRIYVVRATDLHPADINGKADPYIAIKLGKTDIRDKENYISKQLNPVFGKSFDIEASFPMESMLTVAVYDWDLVGTDDLIGETK KPCE_MOUSE Mouse 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCT KPCE_RABIT Others 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCT KPCE_RAT Others 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCT KPCG_BOVIN Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." SDEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMS KPCG_HUMAN Human 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." ADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMS KPCG_MOUSE Mouse 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." SDEIHITVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTKTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMS KPCG_RABIT Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." SDEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMS KPCG_RAT Others 1 " FUNCTION: This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." SDEIHITVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTKTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMS KPCL_HUMAN Human 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." LRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDFVANCTLQFQELVGTTG KPCL_MOUSE Mouse 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." LRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCT KPCL_RAT Others 1 " FUNCTION: This is calcium-independent, phospholipid-dependent, serine- and threonine-specific enzyme. FUNCTION: PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters." LRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCTNVSDGGHLELAVFHETPLGYDHFVANCT QLIVEILQCRNITYKFKSPDHLPDLYVKLYVVNVSTQKRVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLVSNGGKFMKKTLIGEAY OTOF_HUMAN Human 1 FUNCTION: Might be involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. SUBCELLULAR LOCATION: Membrane; single-pass type II membrane protein (By similarity). DIKMEPSAGRPMDYQVSITVIEARQLVGLNMDPVVCVEVGDDKKYTSMKESTNCPYYNEYFVFDFHVSPDVMFDKIIKISVIHSKNLLRSGTLVGSFK IKIALKKEMKTDGEQLIVEILQCRNITYKFKSPDHLPDLYVKIYVMNISTQKKVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLFSNGGKFMKKTLIGEAC OTOF_MOUSE Mouse 1 FUNCTION: Might be involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. SUBCELLULAR LOCATION: Membrane; single-pass type II membrane protein (By similarity). DIKMEPSAGRPMDYQVSITVIEARQLVGLNMDPVVCVEVGDDKKYTSMKESTNCPYYNEYFVFDFHVSPDVMFDKIIKISVIHSKNLLRSGTLVGSFK LIVEILQCRNITYKFKSPDHLPDLYVKIYVINIATQKKVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLFSNGGKFMKKTLIGEAC P3C2A_HUMAN Human 1 " FUNCTION: Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2. May play a role in clathrin-coated endocytic vesicle formation and EGF signaling cascade. May be involved in mitosis and UV-induced damage response. May be a downstream effector in insulin signaling cascade." " SUBCELLULAR LOCATION: Ref.2, Ref.5: Cell membrane. Golgi apparatus. Clathrin-coated vesicles. Ref.4: Nuclear. Cytoplasm. Associated with RNA-containing structures. Ref.6, mainly: Cytoplasm." IGGAVKLSISYRNGTLFIMVMHIKDLVTEDGADPNPYVKTYLLPDNHKTSKRKTKISRKTRNPTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGVT QLIVEILQCRNITYKFKSPDHLPDLYVKLYVINISTQKKVIKKKTRVCRHDREPSFNETFRFSLSPAGHSLQILLFSNGGKFMKKTLIGEAC P3C2A_MOUSE Mouse 1 " FUNCTION: Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2. May play a role in clathrin-coated endocytic vesicle formation and EGF signaling cascade. May be involved in mitosis and UV-induced damage response (By similarity). May be a downstream effector in insulin signaling cascade." GQIGGAVKLSVSYRNGTLFIMVMHIKDLVTEDGADPNPYVKTYLLPDTHKTSKRKTKISRKTRNPTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGG P3C2A_PONPY Others 1 " FUNCTION: Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2. May play a role in clathrin-coated endocytic vesicle formation and EGF signaling cascade. May be involved in mitosis and UV-induced damage response. May be a downstream effector in insulin signaling cascade (By similarity)." IGGAVKLSISYRNGTLFIMVMHTKDLVTEDGADPNPYVKTYLLPDNHKTSKRKTKISRKTRNPTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGVT P3C2B_HUMAN Human 1 " FUNCTION: Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns. Does not phosphorylate PtdIns(4,5)P2. May be involved in EGF and PDGF signaling cascades." " SUBCELLULAR LOCATION: Found mostly in the microsome, but also in the plasma membrane and cytosol. Nuclear in testis." NKLFIMVMHIRGLQLLQDGNDPDPYVKIYLLPDPQKTTKRKTKVARKTCNPTYNEMLVYDGIPKGDLQQRELQLSVLSEQGFWENVLLGEVN PA24A_BRARE Others 1 " FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response." SUBCELLULAR LOCATION: Cytoplasmic. Translocates to membrane vesicles in a calcium-dependent fashion (By similarity). MSNIIVEHQYSHRLKLTVVRAENVTKGAFGDLLDTPDPYVELSVPTTPESRKRTRHINNDINPKWNETFEFILDPNQSNVLEVTLMDANYVMDETLGTAK PA24A_CHICK Others 1 " FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response." SUBCELLULAR LOCATION: Cytoplasmic. Translocates to membrane vesicles in a calcium-dependent fashion (By similarity). DPYQHIVVEHQYSHVFTVTVRKATNVTKGAIGDMLDTPDPYVELFIPSAPDCRKRTKHFNNDVNPVWNETFEFILDPNQDNVLEVTLMDANYVMDETLGMAT PA24A_HORSE Others 1 " FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response." SUBCELLULAR LOCATION: Cytoplasmic. Translocates to membrane vesicles in a calcium-dependent fashion (By similarity). DPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISSTPDSRKRTRHFNNNINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTAT PA24A_HUMAN Human 1 " FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response." SUBCELLULAR LOCATION: Cytoplasmic. Translocates to membrane vesicles in a calcium-dependent fashion. DPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTAT PA24A_MOUSE Mouse 1 " FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response." SUBCELLULAR LOCATION: Cytoplasmic. Translocates to membrane vesicles in a calcium-dependent fashion. DPYQHIIVEHQYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTAT PA24A_RAT Others 1 " FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response." SUBCELLULAR LOCATION: Cytoplasmic. Translocates to membrane vesicles in a calcium-dependent fashion (By similarity). DPYQHIIVEHQYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTAT PIP1_DROME Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." DPFAESTVDGIIAGTVSITVLSGQFLTDKRANTFVEVDMYGLPADTVRKKFRTKTVRDNGMNPLYDEEPFVFKKVVLPELASIRIAAYEEGGKLIGHRV PIPA_DICDI Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." DPTSPERIKSSKYSRLIVNVISARQLPKYTKSTKGEVIDPYVTLSIVGTHFDQKVEKTKVIDNNGFNPHWGEEFEFPLYNSQLSMLLIRVDDKDKVGHNRIGHHC PIPA_DROME Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Involved in phototransduction." DPFADAPVDGVIAAQCSVKVIAGQFLSDKKVGTYVEVDMFGLPSDTVKKEFRTRLVANNGLNPVYNEDPFVFRKVVLPDLAVLRFGVYEESGKILGQRI PLC1_SCHPO Yeast 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." KLTIDVISGQQLRRARELSNSETLSPYVEIQVHSMEESPFRWCSKVVHENGFRPFWGETMVYESIISDDFYSMIRFLVHHRGSNGNDSIFANFT PLC1_YEAST Yeast 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This enzyme is also required for cell growth." TVKIRILSTQLLPRLNDTSPSRNNTNSFVKVEFHTDDEPTMPISIDKGTRISATEASTKSSQGNGFNPIWDAEVSITLKDTDLTFIKFMVISEETQIASVCLKLNYLRMGYRH PLCB1_BOVIN Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." DPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPIWEEEPIVFKKVVLPSLACLRIAVYEEGGKFIGHRI PLCB1_HUMAN Human 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." DPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRI PLCB1_MOUSE Mouse 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (By similarity)." DPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFTTKTSQGNAVNPVWEEEPIVFKKVVLPSLACLRIAAYEEGGKFIGHRI PLCB1_RAT Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." SUBCELLULAR LOCATION: Cytoplasmic and particulate fractions. DPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPSLACLRIAAYEEGGKFIGHRI PLCB2_HUMAN Human 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." NPFSVDRIDVVVATTLSITVISGQFLSERSVRTYVEVELFGLPGDPKRRYRTKLSPSTNSINPVWKEEPFVFEKILMPELASLRVAVMEEGNKFLGHRI PLCB2_RAT Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This protein may be involved in the transduction of bitter taste stimuli." NPFSVDRIDVVVATTLSITVISGQFLSERSVRTYVEVELFGLPGDPKRRYRTKLSPTANSINPVWKEEPFIFEKILVPELASLRIAVMEEGGKFIGHRI PLCB3_MOUSE Mouse 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." SUBCELLULAR LOCATION: Nucleus. DPFTEVIVDGIVANALRVKVISGQFLSDKKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGKFVGHRI PLCB3_RAT Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." SUBCELLULAR LOCATION: Cytoplasmic and particulate fractions. DPFTEVIVDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGRFVGHRI PLCB4_BOVIN Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction." DPFSETPVDGVIAATCSVQVISGQFLSDKKIGTYVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNKLIGQRI PLCB4_HUMAN Human 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction." DPFSETPVDGVIAATCSVQVISGQFLSDKKIGTYVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNKLIGQRI PLCB4_RAT Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction." DPFSETPVDGVIAATCSVQVISGQFLSDKKIGTYVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNKLIGQRI PLCD1_BOVIN Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." PKRLNVRVISGQQLPKVNKNKNSIVDPKVTVEIHGVTGDVASRQTAVVTNNGFNPWWDTELEFEVAVPELALVRFVVEDYDASSKNDFIGQST PLCD1_HUMAN Human 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." NPRALAQGPWWARKRLNIRVISGQQLPKVNKNKNSIVDPKVTVEIHGVSRDVASRQTAVITNNGFNPWWDTEFAFEVVVPDLALIRFLVEDYDASSKNDFIGQST PLCD1_MOUSE Mouse 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." KLRVWIISGQQLPKVNKNKNSIVDPKVIVEIHGVGQDVASRQTAVITNNGFNPRWDTEFEFVVAVPDLALVRFMVEDYDSSSKNDFIGQST PLCD1_RAT Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." RLRVRIISGQQLPKVNKNKNSIVDPKVIVEIHGVGRDTGSRQTAVITNNGFNPRWDMEFEFEVTVPDLALVRFMVEDYDSSSKNDFIGQST PLCG1_BOVIN Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." DPFDKSSLRGLEPCAICIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSIKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQAT PLCG1_MOUSE Mouse 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." DPFDKSSLRGLEPCVICIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQAT PLCG1_RAT Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." DPFDKSSLRGLEPCVICIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQAT PLCG2_HUMAN Human 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling." ILMTLTVKVLGARHLPKLGRSIACPFVEVEICGAEYDNNKFKTTVVNDNGLSPIWAPTQEKVTFEIYDPNLAFLRFVVYEEDMFSDPNFLAHAT PLCG2_RAT Others 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling." ILMTLTVKVLGARHLPKLGRSIACPFVEVEICGAEYDSNKFKTTVVNDNGLSPVWAPTQEKVTFEIYDPNLAFLRFLVYEEDMFSDPNFLAHAT PLCL4_HUMAN Human 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (By similarity)." NPNSEDPLPGQLKKQLVLRIISGQQLPKPRDSMLGDRGEIIDPFVEVEIIGLPVDCSREQTRVVDDNGFNPTWEETLVFMVHMPEIALVRFLVWDHDPIGRDFIGQRT PLDA1_PIMBR Others 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes. MAKTLLHGTLHVTIFEVDHLKAGSVVVFSESLRRTLRKPLVLAKGTPKIYASIDLDKARVGRTRMIENEPNNPKWNESFHIYCGHPSTNVIFTVKDDNPIGATLIGRAY PLDG1_ARATH Mouse 1 " FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Can use phosphatidylserine but prefers ethanolamine-containing lipids as substrates." " SUBCELLULAR LOCATION: Cytoplasmic and membrane-associated. Found mainly associated with intracellular membranes but also with mitochondrial membranes, nuclei and clathrin-coated vesicles. Not found in chloroplast." ATSSGSLRVELLHGNLDIWVKEAKHLPNMDGFHNRLGGMLSGLGRKKVEGEKSSKITSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDSDIIGSQIMGAVG PLDG2_ARATH Mouse 1 " FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Can use phosphatidylserine but prefers ethanolamine-containing lipids as substrates." " SUBCELLULAR LOCATION: Cytoplasmic and membrane-associated. Found mainly associated with intracellular membranes but also with mitochondrial membranes, nuclei and clathrin-coated vesicles. Not found in chloroplast." WLDQQLVPLATSSGSLMVELLHGRRIRKVDGEKSSKFTSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVAHSAAEVHFVVKDNDPIGSKIIGVVG PLDG3_ARATH Mouse 1 " FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action, vesicular trafficking, secretion, cytoskeletal arrangement, meiosis, tumor promotion, pathogenesis, membrane deterioration and senescence. Can use phosphatidylserine but prefers ethanolamine-containing lipids as substrates." " SUBCELLULAR LOCATION: Cytoplasmic and membrane-associated. Found mainly associated with intracellular membranes but also with mitochondrial membranes, nuclei and clathrin-coated vesicles. Not found in chloroplast." DTSSGSLRVELLHGNLDIWVKEAKHLPNMDGFHNTLVGGMFFGLGRRNHKVDGENSSKITSDPYVTVSISGAVIGRTFVISNSENPVWMQHFDVPVAHSAAKVHFVVKDSDIIGSQIIGAVE RFIP1_HUMAN Human 1 FUNCTION: A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and in phagocytosis. SUBCELLULAR LOCATION: Membrane-bound (isoform 2). Rab11A rather than Rab4A mediates localization in the endocytic recycling compartment (ERC). Colocalizes with Rab11A at phagosomes (isoform 2). VSAGRGLGAVWSPTHVQVTVLQARGLRAKGPGGTSDAYAVIQVGKEKYATSVSERSLGAPVWREEATFELPSLLSSGPAAAATLQLTVLHRALLGLDKFLGRAE RFIP1_MOUSE Mouse 1 FUNCTION: A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and phagocytosis (By similarity). SUBCELLULAR LOCATION: Membrane-bound. RAB11A rather than RAB4A mediates RAB11FIP1 localization in the endocytic recycling compartment (ERC). Colocalizes with RAB11A at phagosomes (By similarity). ASAGRGPGTMWSPTHVQVTVLQARGLRAKGPGGTSDAYAVIQVGKEKYATSVSERTLGAPVWREEATFELPPLLSSGAAPAAAATLQLTVLHRALLGLDKFLGRAE RFIP1_RAT Others 1 FUNCTION: A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and phagocytosis (By similarity). SUBCELLULAR LOCATION: Membrane-bound. RAB11A rather than RAB4A mediates RAB11FIP1 localization in the endocytic recycling compartment (ERC). Colocalizes with RAB11A at phagosomes (By similarity). ASAGRGPGTMWSPTHVQVTVLQARGLRAKGPGGTSDAYAVIQVGKEKYATSVSERSLGAPVWREEATFELPPLLSSGTAPAAAAATLQLTVLHRALLGLDKFLGRAE RP3A_BOVIN Others 1 FUNCTION: Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. SSLHCTIIKAKGLKPMDSNGLADPYVKLHLLPGASKSNKLRTKTLRNTRNPIWNETLVYHGITDEDMQRKTLRISVCDEDKFGHNEFIGETR RP3A_HUMAN Human 1 FUNCTION: Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal (By similarity). GALEFSLLYDQDNSSLQCTIIKAKGLKPMDSNGLADPYVKLHLLPGASKSNKLRTKTLRNTRNPIWNETLVYHGITDEDMQRKTLRISVCDEDKFGHNEFIGETR RP3A_MOUSE Mouse 1 FUNCTION: Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. GALEFSLLYDQDNSNLQCTIIRAKGLKPMDSNGLADPYVKLHLLPGASKSNKLRTKTLRNTRNPVWNETLQYHGITEEDMQRKTLRISVCDEDKFGHNEFIGETR RP3A_RAT Others 1 FUNCTION: Protein transport. Probably involved with Ras-related protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal. GALEFSLLYDQDNSNLQCTIIRAKGLKPMDSNGLADPYVKLHLLPGASKSNKLRTKTLRNTRNPVWNETLQYHGITEEDMQRKTLRISVCDEDKFGHNEFIGETR KLNELITENGTVCQQLVVHIKACHGLPLINGQSCDPYATVSLVGPSRNDQKKTKVKKKTSNPQFNEIFYFEVTRSSSYTRKSQFQVEEEDIEKLEIRIDLWNNGNLVQDVFLGEIK SY61_DISOM Others 1 FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. SUBCELLULAR LOCATION: Synaptic vesicles in neurons. NQLIVGIIQAAELPALDVGGTSDPYVKVFVLPDKKKKYETKVHRKTLNPVFNESFIFKIPYSELGGKTLVMAVYDFDRFSKHDVIGEAK NGTVCQQLVVHIKACHGLPLINGQSCDPYATVSLVGPSRNDQKKTKVKKKTSNPQFNEVFYFEVTRSSSYSRKSQFQVEEEDIEKLEIRIDLWNNENLVQDVFLGEIK SY62_DISOM Others 1 FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. SUBCELLULAR LOCATION: Synaptic vesicles in neurons. ANQLTVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVQKKTLNPTFNESFVFKVPYQELGGKTLMMAVYDFDRFSKHDCIGQVT NGTVCQQLVVHIKACHGLPLINGQSCDPYATVSLVGPSRNDQKKTKVKKKTSNPQFNEVFYFEVTRSSSYTRKSQFQVEEEDIEKLEIRIDLWNNENLVQDVFLGEIK SY63_DISOM Others 1 FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. SUBCELLULAR LOCATION: Synaptic vesicles in neurons. QLVVKILKALDLPAKDANGFSDPYVKIYLLPDRKKKFQTKVHRKTLNPIFNETFQFNVPFNELQNRKLHFSVYDFDRFSRHDLIGQVV GVVCHKLATRILECQGLPIVNGQCDPYATVTLAGPCRSEAKKTKVKKKTNNPQFDEVFYFEVTRPCSYSRKSHFDFEDEDVDKLEIRVDLWNASNLKFGDEFLGELR SY65_DROME Others 1 FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. SUBCELLULAR LOCATION: Synaptic vesicles in neurons. SNSLAVTVIQAEELPALDMGGTSDPYVKVYLLPDKKKKFETKVHRKTLSPVFNETFTFKSLPYADAMNKTLVFAIFDFDRFSKHDQIGEVK GVVCHKLATRIVECQGLPIVNGQCDPYATVTLAGPFRSEAKKTKVKRKTNNPQFDEVFYFEVTRPCSYSKKSHFDFEEEDVDKLEIRVDLWNASNLKFGDEFLGELR SYT10_HUMAN Human 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). GKLNFTLQYDYENELLVVKIIKALDLPAKDFTGTSDPYVKMYLLPDRKKKFQTRVHRKTLNPLFDETFQFPVAYDQLSNRKLHFSVYDFDRFSRHDMIGEVI GVVCHKLAARIFECQGLPIVNGQCDPYATVTLAGPFRSEAKKTKVKKKTNNPQFDEVFYFEVTRPCSYSKKSHFDFEEEDVDKLEIRVDLWNASNLKFGDEFLGELR SYT10_MOUSE Mouse 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). GKLNFALQYDYENELLVVKIIKALDLPAKDFTGTSDPYVKIYLLPDRKKKFQTRVHRKTLNPLFDELFQFPVVYDQLSNRKLHFSIYDFDRFSRHDMIGEVI ICLSVQMLEDGQGRCLRCHVLQARDLAPRDISGTSDPFARVFWGSQSLETSTIKKTRFPHWDEVLELREMPGAPSPLRVELWDWDMVGKNDFLGMVE SYT10_PONPY Others 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). GKLNFTLQYDYENELLVVKIIKALDLPAKDFTGTSDPYVKMYLLPDRKKKFQTRVHRKTLNPLFDETFQFPVAYDQLSNRKLHFSVYDFDRFSRHDMIGEVI LRCHVRQARDLAPRDISGTSDPFARVFWGNHSLETSTIKKTRFPHWDEVLELREAPGTTSPLRVELWDWDMVGKNDFLGMVE SYT10_RAT Others 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). GKLNFALQYDYENELLVVKIIKALDLPAKDFTGTSDPYVKIYLLPDRKKKFQTRVHRKTLNPLFDELFQFPVVYDQLSNRKLHFSIYDFDRFSRHDMIGEVI GARACRLRCSVLEARDLAPKDRNGTSDPFVRVRYKGRTRETSIVKKSCYPRWNETFEFELQEGAMEALCVEAWDWDLVSRNDFLGKVV SYT11_HUMAN Human 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). " SUBCELLULAR LOCATION: Membrane; single-pass membrane protein. In substantia nigra, observed in neuronal cell bodies and neurites. Found in the core of the Lewy bodies in the brain of sporadic Parkinson disease patients." LVVTIQEAHGLPVMDDQTQGSDPYIKMTILPDKRHRVKTRVLRKTLDPVFDETFTFYGIPYSQLQDLVLHFLVLSFDRFSRDDVIGEVM SLFININRCVELVGMDSTGFSDPYCKVSLTPITSKAHRAKTSTKKRTLNPEWNEQLQFVVPFKDLPKKTLQIGVYDHDLGKHDDYIGGIL SYT11_MOUSE Mouse 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). LVVTIQEAHGLPVMDDQTQGSDPYIKMTILPDKRHRVKTRVLRKTLDPVFDETFTFYGIPYSQLQDLVLHFLVLSFDRFSRDDVIGEVM SYT11_RAT Others 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). GSLTFSVDYNFPKKALVVTIQEAHGLPVMDGQTQGSDPYIKMTILPDKRHRVKTRVLRKTLDPVFDETFTFYGIPYSQLQDLVLHFLVLSFDRFSRDDVIGEVM SYT12_HUMAN Human 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). TLNVAVMQGKDLLEREEASFESCFMRVSLLPDEQIVGISRIQRNAYSIFFDEKFSIPLDPTALEEKSLRFSVFGIDEDERNVSTGVVELKLSVLDLPLQPFSGWL SYT12_MOUSE Mouse 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). TLHVAVLQGKDLLEREEATFESCFMRVSLLPDEQIVGISRIQRNAYSIFFDEKFSVPLDPTALEEKSLRFSVFGIDEDERNVSTGVVELKLSVLDLPLQPFSGWL SYT12_RAT Others 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). TLHVAVLQGKDLLEREEATFESCFMRVSLLPDEQIVGISRIQRNAYSIFFDEKFSVPLDPTALEEKSLRFSVFGIDEDERNVSTGVVELKLSVLDLPLQPFSGWL SYT13_HUMAN Human 1 FUNCTION: May be involved in transport vesicle docking to the plasma membrane (By similarity). SUBCELLULAR LOCATION: Membrane; single-pass membrane protein (By similarity). LFVTRLEAVTSNHDGGCDCYVQGSVANRTGSVEAQTALKKRQLHTTWEEGLVLPLAEEELPTATLTLTLRTCDRFSRHSVAGELR SYT13_MOUSE Mouse 1 FUNCTION: May be involved in transport vesicle docking to the plasma membrane. SUBCELLULAR LOCATION: Membrane; single-pass membrane protein. LFVTSLEAVTSDHEGGCDCYIQGSVAVKTGSVEAQTALKKRQLHTTWEEGLALPLGEEELPTATLTLTLRTCDRFSRHSVIGELR SYT13_RAT Others 1 FUNCTION: May be involved in transport vesicle docking to the plasma membrane (By similarity). SUBCELLULAR LOCATION: Membrane; single-pass membrane protein (By similarity). LFVTSLEAVTSDHEGGCDCYIQGSVAVKTGSVEAQTALKKRQLHTTWEEGLTLPLGEEELPTATLTLTLRTCDRFSRHSVIGELR AMGDIQIGMEDKKGQLEVEVIRARSLTQKPGSKSTPAPYVKVYLLENGACIAKKKTRIARKTLDPLYQQSLVFDESPQGKVLQVIVWGDYGRMDHKCFMGVAQ SYT14_HUMAN Human 1 FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent. SUBCELLULAR LOCATION: Membrane; single-pass type III membrane protein (Potential). KLLVTVTAVTDIPTYNRTGGNSWQVHLVLLPIKKQRAKTSIQRGPCPVFTETFKFNHVESEMIGNYAVRFRLYGVHRMKKEKIVGEKIFYLTKLNLQGKMSLP AMGDIQIGMEDKKGQLEVEVIRARSLTQKPGSKSTPAPYVKVYLLENGACIAKKKTRIARKTLDPLYQQSLVFDESPQGKVLQVIVWGDYGRMDHKCFMGVAQ SYT14_MOUSE Mouse 1 FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Is Ca(2+)-independent. SUBCELLULAR LOCATION: Membrane; single-pass type III membrane protein (Potential). KLLVTVTAVTDIPTYNRTGGNSWQVHLVLLPIKKQRAKTSIQRGPCPVFTETFKFNHVESEMIGNYAVRFRLYGVHRMKKEKIVGEKIFYLTKLNLQGKMSLP AMGDIQVGMMDKKGQLEVEIIRARGLVVKPGSKTLPAPYVKVYLLDNGVCIAKKKTKVARKTLEPLYQQLLSFEESPQGKVLQIIVWGDYGRMDHKSFMGVAQ SYT15_HUMAN Human 1 FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues (By similarity). " SUBCELLULAR LOCATION: Isoform 1, isoform 2, isoform 4: Cell membrane; single-pass type III membrane protein (By similarity)." GRLWFSVEYEQEAERLLVGLIKAQHLQAPSETCSPLVKLYLLPDERRFLQSKTKRKTSNPQFDEHFIFQVSSKTITQRVLKFSVYHVDRQRKHQLLGQVL AMGDIQVGMMDKKGQLEVEIIRARGLVVKPGSKTLPAPYVKVYLLDNGVCIAKKKTKVARKTLEPLYQQLLSFEESPQGRVLQIIVWGDYGRMDHKSFMGVAQ SYT15_MOUSE Mouse 1 FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. SUBCELLULAR LOCATION: Membrane; single-pass type III membrane protein. GRLWFSVEYQQESERLLVGLIKAQQLQVPSETCSTLVKLHLLPDERRFLQSKTKHKICNPQFDENFIFQVSSKSVTQRVLKFSVYHVNKKRKHQLLGQVL AMGDIQVGMMDKKGQLEVEIIRARGLVVKPGSKTLPAPYVKVYLLDNGVCIAKKKTKVARKTLEPLYQQLLSFEESPQGKVLQIIVWGDYGRMDHKSFMGVAQ SYT15_RAT Others 1 FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues (By similarity). SUBCELLULAR LOCATION: Membrane; single-pass type III membrane protein (By similarity). GRLWFSVEYQQESERLLVDLIKAQHLQVPAETCSTLVKLHLLPDKRRFLQSKAKRKTCNPQFDESFIFQVSSKSVAQRVLKFSVYHINKQRKHQLLGQVL SYT1_BOVIN Others 1 " FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2." SUBCELLULAR LOCATION: Synaptic vesicles and chromaffin granules. GKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFK SYT1_CAEEL Others 1 FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone (By similarity). SUBCELLULAR LOCATION: Synaptic vesicles and vesicle-like structures. QLTVTVIQAEDLPGMDMSGTSDPYVKLYLLPEKKKKVETKVHRKTLNPVFNETFIFKVAFNEITAKTLVFAIYDFDRFSKHDQIGQVL SYT1_CHICK Others 1 FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. SUBCELLULAR LOCATION: Synaptic vesicles and chromaffin granules. NQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEYK SYT1_HUMAN Human 1 " FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2." SUBCELLULAR LOCATION: Synaptic vesicles and chromaffin granules. NQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFK SYT1_MACFA Others 1 " FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2 (By similarity)." SUBCELLULAR LOCATION: Synaptic vesicles and chromaffin granules (By similarity). GKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFK SYT1_MOUSE Mouse 1 " FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2." SUBCELLULAR LOCATION: Synaptic vesicles and chromaffin granules. GKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFK VLGEIQIALMAGRSGIDVEIIKAKNLVVKPGVKVCPAPYVKVYLMEGKQCIAKAKTNAATKTTSPLFQQHLIFNDSPKKKTLQVTVLGDYGRMERKVFMGISQ SYT1_PONPY Others 1 " FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2 (By similarity)." SUBCELLULAR LOCATION: Synaptic vesicles and chromaffin granules. GKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFK LIVGIIRCVHLAAMDANGYSDPFVKLWLKPDMGKKAKHKTQIKKKTLNPEFNEEFFYDIKHSDLAKKSLDISVWDYDIGKSNDYIGGCQ SYT1_RAT Others 1 " FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2." SUBCELLULAR LOCATION: Synaptic vesicles and chromaffin granules. GKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFK GKILVSLMYSTQQGGLIVGIIRCVHLAAMDANGYSDPFVKLWLKPDMGKKAKHKTQIKKKTLNPEFNEEFFYDIKHSDLAKKSLDISVWDYDIGKSNDYIGGCQ SYT2_HUMAN Human 1 FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone (By similarity). SUBCELLULAR LOCATION: Synaptic vesicles and chromaffin granules (By similarity). GKLQFSLDYDFQANQLTVGVLQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPAFNETFTFKVPYQELGGKTLVMAIYDFDRFSKHDIIGEVK GKILVSLMYSTQQGGLIVGIIRCVHLAAMDANGYSDPFVKLWLKPDMGKKAKHKTQIKKKTLNPEFNEEFFYDIKHSDLAKKSLDISVWDYDIGKSNDYIGGCQ SYT2_MOUSE Mouse 1 FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. SUBCELLULAR LOCATION: Synaptic vesicles and chromaffin granules. ANQLTVGVLQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPAFNETFTFKVPYQELAGKTLVMAIYDFDRFSKHDIIGEVK GKILVSLMYSTQQGGLIVGIIRCVHLAAMDANGYSDPFVKLWLKPDMGKKAKHKTQIKKKTLNPEFNEEFFYDIKHSDLAKKSLDISVWDYDIGKSNDYIGGCQ SYT2_RAT Others 1 FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. SUBCELLULAR LOCATION: Synaptic vesicles and chromaffin granules. ANQLTVGVLQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPAFNETFTFKVPYQELGGKTLVMAIYDFDRFSKHDIIGEVK SYT3_HUMAN Human 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Membrane-associated protein. Synaptic vesicles (By similarity). GRISFALRYLYGSDQLVVRILQALDLPAKDSNGFSDPYVKIYLLPDRKKKFQTKVHRKTLNPVFNETFQFSVPLAELAQRKLHFSVYDFDRFSRHDLIGQVV SYT3_MOUSE Mouse 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Membrane-associated protein. Synaptic vesicles. GRISFALRYLYGSDHLVVRILQALDLPAKDSNGFSDPYVKIYLLPDRKKKFQTKVHRKTLNPIFNETFQFSVPLAELAQRKLHFSVYDFDRFSRHDLIGQVV SYT3_RAT Others 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Membrane-associated protein. Synaptic vesicles. GRISFALRYLYGSDQLVVRILQALDLPAKDSNGFSDPYVKIYLLPDRKKKFQTKVHRKTLNPIFNETFQFSVPLAELAQRKLHFSVYDFDRFSRHDLIGQVV SYT4_HUMAN Human 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein. GTLFFSLEYNFERKAFVVNIKEARGLPAMDEQSMTSDPYIKMTILPEKKHKVKTRVLRKTLDPAFDETFTFYGIPYTQIQELALHFTILSFDRFSRDDIIGEVL SYT4_MOUSE Mouse 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein. GTLFLSLEYNFEKKAFVVNIKEAQGLPAMDEQSMTSDPYIKMTILPEKKHRVKTRVLRKTLDPVFDETFTFYGIPYPHIQELSLHFTVLSFDRFSRDDVIGEVL SYT4_RAT Others 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein. GTLFLSLEYNFEKKAFVVNIKEAQGLPAMDEQSMTSDPYIKMTILPEKKHKVKTRVLRKTLDPVFDETFTFYGVPYPHIQELSLHFTVLSFDRFSRDDVIGEVL SYT5_HUMAN Human 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)- dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface (By similarity). " SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). Endosome; recycling endosome; recycling endosomal membrane; multi-pass membrane protein (By similarity). In mast cells, localizes to the endocytic recycling compartment (By similarity)." QLLVGILQAMGLAALDLGGSSDPYVRVYLLPDKRRRYETKVHRQTLNPHFGETFAFKVPYVELGGRVLVMAVYDFDRFSRNDAIGEVR SYT5_MOUSE Mouse 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)- dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface. " SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein. Endosome; recycling endosome; recycling endosomal membrane; multi-pass membrane protein. In mast cells, localizes to the endocytic recycling compartment." QLLVGILQAQGLAALDLGGSSDPYVSVYLLPDKRRRHETKVHRQTLNPHFGETFAFKVPYVELGGRVLVMAVYDFDRFSRNDAIGEVR SYT5_RAT Others 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)- dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface. " SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein. Endosome; recycling endosome; recycling endosomal membrane; multi-pass membrane protein. In mast cells, localizes to the endocytic recycling compartment." QLLVGILQAEGLAALDLGGSSDPYVSVYLLPDKRRRHETKVHRQTLNPHFGETFAFKVPYVELGGRVLVMAVYDFDRFSRNDAIGEVR AGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVF SYT6_HUMAN Human 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). GKINFSLRYDYETETLIVRILKAFDLPAKDFCGSSDPYVKIYLLPDRKCKLQTRVHRKTLNPTFDENFHFPVPYEELADRKLHLSVFDFDRFSRHDMIGEVI AGKLTVCILEAKNLKKMDVGGLSDPYVKIHLLQNGKRLKKKKTTVKKNTLNPYYNESFSFEIPFEQIQKVQVCVTVLDYDKIGKNDAIGKIF SYT6_MOUSE Mouse 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein. GKINFSLRYDYESETLIVRILKAFDLPAKDFCGSSDPYVKIYLLPDRKCKLQTRVHRKTLNPTFDENFHFPVPYEELADRKLHLSVFDFDRFSRHDMIGEVI AGRLTITIIKATNLKAMDLTGFSDPYVKASLICDERRLKKRKTSIKKNTLNPVYNEALVFDIPNENMEHVNVIIAVMDYDCIGHNEVIGMCR SYT6_RAT Others 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). GKINFSLRYDYESETLIVRILKAFDLPAKDFCGSSDPYVKIYLLPDRKCKLQTRVHRKTLNPTFDENFHFPVPYEELADRKLHLSVFDFDRFSRHDMIGEVI GDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIALLQGTKRLKKKKTTIKKNTLNPYFNESFGFEVPFEQIQKVTLIITVVDYDRIGTSEPIGRCV SYT7_HUMAN Human 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). GRIQFSVGYNFQESTLTLKIMKAQELPAKDFSGTSDPFVKIYLLPDKKHKLKTKVKRKNLNPHWNETFLFEGFPYEKVVQRILYLQVLDYDRFSRNDPIGEVS AGKLTVVILEAKNLKKMDVGGLSDPYVKIAIMQNGKRLKKKKTSVKKCTLNPYYNESFSFEVPFEQMQKICLVVTVVDYDRIGTSEPIGRCI SYT7_MOUSE Mouse 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (By similarity). SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). GRIQFSVGYNFQESTLTVKVMKAQELPAKDFSGTSDPFVKIYLLPDKKHKLETKVKRKNLNPHWNETFLFEGFPYEKVVQRVLYLQVLDYDRFSRNDPIGEVS GEIMFSLCYLPTAGRMTLTVIKCRNLKAMDITGSSDPYVKVSLMCEGRRLKKRKTTTKKNTLNPVYNEAIIFDIPPENVDQVSLSIAVMDYDRVGHNEVIGVCR SYT8_MOUSE Mouse 1 FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. May mediate Ca(2+)- regulation of exocytosis in insulin secreted cells and acrosomal reaction in sperm. SUBCELLULAR LOCATION: Cell membrane; single-pass type III membrane protein. Acrosome. GRLLLSLEYDFGSQEIRVGLRQAGNLKAEGTADPYAWVSVSTQSGRRHETKVHRGTLSPMFEETCCFLVPPAELPKATLKVQLWDFKRFSEHEPLGELQ GEIMFSLCYLPTAGRMTLTVIKCRNLKAMDITGSSDPYVKVSLMCEGRRLKKRKTTTKKNTLNPVYNEAIIFDIPPENVDQVSLCIAVMDYDRVGHNEVIGVCR SYT8_RAT Others 1 FUNCTION: May be involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. May mediate Ca(2+)- regulation of exocytosis in insulin secreted cells and acrosomal reaction in sperm (By similarity). SUBCELLULAR LOCATION: Cell membrane; single-pass type III membrane protein (By similarity). Acrosome (By similarity). GQLLLSLEYDFGSQEIRVGLRQAKNLKAEGTADPYARVSVSTQAGRRHETKVHRGTLCPMFEETCCFLVPPAELPKATLKVQLLDFKRFSEHEPLGELQ GEIMFSLCYLPTAGRMTLTVIKCRNLKAMDITGSSDPYVKVSLMCEGRRLKKRKTTTKKNTLNPVYNEAIIFDIPPENVDQVSLSIAVMDYDRVGHNEVIGVCR SYT9_HUMAN Human 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein (By similarity). GKLNFILKYDCDLEQLIVKIHKAVNLPAKDFSGTSDPYVKIYLLPDRKTKHQTKVHRKTLNPVFDEVFLFPVPYNDLEARKLHFSVYDFDRFSRHDLIGQVV GEIMFSLCYLPTAGRMTLTVIKCRNLKAMDITGSSDPYVKVSLMCEGRRLKKRKTTTKKNTLNPVYNEAIIFDIPPENVDQVSLCIAVMDYDRVGHNEVIGVCR SYT9_MOUSE Mouse 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein. GKLNFILKYDCDLEQLIVKIHKAVNLPAKDFSGTSDPYVKIYLLPDRKTKHQTKVHRKTLNPVFDEVFLFPVHYNDLEARKLHFSVYDFDRFSRHDLIGQVV VAQRMTVVVLKARHLPKMDITGLSGNPYVKVNVYYGRKRIAKKKTHVKKCTLNPIFNESFIYDIPTDLLPDISIEFLVIDFDRTTKNEVVGRLI SYT9_RAT Others 1 FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; multi-pass membrane protein. GKLNFILKYDCDLEQLIVKIHKAVNLPAKDFSGTSDPYVKIYLLPDRKTKHQTKVHRKTLNPVFDEVFLFPVHYNDLEARKLHFSVYDFDRFSRHDLIGQVV VAQRMTVVVLKARHLPKMDITGLSGNPYVKVNVYYGRKRIAKKKTHVKKCTLNPVFNESFIYDIPTDLLPDISIEFLVIDFDRTTKNEVVGRLI SYTL4_HUMAN Human 1 FUNCTION: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity). " SUBCELLULAR LOCATION: Peripheral membrane protein. Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles (By similarity)." GRIAFSLKYEQQTQSLVVHVKECHQLAYADEAKKRSNPYVKTYLLPDKSRQGKRKTSIKRDTVNPLYDETLRYEIPESLLAQRTLQFSVWHHGRFGRNTFLGEAE GELQVSLSYQPVAQRMTVVVLKARHLPKMDITGLSGNPYVKVNVYYGRKRIAKKKTHVKKCTLNPIFNESFIYDIPTDLLPDISIEFLVIDFDRTTKNEVVGRLI SYTL4_MOUSE Mouse 1 FUNCTION: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner. " SUBCELLULAR LOCATION: Peripheral membrane protein. Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles." GKIAFSLKFEQKTQTLVIHVKECHQLAYADEAKKRSNPYVKTYLLPDKSRQGKRKTSIKRDTINPLYDETFRYEISESLLAQRTLQFSVWHHGRFGRNTFLGEAE GEILLSLSYLPTAERLTVVVVKAKNLIWTNDKTTADPFVKVYLLQDGRKMSKKKTAVKRDDPNPVFNEAMIFSVPAIVLQDLSLRVTVAESSSDGRGDNVGHVI SYTL4_RAT Others 1 FUNCTION: Modulates exocytosis of dense-core granules and secretion of hormones in the pancreas and the pituitary. Interacts with vesicles containing negatively charged phospholipids in a Ca(2+)-independent manner (By similarity). " SUBCELLULAR LOCATION: Peripheral membrane protein. Detected close to the plasma membrane and on secretory granules. In pancreas, interacts with insulin-containing vesicles." GKIAFSLKFEQKTQTLVIHVKECHQLAYADEAKKRSNPYVKTYLLPDKSRQGKRKTSIKRDTINPLYDETFRYEISESLLAQRTLQFSVWHHGRFGRNTFLGEAE GEILLSLSYLPTAERLTVVVVKAKNLIWTNEKSTADPFVKVYLLQDGRKMSKKKTAVKRDDPNPVFNEAMIFSVPAIVLQDLSLRVTVAESSSDGRGDNVGHVI UN13C_RAT Others 1 FUNCTION: Probably plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Probably is involved in neurotransmitter release. SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; peripheral membrane protein (Probable). Localized to presynaptic structures (Probable). AKQSVLDGTSKWSAKITITVVSAQGLQAKDKTGSSDPYVTVQVGKNKRRTKTIFGNLNPVWDEKFYFECHNSTDRIKVRVWDEDDDIKSRVKQHFKKESDDFLGQTI GEILLSLSYLPTAERLTVVVVKAKNLIWTNDKTTADPFVKVYLLQDGRKMSKKKTAVKRDDPNPVFNEAMIFSVPAIVLQDLSLRVTVAESSSDGRGDNVGHVI UNC13_CAEEL Others 1 " FUNCTION: May form part of a signal transduction pathway, transducing the signal from diacylglycerol to effector functions. One such function could be the release of neurotransmitter from neurons." LCITIKKARLQGAVDEFNSYVTVKLQTVKSTTVAVRGNLPCWEQEFIFETNRPDDGMVLELWAKGVLWDKLIGVHY GEVLLSISYLPAANRLLVVLIKAKNLHSNQSKELLGKDVSVKVTLKHQARKLKKKQTKRAKHKINPVWNEMIMFELPDDLLQASSVELEVLGQDDSGQSCALGHCS CAPS1_HUMAN Human 1 " FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates to DCVs-membrane fusion. However, it may also participate to small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering (By similarity)." " SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Preferentially binds to DCVs but not to SVs. Binds phosphoinosides, with a strong selectivity for PtdIns(4,5)P2 over PtdIns(3,4,5)P3. Probably localizes to different vesicles compared to CADPS2 (By similarity)." LEVVIMEVQGLKSLAPNRIVYCTMEVEGGEKLQTDQAEASKPTWGTQGDFSTTHALPAVKVKLFTESTGVLALEDKELGRVI GEVLLSISYLPAANRLLVVLIKAKNLHSNQSKELLGKDVSVKVTLKHQAQKLKKKQTKRAKHKINPVWNEMIMFELPDDLLRASSVELEVLGQGEEGPSCELGHCS CAPS1_MOUSE Mouse 1 " FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates to DCVs-membrane fusion. However, it may also participate to small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering (By similarity)." " SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. May preferentially binds to DCVs but not to SVs. Probably localizes to different vesicles compared to CADPS2. Binds phosphoinosides, with a strong selectivity for PtdIns(4,5)P2 over PtdIns(3,4,5)P3." LEVVIMEVQGLKSLAPNRIVYCTMEVEGGEKLQTDQAEASKPTWGTQGDFSTTHALPAVKVKLFTESTGVLALEDKELGRVI GEVLLSISYLPAANRLLVVLIKAKNLHSNQSKELLGKDVSVKVTLKHQAQKLKKKQTKRAKHKINPVWNEMIMFELPDDLLQASSVELEVLGQGEEGPSCELGRCS CAPS1_RAT Others 1 " FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates to DCVs-membrane fusion. However, it may also participate to small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering." " SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Preferentially binds to DCVs but not to SVs. Binds phosphoinosides, with a strong selectivity for PtdIns(4,5)P2 over PtdIns(3,4,5)P3. Probably localizes to different vesicles compared to CADPS2." LEVVIMEVQGLKSLAPNRIVYCTMEVEGGEKLQTDQAEASKPTWGTQGDFSTTHALPAVKVKLFTESTGVLALEDKELGRVI PEILIGLLYNATTGRLSAEVIKGSHFKNLAANRPPNTYVKLTLLNSMGQEMSKCKTSIRRGQPNPVYKETFVFQVALFQLSDVTLILSVYNKRSMKREEMIGWIS CAPS1_XENLA Others 1 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) (By similarity). SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Preferentially binds to DCVs but not to SVs. Binds phosphoinosides (By similarity). LEVVIMEVQGLKSLAPNRIVYCTMEVEGGQKLQTDQAEASKPMWGTQGDFSTTHALPAVKVKLFTESTGVLALEDKELGRVV PEILIGLLYNATTGRLSAEVIKGSHFKNLAANRPPNTYVKLTLLNSMGQEMSKCKTSTRRGQPNPVYKETFVFQVALFQLSDVTLILSVYNRRSMKRKEMIGWIS CAPS2_HUMAN Human 1 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates neurotrophin release from granule cells leading to regulate cell differentiation and survival during cerebellar development. May specifically mediate the Ca(2+)- dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles (By similarity). SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Probably localizes to different vesicles compared to CADPS. Enriched on vesicular structures in the parallel fiber terminal of granule cells that are distinct from synaptic vesicles. LEIVIMEVQGLKSVAPNRIVYCTMEVEGEKLQTDQAEASRPQWGTQGDFTTTHPRPVVKVKLFTESTGVLALEDKELGRVI GDLQFCLSYNDYLSRLTVVVLRAKGLRLQDDRGIVSVFVKVSLMNHNKFVKCKKTSAVLGSINPVYNETFSFKADATELDTASLSLTVVQNMEGDKSQQLGRVV CAPS2_MOUSE Mouse 1 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates neurotrophin release from granule cells leading to regulate cell differentiation and survival during cerebellar development. May specifically mediate the Ca(2+)- dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles. SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Probably localizes to different vesicles compared to CADPS. Enriched on vesicular structures in the parallel fiber terminal of granule cells that are distinct from synaptic vesicles. LEIVIMEVQGLKSVAPNRIVYCTMEVEGGEKLQTDQAEASRPQWGTQGDFNTTHPRPVVKVKLFTESTGVLALEDKELGRVV GDIQFCLSYNDYLSRLTVVVLRAKGLQLQEDRSVVSVFVKVSLMNHNKFVKCKRTSAVLGSVNPVYNETFSFKVDTNELDTASLSLVVLQTTEGNKSSPLGRVV CAPS_CAEBR Others 1 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense- core vesicles (By similarity). SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles (By similarity). Strongly enriched in synaptic fractions (By similarity). MEVVVMEVQGLKSIQPNKIVYCVMDVDGHKLATDHAEASKPKWDTQGDFTTKTPLPTVKVKLYTEVKSLVSFDDKELGKIM GDLQFCLSYNDYLSRLTVVVLRAKGLQLQEDRGVVSVFVKVSLMNHNKFVKCKRTSAVLGSVNPVYNETFSFKADANELDTASLSLVVLQITEGDKSYPLGRVV CAPS_CAEEL Others 1 FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense- core vesicles (By similarity). Specifically required to activate the neuronal G-alpha pathway. Functions with G-alpha proteins from the same motor neurons to regulate locomotion. SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles (By similarity). Strongly enriched in synaptic fractions. Often concentrated at or near active zones of motor neuron synapses. MEVVVMEVQGLKSVQPSKIVYCTMEVDGHKLQTDHAEASKPKWDTQGDFSTKNPLPVVKVKLYTEVKSMIAFEDKELGKVI GDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVF CAPS_DROME Others 1 " FUNCTION: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles. However, it probably also participate to small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering." " SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated to vesicles. Restricted to all classes of presynaptic termini independent of the ratio of vesicular content (DCVs versus SVs). Found in all identified classes of peripheral and central synapses. In the CNS, it is highly enriched in the synapse-dense neuropil, which lacks cell bodies. Present in all synapses in the neuropil where it precisely colocalizes with other pansynaptic markers. Similarly abundant in all classes of neuromuscular junction (NMJ) termini, including type I, II, and III NMJs, where it localizes to all 3 bouton types. Expressed at similar levels in boutons which contain primarily small clear glutamatergic vesicles, as well as boutons very highly enriched in large DCVs. It appears that neither bouton class contains a pure population of either SVs or DCVs, but only differs dramatically in the relative abundance of the vesicular classes. Thus, the level of expression does not correlate with the abundance of DCVs. Clearly present presynaptically and colocalizes exclusively with presynaptic markers." LEVIVMEVENGEKLQTDQAEASKPMWDTQGDFTTTHPLPVVKVKLYTENPGMLALEDKELGKVT AGKLTVVILEAKNLKKMDVGGLSDPYVKIVLMQGGKRLKKKKTSIKKCTLNPYYNESFSFEVPFEQIQKVSLMITVMDYDKLGSNDAIGRCL INP4A_HUMAN Human 1 " FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 3,4-bisphosphate." GLSLAGNIQDPDEPILEFSLACSELHTPSLDRKPNSFVAVSVTTPPQAFWTKHAQTEIIEGTNNPIFLSSIAFFQDSLINQMTQVKLSVYDVKDRSQGTMYLLGSGT AGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQIVVTVLDYDKIGKNDAIGKVF INP4A_MOUSE Mouse 1 " FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 1,4-bisphosphate. Involved in the regulation of megakaryocyte and fibroblast proliferation. Regulates cell growth downstream of transcription factor GATA-1." LEFSLACSELHTPSLDRKPNSFVAVSVTTPPQAFWTKHAQTEIIEGTNNPIFLSSIAFFQDSLINQMTQIKLSVYDVKDRSQGTMYLLGSGT AGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVF INP4A_RAT Others 1 " FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 1,4-bisphosphate." GLSLAGNIQDPDEPILEFSLACSELHTPSLDRKPNSFVAVSVTTPPQAFWTKHAQTEIIEGTNNPIFLSSIAFFQDSLINQMTQIKLSVYDVKDRSQGTMYLLGSGT GDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVF INP4B_HUMAN Human 1 " FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 1,4-bisphosphate." GDCQFTSIQKTPNEPQLEFILACKDLVAPVRDRKLNTLVQISVIHPVEQSLTRYSSTEIVEGTRDPLFLTGVTFPSEYPIYEETKIKLTVYDVKDKSHDTVRTSVLPEHKDPPPEVGRSFLGYAS GDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVF INP4B_MACFA Others 1 " FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 1,4-bisphosphate (By similarity)." GDCQFTSIQKTPNEPQLEFILACKDLVAPVRDRKLNTLVQISVIHPVEQSLTRYSSTEIVEGTRDPLFLTGVTFPSEYPIYEETKIKLTVYDVKDKSHDTVRTSVLPEHKDPPPEVGRSFLGYAS GDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKETTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVF INP4B_MOUSE Mouse 1 " FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 1,4-bisphosphate (By similarity)." EDIQFTSIQKIPNEPQLEFILACRDLVAPVSDRKLNTVVQISVIHPVEQTLTRYSSTEIVEGTKDPLFLTGVTFPPDYPIYEETRIKLTVYDVKDKSHDTRSFLGCAS GDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVF INP4B_PONPY Others 1 " FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 1,4-bisphosphate (By similarity)." GDCQFTSIQKTPNEPQLEFILACKDLVAPVRDRKLNTLVQISVIHPVEQSLTRYSSTEIVEGTRDPLFLTGVTFPSEYPIYEETKIKLTVYDVKDKSHDTVRTSVLPEHKDSPPEIGRSFLGYAS GDICTSLRYVPTAGKLTVCILEAKNLKKMDVGGLSDPYGKIHLMQNGKRLKKKKTTVKKKTLNPYFNESFSFEIPFEQIQKVQVVVTVLDYDKLGKNEAIGKIF INP4B_RAT Others 1 " FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4- trisphosphate and inositol 1,4-bisphosphate." QLEFILACKDLVAPVSDRKLNTVVQVSVIHPVEQTLTRYSSTEIVEGTKDPLFLTGVTFPSDYPIYEETRIKLTVYDVKDKPHDTIRTSVLPEHKDPPPEVARSFLGCASFKVGELLKSKEQLLS AGKLTVCILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTVKKKTLNPYFNESFSFEIPFEQIQKVQVVVTVLDYDKLGKNEAIGKIF PK3CA_BOVIN Others 1 " FUNCTION: Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2." NGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLAWGNIN AGKLTVCILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTVKKKTLNPYFNESFSFEIPFEQIQKVQVVVTVLDYDKLGKNEAIGKIF PK3CA_HUMAN Human 1 " FUNCTION: Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2." NGETSTKSLWVINRALRIKILCATYVNLNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLAWGNIN GELNFSLCYLPTAGRLTVTIIKASNLKAMDLTGFSDPYVKASLISEGRRLKKRKTSIKKNTLNPTYNEALVFDVAPESVENVGLSIAVVDYDCIGHNEVIGVCR PK3CA_MOUSE Mouse 1 " FUNCTION: Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2 with a preference for PtdIns(4,5)P2." NGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRLARLCLSICSVKGRKGAKEEHCPLAWGNIN GELNFSLCYLPTAGRLTVTIIKASNLKAMDLTGFSDPYVKASLISEGRRLKKRKTSIKKNTLNPTYNEALVFDVAPESVENVGLSIAVVDYDCIGHNEVIGVCR PLC1_CANAL Yeast 1 " FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes." RFNFEIISGHQLPKFPKDDYKDQAINPYISFEIIGAQDVQWDNNDSSPIAPTTSSSPFIRTTKIIRENGFNPNFNTKFSGSIITTTNDLIFIKFVVYASTSLNYPDYGENFPIAILVTKLNYLKQGYRY GELNFSLCYLPTAGLLTVTIIKASNLKAMDLTGFSDPYVKASLISEGRRLKKRKTSIKKNTLNPTYNEALVFDVAPESVENVGLSIAVVDYDCIGHNEVIGVCR PLDA1_ARATH Mouse 1 " FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action and response to stress, characterized by acidification of the cell." " SUBCELLULAR LOCATION: Cytoplasmic and membrane-associated. Found in vacuoles and also associated with plasma, microsomal and mitochondrial membranes and in clathrin-coated vesicles. Not found in chloroplast or nuclei. Activation increases association of preexisting enzyme with membranes. The distribution of this conventional PLD between membrane-associated and soluble fractions varied from organ to organ and is calcium-regulated." MAQHLLHGTLHATIYEVDALHGGGVRQGFLGKILANVEETIGVGKGETQLYATIDLQKARVGRTRKIKNEPKNPKWYESFHIYCAHLASDIIFTVKDDNPIGATLIGRAY GELLISLCYQSTTNTLTVVVLKARHLPKSDVSGLSDPYVKVNLYHAKKRISKKKTHVKKCTPNAVFNELFVFDIPCEGLEDISVEFLVLDSERGSRNEVIGQLV PLDA1_MAIZE Others 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes. MAQILLHGTLHATIFEAESLSNPHRATGGAPKFIRKLVEGIEDTVGVGKGATKIYATVDLEKARVGRTRMISNEPVNPRWYESFHIYCAHMAADVIFTVKIDNSIGASLIGRAY GELLVSLCYQSTTNTLTVVVLKARHLPKSDVSGLSDPYVKVNLYHAKKRISKKKTHVKKCTPNAVFNELFVFDIPCESLEEISVEFLVLDSERGSRNEVIGRLV PLDA1_ORYSA Others 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes. MAQMLLHGTLHATIFEAASLSNPHRASGSAPKFIRKFVEGIEDTVGVGKGATKVYSTIDLEKARVGRTRMITNEPINPRWYESFHIYCAHMASNVIFTVKIDNPIGATNIGRAY GELLVSLCYQSTTNTLTVVVLKARHLPKSDVSGLSDPYVKVNLYHAKKRISKKKTHVKKCTPNAVFNELFVFDIPCESLEEISVEFLVLDSERGSRNEVIGRLV PLDA1_TOBAC Others 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes. MAQILLHGTLHVTIYEVDNLQKEGGGHFFSKIKEHVEETIGFGKGTPAIYATVDLEKARVGRTRKIKNEPNNPRWYESFHIYCAHMASNVIFTVKDDNPIGATLIGRAY AGKLTVIVLEAKNLKKMDVGGLSDPYVKVHLLQGGKKVRKKKTTIKKNTLNPYYNEAFSFEVPCDQVQKVQVELTVLDYDKLGKNEAIGRVA PLDA1_VIGUN Others 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes. MAQILLHGTLHATIYEVDELHGGGGGNFFSKLKQNIEETVGIGKGVTKLYATIDLEKARVGRTRIIENETTNPKWNESFHIYCGHLASNIIFTVKDDNPIGATLIGRAY AGKLTVIVLEAKNLKKMDVGGLSDPYVKVHLLQGGKKVRKKKTTIKKNTLNPYYNEAFSFEVPCDQVQKVQVELTVLDYDKLGKNEAIGRVA PLDA2_ARATH Mouse 1 " FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes, including phytohormone action and response to stress, characterized by acidification of the cell." " SUBCELLULAR LOCATION: Cytoplasmic and membrane-associated. Found in vacuoles and also associated with plasma, microsomal and mitochondrial membranes and in clathrin-coated vesicles. Not found in chloroplast or nuclei. Activation increases association of preexisting enzyme with membranes. The distribution of this conventional PLD between membrane-associated and soluble fractions varied from organ to organ and is calcium-regulated." MEECLLHGRLHATIYEVDHLHAEGGRSGFLGSILANVEETIGVGKGETQLYATIDLEKARVGRTRKITKEPKNPKWFESFHIYCGHMAKHVIFTVKDANPIGATLIGRGY AGKLTVIVLEAKNLKKMDVGGLSDPYVKVHLLQGGKKVRKKKTTIKKNTLNPYYNEAFSFEVPCDQVQKVQVELTVLDYDKLGKNEAIGRVA PLDA2_ORYSA Others 1 FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes. MAHLLLHGTLEATILEADHLSNPTRATGAAPGIFRKFVEGFEDSLGLGKGATRLYATIDLGRARVGRTRVVDDEPVNPRWYEVFHIYCAHFAADVVFSVKAAQPIGATLIDRAY GEIMFSLCYLPTAGRLTLTVIKCRNLKAMDITGYSDPYVKVSLLCDGRRLKKKKTTIKKNTLNPVYNEAIIFDIPPENMDQVSLLISVMDYDRVGHNEIIGVCR PCLO_CHICK Others 1 FUNCTION: May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking (By similarity). SUBCELLULAR LOCATION: Concentrated at the presynaptic side of synaptic junctions (By similarity). NLIIHILQARNLAPRDNNGYSDPFVKVYLLPGRGQVMVVQNASAEYKRRTKYVQKSLNPEWNQTVIYKNISTEQLKKKTLEVTVWDYDRFSSNDFLGEVL VHVDITATPGTGDHKVTVKVIAINDLNWQTTAMFRPFVEVCILGPNLGDKKRKQGTKTKSNTWSPKYNETFQFILGKENRPGAYELHLSVKDYCFAREDRIIGMTV PCLO_HUMAN Human 1 FUNCTION: May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking (By similarity). SUBCELLULAR LOCATION: Concentrated at the presynaptic side of synaptic junctions (By similarity). KHGSSKLQINYDLGNLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGAEYKRRTKHVQKSLNPEWNQTVIYKSISMEQLKKKTLEVTVWDYDRFSSNDFLGEVL PCLO_MOUSE Mouse 1 FUNCTION: May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking. SUBCELLULAR LOCATION: Concentrated at the presynaptic side of synaptic junctions. LIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQVMVVQNASVEYKRRTKYVQKSLNPEWNQTVIYKSISMEQLMKKTLEVTVWDYDRFSSNDFLGEVL VHVDVTTTPGTGEHKVTVKVIAINDLNWQTTTMFRPFVEVCMLGPSLGDKKRKQGTKTKSNTWSPKYNETFQFILGNENRPGAYELHLSVKDYCFAREDRIIGMTV PCLO_RAT Others 1 FUNCTION: May act as a scaffolding protein involved in the organization of synaptic active zones and in synaptic vesicle trafficking (By similarity). SUBCELLULAR LOCATION: Concentrated at presynaptic side of synaptic junctions. NLIIHILQARNLVPRDNNGYSDPFVKVYLLPGRGQVMVVQNASAEYKRRTKYVQKSLNPEWNQTVIYKSISMEQLMKKTLEVTVWDYDRFSSNDFLGEVL GAVTVKASYRASEQKLRVELLSASSLLPLDSNGSSDPFVQLTLEPRHEFPELAARETQKHKKDLHPLFDETFEFLVPAEPCRKAGACLLLTVLDYDTLGADDLEGEAF RASA2_MOUSE Mouse 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) and phospholipids. SUBCELLULAR LOCATION: Cell membrane (Potential). ETGDEDSREVRVLQSLRGRIYEAKNLLPYLGPNKMRDCFCTINLDQEEVYRTQVVEKSLSPYFSEEFYFEIPRTFQYLSFYVYDKNVLQRDLRIGKVA RASA2_RAT Others 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4) and phospholipids. SUBCELLULAR LOCATION: Cell membrane (Potential). ETGDEDSREVRVLQSLRGRIYEAKNLLPYLGPNKMRDCFCTINLDQEEVYRTQVVEKSLSPYFSEEFYFEIPRTFQYLSFYVYDKNVLQRDLRIGKVA RASA3_BOVIN Others 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4). VFQSVKIKIGEAKNLPTYPGPNKMRDCYCTVNLDQEEVFRTKVVEKSLCPFYGEDFYCEIPRSFRHLSFYIFDRDVFRRDSIIGKVA RASA3_HUMAN Human 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) with high affinity. Might be a specific IP4 receptor. SUBCELLULAR LOCATION: Cell membrane. VFQSVKIKIGEAKNLPSYPGPSKMRDCYCTVNLDQEEVFRTKIVEKSLCPFYGEDFYCEIPRSFRHLSFYIFDRDVFRRDSIIGKVA RASA3_MOUSE Mouse 1 FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4). VFQSVRIKIGEAKNLPSYPGPNKMRDCYCTVNLDQEEVFRTKIVEKSLCPFYGEDFYCEIPRSFRHLSFYIFDRDVFRRDSIIGKVA RASL2_HUMAN Human 1 " FUNCTION: Ca(2+)-dependent Ras GTPase-activating protein, that switches off the Ras-MAPK pathway following a stimulus that elevates intracellular calcium." " SUBCELLULAR LOCATION: Localized to the cytosol as a result of its lack of phosphoinositide binding activity. Upon agonist-stimulated calcium mobilization, utilizes the C2A and C2B domains to associate with the plasma membrane." MAKRSSLYIRIVEGKNLPAKDITGSSDPYCIVKVDNEPIIRTATVWKTLCPFWGEEYQVHLPPTFHAVAFYVMDEDALSRDDVIGKVC RGS3_HUMAN Human 1 " FUNCTION: Down-regulates signaling from heterotrimeric G-proteins by increasing the GTPase activity of the alpha subunits, thereby driving them into their inactive GDP-bound form. Down-regulates G- protein-mediated release of inositol phosphates and activation of MAP kinases." SUBCELLULAR LOCATION: Long isoforms are cytoplasmic and associated with the plasma membrane. Short isoforms are nuclear. GAGQLRLSIDAQDRVLLLHIIEGKGLISKQPGTCDPYVKISLIPEDSRLRHQKTQTVPDCRDPAFHEHFFFPVQEEDDQKRLLVTVWNRASQSRQSGLIGCMS RIMS1_HUMAN Human 1 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short- term synaptic plasticity (By similarity). GQLSVKLWYDKVGHQLIVNVLQATDLPARVDGRPRNPYVKMYFLPDRSDKSKRRTKTVKKILEPKWNQTFVYSHVHRRDFRERMLEITVWDQPRVQEEESEFLGEIL RIMS2_HUMAN Human 1 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein. GQLSIKLWFDKVGHQLIVTILGAKDLPSREDGRPRNPYVKIYFLPDRSDKNKRRTKTVKKTLEPKWNQTFIYSPVHRREFRERMLEITLWDQARVREEESEFLGEIL RIMS2_MOUSE Mouse 1 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein. GQLSIKLWFDKVGHQLIVTILGAKDLPSREDGRPRNPYVKIYFLPDRSDKNKRRTKTVKKTLEPKWNQTFIYSPVHRREFRERMLEITLWDQARVREEESEFLGEIL RIMS2_RAT Others 1 FUNCTION: Rab effector involved in exocytosis. May act as scaffold protein. PRVQIKLWFDKVGHQLIVTILGAKDLPSREDGRPRNPYVKIYFLPDRSDKNKRRTKTVKKTLEPKWNQTFIYSPVHRREFRERMLEITLWDQARVREEESEFLGEIL RIMS3_HUMAN Human 1 FUNCTION: Regulates synaptic membrane exocytosis (By similarity). PMGDVHIAIMDRSGQLEVEVIEARGLTPKPGSKSLPATYIKVYLLENGACLAKKKTKMTKKTCDPLYQQALLFDEGPQGKVLQVIVWGDYGRMDHKCFMGMAQ RIMS3_MOUSE Mouse 1 FUNCTION: Regulates synaptic membrane exocytosis (By similarity). PMGDVHIAIMDRSGQLEVEVIEARGLTPKPGSKSLPATYIKAYLLENGACVAKKKTKVAKKTCDPLYQQALLFDEGPQGKVLQVIVWGDYGRMDHKCFMGMAQ RIMS3_RAT Others 1 FUNCTION: Regulates synaptic membrane exocytosis. PMGDVHIAIMDRSGQLEVEVIEARGLTPKPGSKSLPATYIKAYLLENGACVAKKKTKVAKKTCDPLYQQALLFDEGPQGKVLQVIVWGDYGRMDHKCFMGMAQ RIMS4_HUMAN Human 1 FUNCTION: Regulates synaptic membrane exocytosis (By similarity). PMGDVEIGLQERNGQLEVDIIQARGLTAKPGSKTLPAAYIKAYLLENGICIAKKKTKVARKSLDPLYNQVLLFPESPQGKVLQVIVWGNYGRMERKQFMGVAR RIMS4_MOUSE Mouse 1 FUNCTION: Regulates synaptic membrane exocytosis (By similarity). PMGDVEIGLQERNGQLEVDIIQARGLTAKPGSKTLPAAYIKAYLLENGVCIAKKKTKVARKSLDPLYNQVLLFPESPQGKVLQVIVWGNYGRMERKQFMGVAR RIMS4_RAT Others 1 FUNCTION: Regulates synaptic membrane exocytosis (By similarity). PMGGVEIGLQERNGQLEVDIIQARGLTAKPGSKTLPAAYIKAYLLENGVCIAKKKTKVARKSLDPLYNQVLLFPESPQGKVLQVIVWGNYGRMERKQFMGVAR RPGR1_BOVIN Others 1 FUNCTION: Essential for RPGR function and is also required for normal disk morphogenesis (By similarity). SUBCELLULAR LOCATION: Situated between the axonemal microtubules and the plasma membrane (By similarity). QKDEPRSGTWKNQNELRVEIIRCCGLRSRSLGAQPSPYVMYRFFTFSDHDTTIIPASSNPYFRDLARFPVLVTSDLDQYLRREALSVYVFDDEDSEPGSYLGRVQ RPGR1_MOUSE Mouse 1 FUNCTION: Essential for RPGR function and is also required for normal disk morphogenesis. SUBCELLULAR LOCATION: Situated between the axonemal microtubules and the plasma membrane. QSNESRSETWAPQNELRVEITRCCGLRSRRLGRQPSPYVMYRFFTFPDHDTIIIPASSNPYFKDQALFPVLVTSDLDQYLRREALSVYVFDDEDPEPGSYLGRAQ SY65_APLCA Others 1 FUNCTION: Acts as inhibitor of neurotransmitter release. Overexpression leads to a decrease in the amplitude of the excitatory postsynaptic potential in dissected cholinergic and glutaminergic neurons while depletion with antisense oligonucleotides leads to an increase. Overexpression of isoform 1 blocks the reversal of synaptic depression by serotonin in sensory neurons. SUBCELLULAR LOCATION: Synaptic vesicles and vesicle-like structures. GKLQFSLDYDFQKGELSVNVIQAADLPGMDMSGTSDPYVKVYLLPDKKKKYETKVHRKTLNPVFNESFTFKVPYAEVGSKILTFAVYDFDRFSKHDQIGQVQ RGS7_CAEEL Others 1 " FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunit egl-30 (G-alpha(q)), thereby driving it into its inactive GDP-bound form. May organize egl-30 into a stable multiprotein signaling complex, and thereby persistently inhibit egl-30 when triggered by calcium or phospholipids." CYRTRLVTNCNSPSFDESFYFTFSENCVRDLLIVTVYEMDSNNAEKKRILGCMT RPGR1_HUMAN Human 1 FUNCTION: Essential for RPGR function and is also required for normal disk morphogenesis (By similarity). SUBCELLULAR LOCATION: Situated between the axonemal microtubules and the plasma membrane (By similarity). LWIEITKCCGLRSRWLGTQPSPYAVYRFFTFSDHDTAIIPASNNPYFRDQARFPVLVTSDLDHYLRREALSIHVFDDEDLEPGSYLGRAR ABR_HUMAN Human 0 " FUNCTION: GTPase-activating protein for RAC and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them." QAFVLSSVELQVLTGSCFKLRTVHNIPVTSNKDDDESPGLYGFLHVIVHSAKGFKQSANLYCTLEVDSFGYFVSKAKTRVFRDTAEPKWDEEFEIELEGSQSLRILCYEKCYDKTKVNKDNNEIVDKIMGKGQ GEIMFSLCYLPTAGRLTLTVIKCRNLKAMDITGYSDPYVKVSLLCDGRRLKKKKTTIKKNTLNPVYNEAIIFDIPPENMDQVSLLISVMDYDRVGHNEIIGVCR BAIP3_HUMAN Human 0 EAIERVRKAKAPTYALKVSVMRAKNLLAKDPNGFSDPYCMLGILPASDATREPRAQKEQRFGFRKGSKRGGPLPAKCIQVTEVKSSTLNPVWKEHFLFEIEDVSTDQLHLDIWDHDDDVSLVEACRKLNEVIGLKG GEIMFSLCYLPTAGRLTLTVIKCRNLKAMDITGYSDPYVKVSLLCDGRRLKKKKTTIKKNTLNPVYNEAIIFDIPPENMDQVSLLISVMDYDRVGHNEIIGVCR BAIP3_MOUSE Mouse 0 EAIMRVKKAKAPTYALKVSVMRAKNLLAKDPNGFSDPYCMLGILPASSAPQESSGQKEQRFGFRKGSKRSSPLPAKCIQVTEVKNSTLNPVWKEHFLFEIDDVNTDQLHLDIWDHDDDVSLAEACRKLNEVIGLKG GELLLSLCYNPSANSIIVNIIKARNLKAMDIGGTSDPYVKVWLMYKDKRVEKKKTVTMKRNLNPNFNESFAFDIPTEKLRETTIIITVMDKDKLSRNDVIGKIY BCR_HUMAN Human 0 " FUNCTION: GTPase-activating protein for RAC1 and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. Displays serine/threonine kinase activity." RSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQ GELLLSLCYNPSANSIIVNIIKARNLKAMDIGGTSDPYVKVWLMYKDKRVEKKKTVTKKRNLNPIFNESFAFDIPTEKLRETTIIITVMDKDKLSRNDVIGKIY BUD2_YEAST Yeast 0 FUNCTION: Stimulates the GTPase activity of BUD1/RSR1. Participates in the regulation of bud-site selection. ITGSDKSNDMKISNSFKISILEANFQSINLNDKNNTPWSIFTDITAWGHTWARTSMVSNSSNPFWREEFQFNELLRLTNSYLEIKQLFHDLNNKKRLRLIGKIK GELCFSLRYVPSSGSLTVVVLEARGLNPGLAEAYVKIQLMLNQRKWKKSKTSSKKGTTTPYFNEAFVFLVPVSQLQSVDLVLAVWARGLQLRTEPVGKVL CPNE2_HUMAN Human 0 PAAGAAPMGPQYCVCKVELSVSGQNLLDRDVTSKSDPFCVLFTENNGRWIEYDRTETAINNLNPAFSKKFVLDYHFEEVQKLKFALFDQDKSSMRLDEHDFLGQFS GELCFSLRYVPSSGRLTVVILEARGLNPGLAEAYVKVQLILNQRKWKKNKTSSKKGTTNPYFNEAFVFLVPVSQLQSMDLVLAVWARGLQLLAEPVGKVLLGPRA CPNE2_MOUSE Mouse 0 PTAGAIPLGSQCCVCKVELSVSGQNLLDRDVTSKSDPFCVLFIEDNGRWMEFDRTETAVNNLNPAFSKKFVLDYHFEEVQKLKFALFDQDKSSAQLDEHDFLGQFS GELMFSLCYLPTAGRLTITIIKARNLKAMDITGASDPYVKVSLMCDGRRLKKRKTSTKRNTLNPVYNEAIVFDVPPENIDQIHLSIAVMDYDRVGHNEIIGVCQ DOC2G_MOUSE Mouse 0 " FUNCTION: May be involved in regulation of vesicular trafficking. In vitro, does not bind calcium and phospholipids." GTLEFTLLFDEDNSALHCTAHRAKGLKPPAAGSVDTYVKANLLPGASKASQLRTRTVRGTREPVWEETLTYHGFTCQDAGRKTLRLCVCEDSRLRRRRRGPPLGELR GELMFSLCYLPTAGRLTITIIKARNLKAMDITGASDPYVKVSLMCDGRRLKKRKTSTKRNTLNPVYNEAIVFDVPPESIDQIHLSIAVMDYDRVGHNEVIGVCQ DYSF_HUMAN Human 0 SUBCELLULAR LOCATION: Type II membrane protein (Probable). Localize