###################################################### ##### Sequences and other information for the ENTH 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. ###################################################### ENT1_SCHPO Yeast 1 " FUNCTION: Binds to membranes enriched in phosphatidylinositol-3,5- biphosphate (PtdIns(3,5)P2) and phosphatidylinositol-4,5- biphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin." SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Localizes in a punctate pattern. Colocalizes with F- actin. NFSKGYTDTQIKVRNATTNDSWGPSGTAMAEIAELTYDQNEMLEVMDIIDRRLNDKGKNWRHVFKSLSLLEYCLHNGSENVVRWAKDNIYIITTLREFVYVDDNGHDQGQNVRTKAKEITSLLEDEHALKEAR ENT1_YEAST Yeast 1 " FUNCTION: Binds to membranes enriched in phosphatidylinositol-3,5- biphosphate (PtdIns(3,5)P2) and phosphatidylinositol-4,5- biphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Negatively regulated via phosphorylation." SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Localizes in a punctate pattern. Found in the actin cortical patches. NLVKGYSSTQVLVRNATSNDNHQVSKDSLIELAEKSYDSADFFEIMDMLDKRLNDKGKYWRHIAKALTVIDYLIRFGSENCVLWCRENLYIIKTLKEFRHEDDEGIDQGQIVRVKAKELTALLSDDERLNEER ENT2_YEAST Yeast 1 " FUNCTION: Binds to membranes enriched in phosphatidylinositol-3,5- biphosphate (PtdIns(3,5)P2) and phosphatidylinositol-4,5- biphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin." " SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane protein. Localizes in a punctate pattern. Found in the actin cortical patches, although the majority is located at the cell periphery." NMMKGYSSTQVLVRDATANDSRTPSIDTLDDLAQRSYDSVDFFEIMDMLDKRLNDKGKYWRHVAKSLTVLDYLVRFGSENCVLWCRENFYVIKTLREFRHENESGFDEGQIIRVKAKELVSLLNDEERLREER EPN1_HUMAN Human 1 " FUNCTION: Binds to membranes enriched in phosphatidylinositol-4,5- biphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane; peripheral membrane protein (By similarity). Nucleus (By similarity). Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 (By similarity). NIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER EPN1_MOUSE Mouse 1 " FUNCTION: Binds to membranes enriched in phosphatidylinositol-4,5- biphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis." SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane; peripheral membrane protein (By similarity). Nucleus (By similarity). Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Detected in presynaptic nerve terminals and in Golgi stacks. May shuttle to the nucleus when associated with ZBTB16/ZNF145 (By similarity). NIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER EPN4_HUMAN Human 1 " FUNCTION: Binds to membranes enriched in phosphatidylinositol-4,5- biphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly." " SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm; perinuclear region. Membrane; peripheral membrane protein. Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans-Golgi network." NVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREER EPN4_MOUSE Mouse 1 " FUNCTION: Binds to membranes enriched in phosphatidylinositol-4,5- biphosphate (PtdIns(4,5)P2). May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly (By similarity)." " SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm; perinuclear region (By similarity). Membrane; peripheral membrane protein (By similarity). Found throughout the cell, with the exception of the cell surface. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the trans-Golgi network (By similarity)." NVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREER AP180_HUMAN Human 1 " FUNCTION: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats (By similarity)." SUBCELLULAR LOCATION: Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane (By similarity). QYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDF AP180_MOUSE Mouse 1 " FUNCTION: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats." SUBCELLULAR LOCATION: Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. QYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDF AP180_RAT Others 1 " FUNCTION: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats." SUBCELLULAR LOCATION: Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane. QYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDF ENT3_YEAST Yeast 1 " FUNCTION: Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol- 3,5-biphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB)." SUBCELLULAR LOCATION: Cytoplasmic. Associates with the trans Golgi network (TGN) and endosomal clathrin coats. NVVFNYTEMEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFTEKAGSEWRQIYKALQLLDYLIKHGSERFIDDTRNSINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNKIRAER ENT5_YEAST Yeast 1 " FUNCTION: Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol- 3,5-biphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB)." SUBCELLULAR LOCATION: Cytoplasmic. Found predominantly on endosomal structures. NVIVQYEPYQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEWRVVLKCLVVIEFLLLNVDTGDELNQIRSCLLTHKHILTREIAQFKVKFSNDGKMEIHERGIRKKGELILQYLEDSQFLKKER EPN1_RAT Others 1 " FUNCTION: Binds to membranes enriched in phosphatidylinositol-4,5- biphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis." SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; peripheral membrane protein. Nucleus. Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Colocalizes with clathrin at the Golgi complex. Detected in presynaptic nerve terminals and in synaptosomes. May shuttle to the nucleus when associated with ZBTB16/ZNF145. NIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREER EPN2_HUMAN Human 1 FUNCTION: Plays a role in the formation of clathrin-coated invaginations and endocytosis. " SUBCELLULAR LOCATION: Cytoplasm. In punctate structures throughout the cell, associated with clathrin-coated vesicles, and particularly concentrated in the region of the Golgi complex." NIVNNYSEAEIKVREATSNDPWGPSSSLMTEIADLTYNVVAFSEIMSMVWKRLNDHGKNWRHVYKALTLLDYLIKTGSERVAQQCRENIFAIQTLKDFQYIDRDGKDQGINVREKSKQLVALLKDEERLKAER EPN2_MOUSE Mouse 1 FUNCTION: Plays a role in the formation of clathrin-coated invaginations and endocytosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm (By similarity). In punctate structures throughout the cell and particularly concentrated in the region of the Golgi complex (By similarity). NIVNNYSEAEIKVREATSNDPWGPSSSLMTEIADLTYNVVAFSEIMSMVWKRLNDHGKNWRHVYKALTLLDYLIKTGSERVAQQCRENIFAIQTLKDFQYIDRDGKDQGINVREKSKQLVALLKDEERLKVER EPN2_RAT Others 1 FUNCTION: Plays a role in the formation of clathrin-coated invaginations and endocytosis. SUBCELLULAR LOCATION: Cytoplasm (By similarity). In punctate structures throughout the cell and particularly concentrated in the region of the Golgi complex (By similarity). NIVNSYSEAEIKVREATSNDPWGPSSSLMTEIADLTYNVVRFSEIMSMVWKRLNDHGKNWRHVYKALTLLDYLIKTGSERVAQQCRENIFAIQTLKDFQYIDRDGKDQGINVREKSKQLVALLKDEERLKVER HIP1R_HUMAN Human 1 " FUNCTION: Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton." " SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region (By similarity)." EREQFDKTQAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIREIGDLWGHLHDRYGQLVNVYTKLLLTKISFHLKHPQFP HIP1R_MOUSE Mouse 1 " FUNCTION: Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton." " SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region." EREQFDKTQAISISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLSSSSILSWKFCHVLHKVLRDGHPNVLHDYQRYRSNIREIGDLWGHLRDQYGHLVNIYTKLLLTKISFHLKHPQFP HIP1_HUMAN Human 1 FUNCTION: May play a functional role in the cell filament networks. SUBCELLULAR LOCATION: Cytoplasmic. Membrane-associated protein. ERESFERTQTVSINKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAVLCWKFCHVFHKLLRDGHPNVLKDSLRYRNELSDMSRMWGHLSEGYGQLCSIYLKLLRTKMEYHTKNPRFP PICAL_HUMAN Human 1 " FUNCTION: Assembly protein recruiting clathrin and adaptor protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction." SUBCELLULAR LOCATION: Clathrin-coated areas of the plasma membrane. Colocalized with clathrin in the Golgi area. QHSVTGSAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSYRQVAFDF PICA_CAEEL Others 1 " FUNCTION: Assembly protein recruiting clathrin and adaptor protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction. Required for the efficient targeting of the synaptic vesicle protein synaptobrevin." SUBCELLULAR LOCATION: Clathrin-coated areas of the plasma membrane. Colocalized with clathrin in the Golgi area. KHSLAGSQLGKTICKATTEEVMAPKKKHLDYLLHCTNEPNVSIPSMANLLIERTQNPNWTVVYKALITIHNIMCYGNERFSQYLASCNTTFNLTAFVDKVGGAGGYDMSTHVRRYAKYIGEKINTYRMCAFDF PICA_DROME Others 1 " FUNCTION: Assembly protein recruiting clathrin and adaptor protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction." SUBCELLULAR LOCATION: Clathrin-coated areas of the plasma membrane. Colocalized with clathrin in the Golgi area. RHSLAGQGLAKSVCKATTEECIGPKKKHLDYLVHCTNEPNVSIPHLANLLIERSQNANWVVVYKSLITTHHLMAYGNERFMQYLASSNSTFNLSSFLDKGTVQDGGMGVPGGRMGYDMSPFIRRYAKYLNEKSLSYRAMAFDF PICA_MOUSE Mouse 1 " FUNCTION: Assembly protein recruiting clathrin and adaptor protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction. Plays a crucial role in fetal and adult hematopoiesis, and normal prenatal and postnatal growth and viability." SUBCELLULAR LOCATION: Clathrin-coated areas of the plasma membrane. Colocalized with clathrin in the Golgi area (By similarity). QHSVTGSAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSYRQVAFDF PICA_RAT Others 1 " FUNCTION: Assembly protein recruiting clathrin and adaptor protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction (By similarity)." SUBCELLULAR LOCATION: Clathrin-coated areas of the plasma membrane. Colocalized with clathrin in the Golgi area (By similarity). QHSVTGSAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSYRQVAFDF EPN3_HUMAN Human 1 SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm; perinuclear region. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the cell periphery. Nucleus (Probable). May shuttle to the nucleus. NIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFTEVMGMLWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQER EPN3_MOUSE Mouse 1 SUBCELLULAR LOCATION: Cytoplasmic. Concentrated in the perinuclear region and associated with clathrin-coated vesicles close to the cell periphery. May shuttle to the nucleus (By similarity). NIVHNYSEAEIKVREATSNDPWGPPSSLMSEIADLTFNTVAFAEVMGMVWRRLNDSGKNWRHVYKALTLLDYLLKTGSERVAHQCRENLYTIQTLKDFQYIDRDGKDQGVNVREKVKQVMALLKDEERLRQER SLA2_SCHPO Yeast 1 FUNCTION: Required for cellular morphogenesis and polarization of the cortical cytoskeleton. Required for establishment of new polarized growth zones where it acts in actin organization. Involved plasma membrane internalization and is essential for fluid-phase endocytosis. SUBCELLULAR LOCATION: Cytoplasm. Localizes at cell ends during interphase and to the medial ring at cell division. MQSDASLMTSVRKATSIDETAPKRKHVRSCIIFTWDHHTARPFWTAIKVQPLLANEVQTFKALITIHRVLQEGHKSALVDSQSEKGWLKTCERQYDGESSPKGYSDLIRDYVDYLLDKLSFHAQHPEFN SLA2_YEAST Yeast 1 FUNCTION: Required for cellular morphogenesis and polarization of the cortical cytoskeleton. It might act in concert with proteins such as CDC42 and CDC43 to limit the region of cortical patch formation to the cortex of the bud. Required for the accumulation and/or maintenance of plasma membrane H(+)-ATPase on the cell surface. MSRIDSDLQKALKKACSVEETAPKRKHVRACIVYTWDHQSSKAVFTTLKTLPLANDEVQLFKMLIVLHKIIQEGHPSALAEAIRDRDWIRSLGRVHSGGSSYSKLIREYVRYLVLKLDFHAHHRGFN CAP10_ARATH Mouse 0 KVNSDYKELDIAIVKATNHVERPSKERYIRAIFMAISATRPRADVAYCIHALARRLSRTHNWAVALKTLIVIHRALREVDQTFHEEVINYSRSRSHMLNMSHFKDDSGPNAWAYSAWVRFYALFLEERLECFRVLKYDV CAP11_ARATH Mouse 0 YNEKAFFDIEVAVVRATSHDDCPVDDKTMHEILFLVSNTPGSIPFLAEQISRRLAKTRDCLVAGKTLLLFHRLLRGSSRSIEQQLHIAHTSGHLQIGCSWFMMSLDSRSFVFLQNYVAYLQERVGWIINQAGKL CAP12_ARATH Mouse 0 NSSYRNADLEAAIIKATSHDDSSVDYSNAHRVYKWIRSSPLNLKTLVYAISSRVNHTRSWIVALKSLMLLHGVLCCKVPSVVGEFRRLPFDLSDFSDGHSCLSKTWGFNVFVRTYFAFLHHYSSFLSDQIHRL CAP13_ARATH Mouse 0 KTSFRNPDLDSAIIHATSHDDSSVDYHNAHRVYKWIRSSPANLKPLVHALSSRVNRTRSWIVALKALMLVHGVLCCKVTSLQEIRRLPFDLSDFSDGHSRPSKTWGFNAFIRAYFSFLDQYSFFLSDQIRRR CAP14_ARATH Mouse 0 LITATDEKFTAAVIKATSHNDVSMDIENVQFIYRYIQSNPSSFKPIIRAVSLRVEHTRNWTVALKCLMLLHGLFFSGIMTVDSIGRLPFDLSGFGRRKSRFSRTGRFNIFVRAYFMFLDERSILYYNKNMIR CAP15_ARATH Mouse 0 SLIAADDILTAAVVKATSHDELSIDTESAQFIYRHVLSSPSSLKPLVSLISSRVKRTRSWAVALKGLMLMHGFFLCKSTVAESIGRLPFDLSSFGEGNSRIMSKSGGFNLFVRAYFAFLDRRSILFHDGNRHR CAP16_ARATH Mouse 0 NTKSKTLSFHLSVLRATTHDPSTPPGNRHLAVILSAGTGSRATASSAVESIMERLHTTGDACVALKSLIIIHHIVKHGRFILQDQLSVFPASGGRNYLKLSAFRDEKSPLMWELSSWVRWYALYLEHLLSTSRIMGFFI CAP17_ARATH Mouse 0 FGSTAVKYIHLALLKSTTRTPNKPPNSDYVSAVISYSNSRYAPAAFSAALWRLRVTKNAIVATKSLIVIHKLIKSSRDKFEGLGHGRNNLKLNEFSDKSSNLTLELSQWIRWYGQYLDRLSWVPKVLGSFP CAP18_ARATH Mouse 0 CSSVNAKTIDLALLKATSHTSNNPPSDKYVTFLQSTIDTCYGPDTVDAILHRLRVTTDVCVAAKCLILLHKMVKSESGYNGEDSLRNNINHRTLIYTQGGSNLKLNDLNVNSSRFTRELTPWVQWYKQYLDCYLSIAEVLGITP CAP1_ARATH Mouse 0 VASNMAPDLEVAIVKATSHDDDQSSDKYIREILSLTSLSRGYVHACVTSVSRRLKKTRDWIVALKALMLVHRLLNEGDPLFQEEILYATRRGTRILNMSDFRDEAHSSSWDHSAFVRTYASYLDQRLELALFERRGR CAP2_ARATH Mouse 0 VASNMAPDLEVAIVKATSHDDDPASEKYIREILNLTSLSRGYILACVTSVSRRLSKTRDWVVALKALMLVHRLLNEGDPIFQEEILYSTRRGTRMLNMSDFRDEAHSSSWDHSAFVRTYAGYLDQRLELALFERKSG CAP3_ARATH Mouse 0 GRSSSLTELEIAVVKATRHDDYPAEDKYIREILCLTSYSRNYVSACVATLSRRLNKTKNWSVALKTLILIQRLLTDGDRAYEQEIFFATRRGTRLLNMSDFRDASQSDSWDYSAFVRTYALYLDERLDYRMQGRRGK CAP4_ARATH Mouse 0 GRSASLSELDVAIVKATRHEEFPAEEKYIREILSLTSYSRSYINACVSTLSRRLNKTKCWTVALKTLILIQRLLGEGDQAYEQEIFFATRRGTRLLNMSDFRDVSRSNSWDYSAFVRTYALYLDERLDFRMQARHGK CAP5_ARATH Mouse 0 TGGGDLTTLEVAILKATSHDEEVPIDDRLVTEILGIISSKKSHAASCAAAIGRRIGRTRNWIVALKSLVLVLRIFQDGDPYFPREVLHAMKRGAKILNLSSFRDDSNSCPWDFTAFVRTFALYLDERLDCFLTGKLQR CAP6_ARATH Mouse 0 KVNSEFKDLDVAIVKATNHVESAPKERHIRRIFSATSVVQPRADVAYCIHALAKRLSKTRNWVVAIKVLIVIHRTLREGDPTFREELLNYSHRGHILRISNFKDDTSPLAWDCSAWIRTYALFLEERLECYRVLKYDI CAP7_ARATH Mouse 0 KVNSEFKDLDIAIVKATNHVESPPKERHVRKIFSATSVIQPRADVAYCIHALSKRLSKTRNWVVAMKVLIVIHRTLREGDPTFREELLNYSHRRHILRISNFKDDTSPLAWDCSAWVRTYALFLEERLECYRVLKYDI CAP8_ARATH Mouse 0 RVNSEYADLDVAIVKATNHVECPPKDRHLRKIFAATSVTRARADVAYCIHALSRRLHKTRNWTVALKTLIVIHRLLREGDPTFREELLNFSQRGRILQLSNFKDDSSPIAWDCSAWVRTYALFLEERLECFRVLKYDT CAP9_ARATH Mouse 0 RVNSDYAELDVAIVKATNHVECPPKDRHLRKIFLATSAIRPRADVAYCIHALSRRLHKTRNWTVALKALLVIHRLLRDGDPTFREELLNFSQKGRIMQISNFKDDSSPVAWDCSGWVRTYALFLEERLECFRVLKYDI ENT4_YEAST Yeast 0 FKSFIQSPTESKVKQATNEDETSGATGTLMNEISILTYSPKTVREIIQVIRKRLLLGQNRRNSHRNCIQVMKTLTLVSYLMNNGSNEFIKWLKGNMILIEILEDFQVQDPRDERKAEDIQKLSRNVLGLLQDDGLLEKQR SLAP2_CAEEL Others 0 AREVFVRAQLEAVQKAITKNEVPLKPKHARTIIVGTHKEKSSGIFWHTVGRIQLEKHPVLTWKFCHLVHKLLRDGHRKVPEETYRYVNRFTQLSQFWKHLNTSGYGPCIESYCKLLHDRVTFHNKYPVVP YCTB_SCHPO Yeast 0 YTSMEARVREATNNEPWGASTSLMMEIAQGTHNYSQLNEILPMIYRRFTEKTAEEWRQIYKALQLLEFLVKNGSERVVDDARAHQATIKMLRNFHYIDHRQKDQGLNVRTRAKELVELLNDSERI YG54_YEAST Yeast 0 MSSLYTKLVKGATKIKMAPPKQKYVDPILSGTSSARGLQEITHALDIRLSDTAWTIVYKALIVLHLMIQQGEKDVTLRHYSHNLDVFQLRKISHTTKWSSNDMRALQRYDEYLKTRCEEYGRLGMDH YHW1_YEAST Yeast 0 MTTYFKLVKGATKIKSAPPKQKYLDPILLGTSNEEDFYEIVKGLDSRINDTAWTIVYKSLLVVHLMIREGSKDVALRYYSRNLEFFDIENIRGSNGSASGDMRALDRYDNYLKVRCREFGKIKKDY