ID ATG20_ASHGO STANDARD; PRT; 577 AA. AC Q75B65; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 16-MAY-2006, entry version 16. DE Autophagy-related protein 20. GN Name=ATG20; OrderedLocusNames=ADL293W; OS Ashbya gossypii (Yeast) (Eremothecium gossypii). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=33169; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient RT Saccharomyces cerevisiae genome."; RL Science 304:304-307(2004). CC -!- FUNCTION: May be required for cytoplasm to vacuole transport (Cvt) CC and pexophagy (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; CC peripheral membrane protein (By similarity). Endosome; endosomal CC membrane; peripheral membrane protein (By similarity). Endosome CC and other perivacuolar punctate structures (By similarity). CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which CC is necessary for peripheral membrane localization of ATG20 to the CC perivacuolar punctate structures (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016817; AAS51627.1; -; Genomic_DNA. DR AGD; ADL293W; -. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Autophagy; Complete proteome; Membrane; Protein transport; Transport. FT CHAIN 1 577 Autophagy-related protein 20. FT /FTId=PRO_0000213819. FT DOMAIN 95 239 PX. SQ SEQUENCE 577 AA; 63967 MW; 26F8BA003E0D93E8 CRC64; MTEQSEHSNG GVCASSIQPA RNGGLCGHGG VGGVGEAEGD PVHTQIIQED NPFVEHGQSY VAPHSGGGRT SSGSSSSASL QEGLLAPPLA KSSAGEQGRV RILEASKVSE GQGRSYITYT ISYRDRVVRR RYSEFESLRK ILIKLFPMTL IPPIPEKQSL TSYGKSIAGS NANYVLPSEA AGCDLAVSVI NGSVNLNDQK MIRHRIRMLT SFLNRLLQNE EVTKTSIIGD FLDPNNANWN DVITTSATIS SLPKSVLQCN PLDPTNTTPA HASLPIPPLS SAPQLMGKDG VGTSTKPSAE DMEFSRIEYE YKKYEQLLHT GVYKYNRRIT RTMHELKQDL ADLSEAFAEF AVEQSKGGDL AELLSYLSNA NDEAAAVLDD LVGKIYYNIN EPLSEAVHIA GAARELIQYR RLKFAQRDML KKSLLGKEGH LKRLQEQEDD AKAIDQLVDQ HLGEGTRINL QRPSEASPNT YKRKLFSRFN KLANIVKETV TYQEQDPKVN IKTVQEDIEQ IKESLDVSAS DLDVITATIR DVQLPAFSRN RDKELYDILK NYSKYMKEYA AKNLEIWKDL RKQEENA // ID ATG20_CANAL STANDARD; PRT; 407 AA. AC Q59TN9; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 04-APR-2006, entry version 6. DE Autophagy-related protein 20. GN Name=ATG20; ORFNames=CaO19.1297, CaO19.8877; OS Candida albicans (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5476; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., RA Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., RA Davis R.W., Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). CC -!- FUNCTION: May be required for cytoplasm to vacuole transport (Cvt) CC and pexophagy (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; CC peripheral membrane protein (By similarity). Endosome; endosomal CC membrane; peripheral membrane protein (By similarity). Endosome CC and other perivacuolar punctate structures (By similarity). CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which CC is necessary for peripheral membrane localization to the CC perivacuolar punctate structures (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACQ01000138; EAK93844.1; -; Genomic_DNA. DR EMBL; AACQ01000139; EAK93812.1; -; Genomic_DNA. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Autophagy; Membrane; Protein transport; Transport. FT CHAIN 1 407 Autophagy-related protein 20. FT /FTId=PRO_0000213820. FT DOMAIN 164 340 PX. FT COMPBIAS 92 131 Asn-rich. FT COMPBIAS 256 280 Gly-rich. SQ SEQUENCE 407 AA; 45013 MW; 363F5038DAB68ACC CRC64; MSSVLRNQDN PPTISEVSST TKENTDNSNS KQEEKEKEKE ISSTIENPTF VDDEEDNNPF SHHGEGLTSF MTANSFNEGP NTKSDKRTTK ENNNSSSNNN RGDNNDDDDD DSLLLYNTSN NNKSNNVSRV NPMLKSTGEV FKTVNMNFES RVTKLLKPNT KIRIQITEAG NSNEGMSNSS KKYTVYTIKL INLEDPNNDI LTRRRYSDFE SLRDVLTKIF PLIVIPPIPP KNYFDFSMLN GLVGSNHENS SLSVAGSNGN SGGSGGGGAS GGAGSGSGNG SIITSPKTYS YINSTHLTKG KLIEHRKRLL TNFLNNCLEI KQIRSLEFFA KFLDPNANWG DEIALIQSQL PKSIYLSNPE NGLKTDPIYS NLPNPSNKNT ISFFKDNKKK LTKKTNKLLS NGSENHK // ID ATG20_CANGA STANDARD; PRT; 753 AA. AC Q6FR93; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 16-MAY-2006, entry version 14. DE Autophagy-related protein 20. GN Name=ATG20; OrderedLocusNames=CAGL0H10428g; OS Candida glabrata (Yeast) (Torulopsis glabrata). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5478; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- FUNCTION: May be required for cytoplasm to vacuole transport (Cvt) CC and pexophagy (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; CC peripheral membrane protein (By similarity). Endosome; endosomal CC membrane; peripheral membrane protein (By similarity). Endosome CC and other perivacuolar punctate structures (By similarity). CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which CC is necessary for peripheral membrane localization to the CC perivacuolar punctate structures (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR380954; CAG60184.1; -; Genomic_DNA. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Autophagy; Complete proteome; Membrane; Protein transport; Transport. FT CHAIN 1 753 Autophagy-related protein 20. FT /FTId=PRO_0000213821. FT DOMAIN 283 429 PX. SQ SEQUENCE 753 AA; 84641 MW; B68985FA37415151 CRC64; MGRSKRSKKK SLAHLQSDGK DKLSSEENIS RGSEVEESPE NFEEAQDYGD SLKDTDEQSD SITAIRSVTG GTASTITDLN NKFKSQELVD NEKVEINTKS TEEVGCKPST DHSTEALDEG HDTGISSTNK DDSDVRIIGD DNEDSEAIES VDIKGKVSSG ISDADVLKPQ EELVHTAILE NDNPFYDANK EISGSKKLDE KVNSVDSMAE TTKVNSGDSK QRMGDLVVRR SENLHNPNLD YEEEDEILVS NTDTNKHSKE SSSALNNANM KSFGNAVKSY TKKSGKHVRI LEAKKVSEGQ SRTFVAYFIK YNGHMVRRRY SDFESLRSIL VKLFPLMVIP PIPEKEGLKS YSKAIAGLKH AKYILPSEQT DSVDLSLSII DQSVSDKEEN IIRHRVRILT KFLNRLLDNT DISSTSLIED FLNPNNSNWN DFVTSSATFS MLPRNRLQAN PVDPTNTTRV HACLPIPNTS VALGKRDPEL FVSGNENDDT DGYILLEKEH KRYESIVNNT YKYNRRITKN FNEMKHDYDD LAAAFAELSN LDISSNPKHV DFCATFDKSS IAMQALVSNL YYNIDEPLNE AIYNTNAVTE LLMFRKLKAV QLYKVEKSLV GKVHELQKLE KGENKIESEP NQESLTSARR LSPIPAPQKL GGSFFNKISE IANKVKESVS YQELDVETQI SNLRKEIERL KETSAVTTKD MEVINDTICK EEVPKALKCG EKELEDILAS YASYMKTYAK QNLEYWKSIQ EAR // ID ATG20_DEBHA STANDARD; PRT; 625 AA. AC Q6BZE1; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 30-MAY-2006, entry version 14. DE Autophagy-related protein 20. GN Name=ATG20; OrderedLocusNames=DEHA0A02475g; OS Debaryomyces hansenii (Yeast) (Torulaspora hansenii). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Debaryomyces. OX NCBI_TaxID=4959; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 36239 / CBS 767 / IFO 0083 / IGC 2968 / JCM 1990; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- FUNCTION: May be required for cytoplasm to vacuole transport (Cvt) CC and pexophagy (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; CC peripheral membrane protein (By similarity). Endosome; endosomal CC membrane; peripheral membrane protein (By similarity). Endosome CC and other perivacuolar punctate structures (By similarity). CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which CC is necessary for peripheral membrane localization to the CC perivacuolar punctate structures (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR382133; CAG84380.1; -; Genomic_DNA. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Autophagy; Complete proteome; Membrane; Protein transport; Transport. FT CHAIN 1 625 Autophagy-related protein 20. FT /FTId=PRO_0000213822. FT DOMAIN 79 202 PX. SQ SEQUENCE 625 AA; 72087 MW; A4207DAA76E3208F CRC64; MNPNDNNLFG DIEQDNNPSF YGNQSFLRDP YGKSKQTCPP SVTSNGDPSI TNDDNNLAHN NDLVSNSIVL SKKIEQMVND PNLQINVISS ERMINSSVVA YSIELSSFDD NRMIVKRRYS EFKSLRDNLQ ILFPTLVIPP IPEKHTLFTY LINSIDNSKE LNIIETRKRC FANFLKDIIF DSNVALKSCV LVHKFLDPNY ELCWNNAVNE PPVSLIPNNL LLANPVNPTD QNGLYSLLPI VNGFELNSNI DNISSLHKLN EDLHKLNEQV HVFELRKEQN ERRHPSEPTT SLFTEIPISL IDFEKNFHQN IKVLTELNKL NSRSVKNFKS IINTLIELGG NLNNFSLQIH ELNTDSNALS SLIEKFGSTI DSNFLGYEAF LMNDIIPEWQ EPISQLVQYY LTSLQLIKFY KFKIIQYKLV YKLKFNKYQE LANISTNFES QLKLKDLRNL DIDSPSINEA IKKIELNQKR LKNRKISSKK SWYGLFGGNS KPTFNLREDL PALTIPSEGT GIRRERTPLV SDENMSYPVN PSANLENTNI DINSHYKHKI NQIEKELTKL DQLIDLTNTD ISTLTQELNL NFNDFLVRVE KKWLVIMLEF IKNGKQLFKD NLQNWNECKV FINDL // ID ATG20_KLULA STANDARD; PRT; 636 AA. AC Q6CNX6; DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 30-MAY-2006, entry version 14. DE Autophagy-related protein 20. GN Name=ATG20; OrderedLocusNames=KLLA0E09141g; OS Kluyveromyces lactis (Yeast) (Candida sphaerica). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=28985; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 2359 / IFO 1267 / NRRL Y-1140 / WM37; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- FUNCTION: May be required for cytoplasm to vacuole transport (Cvt) CC and pexophagy (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; CC peripheral membrane protein (By similarity). Endosome; endosomal CC membrane; peripheral membrane protein (By similarity). Endosome CC and other perivacuolar punctate structures (By similarity). CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which CC is necessary for peripheral membrane localization to the CC perivacuolar punctate structures (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR382125; CAG99450.1; -; Genomic_DNA. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Autophagy; Complete proteome; Membrane; Protein transport; Transport. FT CHAIN 1 636 Autophagy-related protein 20. FT /FTId=PRO_0000213823. FT DOMAIN 160 305 PX. SQ SEQUENCE 636 AA; 72225 MW; ED55D1FA454016D6 CRC64; MQINFEPMPN SVTHLENNSP SRLKNNKTVE EHKEHEPDLQ TQSEMRRESN GSPKDTAVTN QNGDQPHENV IHTQIIKKDN PFFNYMQDNV DGSDENGKND DDDENAKNAG SDDNEDQLLQ PNRRKNSKER RRSSVATSKD SSPDVPYNTL NHNASGMTKE GKKRAQILEA SKVSEGQGRT YIAYAIKYGD SIVKRRYSDF ESLRKVLVKL FPISLIPPIP EKQSLKSYGK AMTYSKSSYL LPTESGDSVD LSLSVINGPV TTNDEKLIRH RIRMLTSFLN RLLKNQEITK TSIVYDFLDP NNKNWNDLIT SSLTISSLPK SVLQCNPIDP TNTTKAHSYL PVPSSSTQLL ASKDNHSASD ADEFTKIEAE FKNYEQLIHS GLYKYSRATT KEVNYLREDL KGISSEFAQL STDETKNESG LAELLSHSSD AYGTLQEILE TLVGNLHYNI NEPLSECAHM ATAVRDLIHY RRLKLIQKDI LERTILYKRG QLIKFQQQEN DHKQIDNMVK EELGTNGAVN LENPAGPQSY SGKFINKFTQ LAIIIKDSVS YQEQDPAAAA RSLEKELIQL DETLKVATSD LVVISETLKN TELPNFIKER DEELTQIFKN YAKYMKENAT RNLEIWKELH NRIQEA // ID ATG20_YEAST STANDARD; PRT; 640 AA. AC Q07528; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAY-2006, entry version 37. DE Sorting nexin-42 (Autophagy-related protein 20) (Cytoplasm to vacuole DE targeting protein 20). GN Name=ATG20; Synonyms=CVT20, SNX42; OrderedLocusNames=YDL113C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c; RX MEDLINE=97313263; PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [2] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG17 AND SNX4, AND RP MUTAGENESIS OF TYR-193. RX PubMed=12048214; DOI=10.1074/jbc.M204736200; RA Nice D.C., Sato T.K., Stromhaug P.E., Emr S.D., Klionsky D.J.; RT "Cooperative binding of the cytoplasm to vacuole targeting pathway RT proteins, Cvt13 and Cvt20, to phosphatidylinositol 3-phosphate at the RT pre-autophagosomal structure is required for selective autophagy."; RL J. Biol. Chem. 277:30198-30207(2002). RN [3] RP NOMENCLATURE. RX MEDLINE=22912406; PubMed=14536056; DOI=10.1016/S1534-5807(03)00296-X; RA Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y., RA Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., RA Ohsumi Y.; RT "A unified nomenclature for yeast autophagy-related genes."; RL Dev. Cell 5:539-545(2003). RN [4] RP FUNCTION, AND INTERACTION WITH SNX4. RX PubMed=12554655; DOI=10.1093/emboj/cdg062; RA Hettema E.H., Lewis M.J., Black M.W., Pelham H.R.B.; RT "Retromer and the sorting nexins Snx4/41/42 mediate distinct retrieval RT pathways from yeast endosomes."; RL EMBO J. 22:548-557(2003). RN [5] RP SUBCELLULAR LOCATION. RX MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Required for cytoplasm to vacuole transport (Cvt) and CC pexophagy. Involved in proper sorting of the v-SNARE protein SNC1. CC -!- SUBUNIT: Forms a complex with SNX4 and ATG17. CC -!- INTERACTION: CC P47057:SNX4; NbExp=1; IntAct=EBI-36894, EBI-17610; CC P53039:YIP1; NbExp=1; IntAct=EBI-36894, EBI-25295; CC P53845:YNL263C; NbExp=1; IntAct=EBI-36894, EBI-28230; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; peripheral membrane CC protein. Endosome; endosomal membrane; peripheral membrane CC protein. Endosome and other perivacuolar punctate structures. CC -!- DOMAIN: The PX domain binds phosphatidylinositol 3-phosphate which CC is necessary for peripheral membrane localization of ATG20 to the CC perivacuolar punctate structures. CC -!- MISCELLANEOUS: Present with 358 molecules/cell. CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z74161; CAA98681.1; -; Genomic_DNA. DR PIR; S67656; S67656. DR IntAct; Q07528; -. DR Ensembl; YDL113C; Saccharomyces cerevisiae. DR GenomeReviews; Z71256_GR; YDL113C. DR SGD; S000002271; ATG20. DR LinkHub; Q07528; -. DR GO; GO:0016020; C:membrane; IPI. DR GO; GO:0008289; F:lipid binding; IMP. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0006914; P:autophagy; IDA. DR GO; GO:0006623; P:protein targeting to vacuole; IMP. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Coiled coil; Complete proteome; Protein transport; Transport; Vacuole. FT CHAIN 1 640 Sorting nexin-42. FT /FTId=PRO_0000213824. FT DOMAIN 140 301 PX. FT COILED 475 512 Potential. FT COILED 562 593 Potential. FT MUTAGEN 193 193 Y->A: Abolishes the intracellular FT punctate localization and decreases the FT cytoplasm to vacuole transport. SQ SEQUENCE 640 AA; 72546 MW; 160977A8BECB6D93 CRC64; MSDLNDVQEN AKLNSETRNT GKAEPPHGTT EYVAEAEISK NGVGSPKKSP KKGKVGKGDN NKVETELVHT ALLEKDNPFM EEGPTGFTKS ALLEIPGMRS HNLKNPNEDY EDDSEGLLPL NQESNAETCR TSLSGSINSM NGETSASEEP SVSNRKKSAR IHILEAKRVS EGQGRAYIAY VIQFENSTVQ RRYSDFESLR SILIRLFPMT LIPPIPEKQS IKNYGKSITG SSSKYLLPSE GSGSVDLSLS VIHASVNNSD EKLIRHRIRM LTEFLNKLLT NEEITKTSII TDFLDPNNHN WHEFVNSSST FSSLPKSILQ CNPLDPTNTT RIHAMLPIPG SSSQLLLNKE SNDKKMDKER SKSFTNIEQD YKQYENLLDN GIYKYNRRTT KTYHDLKSDY NEIGEVFAQF AHEQAQVGEL AEQLSYLSNA FSGSSISLEK LVGRLYYNIN EPLNESVHMA TSARELIKYR KLKYLQNEMI KKSLNSKRAQ LEKLEAQNNE YKDVDKIIDN EMSKSHTINL ERPNNNTGSG GKSYGGKLFN GFNKLASMVK DSVKYQETDP HTASINLKKE IEQLSESLEV TENDLEVISK VIKNDQLPKF SKEREVDLSE ILKHYSRYMR NYARQNLEIW KEVKRHQDFA // ID BEM1_YEAST STANDARD; PRT; 551 AA. AC P29366; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 21-MAR-2006, entry version 62. DE Bud emergence protein 1 (Suppressor of RHO3 protein 1). GN Name=BEM1; Synonyms=SRO1; OrderedLocusNames=YBR200W; ORFNames=YBR1412; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92168167; PubMed=1538785; DOI=10.1038/356077a0; RA Chenevert J., Corrado K., Bender A., Pringle J., Herskowitz I.; RT "A yeast gene (BEM1) necessary for cell polarization whose product RT contains two SH3 domains."; RL Nature 356:77-79(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=S288c; RX MEDLINE=95066384; PubMed=7975899; RA Mallet L., Bussereau F., Jacquet M.; RT "Nucleotide sequence analysis of an 11.7 kb fragment of yeast RT chromosome II including BEM1, a new gene of the WD-40 repeat family RT and a new member of the KRE2/MNT1 family."; RL Yeast 10:819-831(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c; RX MEDLINE=95112788; PubMed=7813418; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., RA Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., RA Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., RA Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., RA Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., RA Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., RA Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., RA Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., RA Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., RA Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., RA Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., RA van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., RA Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., RA Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [4] RP INTERACTION WITH BUD5. RX MEDLINE=91292524; PubMed=1905981; DOI=10.1016/0092-8674(91)90016-R; RA Chant J., Corrado K., Pringle J.R., Herskowitz I.; RT "Yeast BUD5, encoding a putative GDP-GTP exchange factor, is necessary RT for bud site selection and interacts with bud formation gene BEM1."; RL Cell 65:1213-1224(1991). RN [5] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [6] RP STRUCTURE BY NMR OF 472-551. RX PubMed=11483498; DOI=10.1093/emboj/20.15.3947; RA Terasawa H., Noda Y., Ito T., Hatanaka H., Ichikawa S., Ogura K., RA Sumimoto H., Inagaki F.; RT "Structure and ligand recognition of the PB1 domain: a novel protein RT module binding to the PC motif."; RL EMBO J. 20:3947-3956(2001). CC -!- FUNCTION: Necessary for cell polarization during vegetative CC growth. May link the cytoskeleton to morphogenic determinants on CC the cell surface. CC -!- SUBUNIT: Interacts with BUD5. CC -!- INTERACTION: CC Q03497:STE20; NbExp=3; IntAct=EBI-3508, EBI-18285; CC -!- MISCELLANEOUS: Present with 6490 molecules/cell. CC -!- SIMILARITY: Contains 1 OPR domain. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC -!- SIMILARITY: Contains 2 SH3 domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X63826; CAA45320.1; -; Genomic_DNA. DR EMBL; Z21487; CAA79687.1; -; Genomic_DNA. DR EMBL; Z36069; CAA85162.1; -; Genomic_DNA. DR PIR; S23400; S23400. DR PDB; 1IP9; NMR; A=472-551. DR PDB; 1IPG; NMR; A=472-551. DR IntAct; P29366; -. DR GermOnline; 138743; -. DR Ensembl; YBR200W; Saccharomyces cerevisiae. DR GenomeReviews; Y13134_GR; YBR200W. DR SGD; S000000404; BEM1. DR BioCyc; SCER-S28-01:SCER-S28-01-000467-MONOMER; -. DR LinkHub; P29366; -. DR GO; GO:0005935; C:bud neck; IDA. DR GO; GO:0005934; C:bud tip; IDA. DR GO; GO:0000131; C:incipient bud site; IDA. DR GO; GO:0043332; C:mating projection tip; TAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0000753; P:cellular morphogenesis during conjugation w...; IGI. DR GO; GO:0030468; P:establishment of cell polarity (sensu Fungi); TAS. DR InterPro; IPR000108; Neu_cyt_fact_2. DR InterPro; IPR000270; OPR_PB1. DR InterPro; IPR001683; PX. DR InterPro; IPR001452; SH3. DR Pfam; PF00564; PB1; 1. DR Pfam; PF00787; PX; 1. DR Pfam; PF00018; SH3_1; 2. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 1. DR SMART; SM00666; PB1; 1. DR SMART; SM00312; PX; 1. DR SMART; SM00326; SH3; 2. DR PROSITE; PS50195; PX; 1. DR PROSITE; PS50002; SH3; 2. KW 3D-structure; Complete proteome; Cytoskeleton; Repeat; SH3 domain. FT CHAIN 1 551 Bud emergence protein 1. FT /FTId=PRO_0000064908. FT DOMAIN 72 132 SH3 1. FT DOMAIN 155 217 SH3 2. FT DOMAIN 278 404 PX. FT DOMAIN 478 551 OPR. FT STRAND 470 470 FT STRAND 479 483 FT STRAND 485 485 FT TURN 486 487 FT STRAND 490 494 FT STRAND 496 496 FT HELIX 500 511 FT TURN 512 512 FT STRAND 513 514 FT STRAND 516 520 FT STRAND 523 525 FT STRAND 528 528 FT STRAND 532 532 FT HELIX 533 541 FT TURN 542 543 FT STRAND 546 550 SQ SEQUENCE 551 AA; 61605 MW; FB6C525AE9A19181 CRC64; MLKNFKLSKR DSNGSKGRIT SADISTPSHD NGSVIKHIKT VPVRYLSSSS TPVKSQRDSS PKNRHNSKDI TSPEKVIKAK YSYQAQTSKE LSFMEGEFFY VSGDEKDWYK ASNPSTGKEG VVPKTYFEVF DRTKPSSVNG SNSSSRKVTN DSLNMGSLYA IVLYDFKAEK ADELTTYVGE NLFICAHHNC EWFIAKPIGR LGGPGLVPVG FVSIIDIATG YATGNDVIED IKSVNLPTVQ EWKSNIARYK ASNISLGSVE QQQQQSITKP QNKSAKLVDG ELLVKASVES FGLEDEKYWF LVCCELSNGK TRQLKRYYQD FYDLQVQLLD AFPAEAGKLR DAGGQWSKRI MPYIPGPVPY VTNSITKKRK EDLNIYVADL VNLPDYISRS EMVHSLFVVL NNGFDREFER DENQNNIKTL QENDTATFAT ASQTSNFAST NQDNTLTGED LKLNKKLSDL SLSGSKQAPA QSTSGLKTTK IKFYYKDDIF ALMLKGDTTY KELRSKIAPR IDTDNFKLQT KLFDGSGEEI KTDSQVSNII QAKLKISVHD I // ID KS6C1_HUMAN STANDARD; PRT; 1066 AA. AC Q96S38; Q8TDD3; Q9NSF4; Q9UL66; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 30-MAY-2006, entry version 25. DE Ribosomal protein S6 kinase delta-1 (EC 2.7.11.1) (52 kDa ribosomal DE protein S6 kinase) (Ribosomal S6 kinase-like protein with two PSK DE domains 118 kDa protein) (SPHK1-binding protein). GN Name=RPS6KC1; Synonyms=RPK118; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH SPHK1 RP AND PHOSPHATIDYLINOSITOL 3-PHOSPHATE, AND SUBCELLULAR LOCATION. RX MEDLINE=22194308; PubMed=12077123; DOI=10.1074/jbc.M201442200; RA Hayashi S., Okada T., Igarashi N., Fujita T., Jahangeer S., RA Nakamura S.; RT "Identification and characterization of RPK118, a novel sphingosine RT kinase-1-binding protein."; RL J. Biol. Chem. 277:33319-33324(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Guo J.H., Yu L.; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Brain; RG Human chromosome 1 international sequencing consortium; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 598-1066. RX MEDLINE=20021769; PubMed=10552933; DOI=10.1006/geno.1999.5963; RA Zhang H., Yu L., Mao N., Fu Q., Tu Q., Gao J., Zhao S.; RT "Cloning, characterization, and chromosome mapping of RPS6KC1, a novel RT putative member of the ribosome protein S6 kinase family, to RT chromosome 12q12-q13.1."; RL Genomics 61:314-318(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 683-1066. RC TISSUE=Amygdala; RG The German cDNA consortium; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May be involved in transmitting sphingosine-1 phosphate CC (SPP)-mediated signaling into the cell. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with SPHK1 and phosphatidylinositol 3- CC phosphate. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane-associated; also found CC in some small dot-like or ring-shaped early endosome structures. CC -!- TISSUE SPECIFICITY: Highly expressed in testis, skeletal muscle, CC brain, heart, placenta, kidney and liver and weakly expressed in CC thymus, small intestine, lung and colon. CC -!- DOMAIN: The first protein kinase domain appears to be a CC pseudokinase domain as it does not contain the classical CC characteristics, such as the ATP-binding motif, ATP-binding site CC and active site. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. S6 CC kinase subfamily. CC -!- SIMILARITY: Contains 1 MIT domain. CC -!- SIMILARITY: Contains 2 protein kinase domains. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC -!- CAUTION: Instead of Lys-820, Arg-820 is found at the binding site. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB070706; BAB63956.1; -; mRNA. DR EMBL; AF477978; AAL84818.1; -; mRNA. DR EMBL; AL645860; CAH70703.1; -; Genomic_DNA. DR EMBL; AL512449; CAH70703.1; JOINED; Genomic_DNA. DR EMBL; AL583826; CAH70703.1; JOINED; Genomic_DNA. DR EMBL; AL512449; CAH71999.1; -; Genomic_DNA. DR EMBL; AL583826; CAH71999.1; JOINED; Genomic_DNA. DR EMBL; AL645860; CAH71999.1; JOINED; Genomic_DNA. DR EMBL; AL583826; CAH73804.1; -; Genomic_DNA. DR EMBL; AL512449; CAH73804.1; JOINED; Genomic_DNA. DR EMBL; AL645860; CAH73804.1; JOINED; Genomic_DNA. DR EMBL; BC104769; AAI04770.1; -; mRNA. DR EMBL; AF037447; AAF13027.1; -; mRNA. DR EMBL; AL356893; CAB92850.1; ALT_INIT; mRNA. DR UniGene; Hs.591416; -. DR HSSP; Q08826; 1OCS. DR Ensembl; ENSG00000136643; Homo sapiens. DR HGNC; HGNC:10439; RPS6KC1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. DR PROSITE; PS50195; PX; 1. KW ATP-binding; Kinase; Membrane; Nucleotide-binding; Repeat; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 1066 Ribosomal protein S6 kinase delta-1. FT /FTId=PRO_0000233127. FT DOMAIN 8 132 PX. FT DOMAIN 277 305 MIT. FT DOMAIN 344 445 Protein kinase 1. FT DOMAIN 794 1056 Protein kinase 2. FT NP_BIND 801 809 ATP (By similarity). FT ACT_SITE 929 929 Proton acceptor (By similarity). FT BINDING 820 820 ATP (By similarity). FT CONFLICT 35 35 R -> G (in Ref. 1). FT CONFLICT 250 250 A -> V (in Ref. 1). FT CONFLICT 1065 1065 Missing (in Ref. 5). SQ SEQUENCE 1066 AA; 118682 MW; 670EE5965F3B8274 CRC64; MTSYRERSAD LARFYTVTEP QRHPRGYTVY KVTARVVSRR NPEDVQEIIV WKRYSDFKKL HKELWQIHKN LFRHSELFPP FAKGIVFGRF DETVIEERRQ CAEDLLQFSA NIPALYNSKQ LEDFFKGGII NDSSELIGPA EAHSDSLIDT FPECSTEGFS SDSDLVSLTV DVDSLAELDD GMASNQNSPI RTFGLNLSSD SSALGAVASD SEQSKTEEER ESRSLFPGSL KPKLGKRDYL EKAGELIKLA LKKEEEDDYE AASDFYRKGV DLLLEGVQGE SSPTRREAVK RRTAEYLMRA ESISSLYGKP QLDDVSQPPG SLSSRPLWNL RSPAEELKAF RVLGVIDKVL LVMDTRTEQT FILKGLRKSS EYSRNRKTII PRCVPNMVCL HKYIISEESV FLVLQHAEGG KLWSYISKFL NRSPEESFDI KEVKKPTLAK VHLQQPTSSP QDSSSFESRG SDGGSMLKAL PLKSSLTPSS QDDSNQEDDG QDSSPKWPDS GSSSEEECTT SYLTLCNEYG QEKIEPGSLN EEPFMKTEGN GVDTKAIKSF PAHLAADSDS PSTQLRAHEL KFFPNDDPEA VSSPRTSDSL SRSKNSPMEF FRIDSKDSAS ELLGLDFGEK LYSLKSEPLK PFFTLPDGDS ASRSFNTSES KVEFKAQDTI SRGSDDSVPV ISFKDAAFDD VSGTDEGRPD LLVNLPGELE STREAAAMGP TKFTQTNIGI IENKLLEAPD VLCLRLSTEQ CQAHEEKGIE ELSDPSGPKS YSITEKHYAQ EDPRMLFVAA VDHSSSGDMS LLPSSDPKFQ GLGVVESAVT ANNTEESLFR ICSPLSGANE YIASTDTLKT EEVLLFTDQT DDLAKEEPTS LFQRDSETKG ESGLVLEGDK EIHQIFEDLD KKLALASRFY IPEGCIQRWA AEMVVALDAL HREGIVCRDL NPNNILLNDR GHIQLTYFSR WSEVEDSCDS DAIERMYCAP EVGAITEETE ACDWWSLGAV LFELLTGKTL VECHPAGINT HTTLNMPECV SEEARSLIQQ LLQFNPLERL GAGVAGVEDI KSHPFFTPVD WAELMR // ID KS6C1_MOUSE STANDARD; PRT; 1056 AA. AC Q8BLK9; Q3UDY3; Q6PDY4; Q8BMQ5; Q8BX49; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 30-MAY-2006, entry version 32. DE Ribosomal protein S6 kinase delta-1 (EC 2.7.11.1) (52 kDa ribosomal DE protein S6 kinase). GN Name=Rps6kc1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-1056 (ISOFORM 3). RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, Ovary, and Uterus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 436-1056 (ISOFORM 1). RC STRAIN=C57BL/6; TISSUE=Brain, and Cerebellum; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May be involved in transmitting sphingosine-1 phosphate CC (SPP)-mediated signaling into the cell (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Interacts with SPHK1 and phosphatidylinositol 3-phosphate CC (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane-associated; also found CC in some small dot-like or ring-shaped early endosome structures CC (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8BLK9-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=2; CC IsoId=Q8BLK9-2; Sequence=VSP_018043, VSP_018044, VSP_018050, CC VSP_018051; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q8BLK9-3; Sequence=VSP_018046, VSP_018048, VSP_018049; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q8BLK9-4; Sequence=VSP_018045, VSP_018047; CC Note=No experimental confirmation available; CC -!- DOMAIN: The first protein kinase domain appears to be a CC pseudokinase domain as it does not contain the classical CC characteristics, such as the ATP-binding motif, ATP-binding site CC and active site. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. S6 CC kinase subfamily. CC -!- SIMILARITY: Contains 1 MIT domain. CC -!- SIMILARITY: Contains 2 protein kinase domains. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK030313; BAC26894.1; -; mRNA. DR EMBL; AK044809; BAC32101.1; -; mRNA. DR EMBL; AK049003; BAC33510.1; ALT_INIT; mRNA. DR EMBL; AK149858; BAE29128.1; -; mRNA. DR EMBL; BC058403; AAH58403.1; -; mRNA. DR UniGene; Mm.220912; -. DR Ensembl; ENSMUSG00000037581; Mus musculus. DR MGI; MGI:2443419; Rps6kc1. DR GO; GO:0007242; P:intracellular signaling cascade; RCA. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. DR PROSITE; PS50195; PX; 1. KW Alternative splicing; ATP-binding; Kinase; Membrane; KW Nucleotide-binding; Repeat; Serine/threonine-protein kinase; KW Transferase. FT CHAIN 1 1056 Ribosomal protein S6 kinase delta-1. FT /FTId=PRO_0000233128. FT DOMAIN 8 132 PX. FT DOMAIN 276 304 MIT. FT DOMAIN 343 444 Protein kinase 1. FT DOMAIN 789 1046 Protein kinase 2. FT NP_BIND 795 803 ATP (By similarity). FT ACT_SITE 919 919 Proton acceptor (By similarity). FT BINDING 823 823 ATP (By similarity). FT VAR_SEQ 36 47 Missing (in isoform 2). FT /FTId=VSP_018043. FT VAR_SEQ 89 158 Missing (in isoform 2). FT /FTId=VSP_018044. FT VAR_SEQ 279 336 ESSPTRREAVKRRTAEYLMRAESICSLRAAPQLHTGPQPPG FT SLSSRPPWSLRSPAEEL -> KVRQCHHWLESLGSLQKSER FT NLEKPSHTRAQQDIASPLVTKITKSHHLIICRSVHSSK FT (in isoform 4). FT /FTId=VSP_018045. FT VAR_SEQ 317 347 Missing (in isoform 3). FT /FTId=VSP_018046. FT VAR_SEQ 337 1056 Missing (in isoform 4). FT /FTId=VSP_018047. FT VAR_SEQ 932 947 HIQLTYFSRWSEVEDS -> QELSQMHFFLFAVASN (in FT isoform 3). FT /FTId=VSP_018048. FT VAR_SEQ 948 1056 Missing (in isoform 3). FT /FTId=VSP_018049. FT VAR_SEQ 961 961 E -> G (in isoform 2). FT /FTId=VSP_018050. FT VAR_SEQ 962 1056 Missing (in isoform 2). FT /FTId=VSP_018051. FT CONFLICT 855 857 GSE -> DSD (in Ref. 2; AAH58403). FT CONFLICT 855 855 G -> D (in Ref. 1; BAC33510). SQ SEQUENCE 1056 AA; 115712 MW; 315E6BB9926E4F42 CRC64; MTSPWGHSAD LARFYTVTEP QRHPRGYTVY KVTARVVSRR NPEDVQEIIV WRRYSDFKKL HRELWQIHRN AFRHSELFPP FAKGTVFGRF DKTVIEERRQ CAEDLLQFSA NIPALYNSRQ LQDFFKGGVI SDGSELIGPA EAYPDSPANA FPECGTEGFS SDSDLLSLTV DADSLAEVDD GMASRQGSPS RTFGLSLSTD SSAVGAVASD SEPSRVEDRE SRSLFPSSLK PRLGRRDYLE KAGELIKLAL KKEEEDDYEA ASDFYRKGVD LLLEGVQGES SPTRREAVKR RTAEYLMRAE SICSLRAAPQ LHTGPQPPGS LSSRPPWSLR SPAEELKAFR VLGVIDKVLL VMDTRTEQTF ILKGLRKSSE CSRNRKTIIP RCVPNMVCLH TYIISEESVF LVLQRAEGGK LWSYISKFLN RSSQESLDIK EGRPSMPPRV CLQQPSASPQ GGSSFESRGS DTGSMLKALP LKTSLTPSSQ DDSNQEDDGQ PSSPKWLDSG SSSEDECTAG YLTLCNEYGQ EKMDLVSLSE ESVMQPEGDK ADTQAVSSPA SLATGSVSPS THLRVFSGGE DLEAVSSPPT SESLSRSKNS PMEFFRIDSK DSTSELLGLD FGEKLHSLKP EPLKALFTLE DGDSPSQSLD PGESKRESEA QDSVSRGSDD SVPVISFKEA AAEAISGAEE GRPDLLVNLP GELQPTKEAS AMDPKFSQAS AGRLDSKLLE APDVLCLRLS SEQCHGLGPE GPEELSDPTE FCPGGVIPEH DAQADPGVLF EAAVDHRSSP DQFLFSSLRS ESDRLGQVEV VVTAQALQES LFHISSPCSG ANKEHSAYAD TATSEEVLLF TEPTKEEANS LFQRGSEAQE RGVGAGEADK EIHQIFEDLD KRLAASSRFF IPEGCIQRWA AEMVVALDAL HREGIVCRDL NPNNILLNDG GHIQLTYFSR WSEVEDSCDS DAVARMYCAP EVGAVTEETE ACDWWSLGAV LFELLTGKTL VECHPAGINT HTTLNMPGCV SEEARSLIQQ LLQFNPMERL GAGVAGVEDI KSHPFFTPVD WAELTR // ID MDM1_YEAST STANDARD; PRT; 1127 AA. AC Q01846; Q04196; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 3. DT 30-MAY-2006, entry version 47. DE Structural protein MDM1. GN Name=MDM1; OrderedLocusNames=YML104C; ORFNames=YM8339.15C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c / AB972; RX MEDLINE=97313268; PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., RA Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., RA Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome RT XIII."; RL Nature 387:90-93(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 633-1127, FUNCTION, AND RP SUBCELLULAR LOCATION. RX MEDLINE=92332595; PubMed=1378448; DOI=10.1083/jcb.118.2.385; RA McConnell S.J., Yaffe M.P.; RT "Nuclear and mitochondrial inheritance in yeast depends on novel RT cytoplasmic structures defined by the MDM1 protein."; RL J. Cell Biol. 118:385-395(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 874-1127. RA Stirling C.J.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [4] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Essential for mitotic growth. Mediates organelle CC inheritance. CC -!- INTERACTION: CC P40073:SSU81; NbExp=1; IntAct=EBI-10626, EBI-18140; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Present with 784 molecules/cell. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC -!- SIMILARITY: Contains 1 PXA domain. CC -!- CAUTION: Ref.2 sequence differs from that shown due to a CC frameshift in position 638. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X80835; CAA56793.1; -; Genomic_DNA. DR EMBL; Z49210; CAA89114.1; ALT_INIT; Genomic_DNA. DR EMBL; X66371; CAA47014.1; ALT_FRAME; Genomic_DNA. DR EMBL; X65783; CAA46664.1; -; Genomic_DNA. DR PIR; S47445; S47445. DR IntAct; Q01846; -. DR GermOnline; 142638; -. DR Ensembl; YML104C; Saccharomyces cerevisiae. DR GenomeReviews; Z71257_GR; YML104C. DR SGD; S000004572; MDM1. DR BioCyc; SCER-S28-01:SCER-S28-01-004476-MONOMER; -. DR LinkHub; Q01846; -. DR GO; GO:0005737; C:cytoplasm; TAS. DR GO; GO:0005882; C:intermediate filament; TAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS. DR GO; GO:0000001; P:mitochondrion inheritance; IDA. DR GO; GO:0007005; P:mitochondrion organization and biogenesis; TAS. DR GO; GO:0007097; P:nuclear migration; TAS. DR InterPro; IPR001683; PX. DR InterPro; IPR003114; PX_assoc. DR Pfam; PF00787; PX; 1. DR Pfam; PF02194; PXA; 1. DR SMART; SM00312; PX; 1. DR SMART; SM00313; PXA; 1. DR PROSITE; PS50195; PX; 1. DR PROSITE; PS51207; PXA; 1. KW Coiled coil; Complete proteome. FT CHAIN 1 1127 Structural protein MDM1. FT /FTId=PRO_0000096330. FT DOMAIN 85 273 PXA. FT DOMAIN 782 905 PX. FT COILED 705 762 Potential. FT CONFLICT 635 635 H -> D (in Ref. 2). FT CONFLICT 772 772 Q -> R (in Ref. 2). FT CONFLICT 899 899 T -> I (in Ref. 2). FT CONFLICT 1063 1063 R -> K (in Ref. 2). FT CONFLICT 1081 1081 T -> S (in Ref. 2). FT CONFLICT 1096 1096 G -> R (in Ref. 2). SQ SEQUENCE 1127 AA; 129981 MW; 7C9177B87FDAF512 CRC64; MPKFPQFRLI LVLFYLISMI QWSVITFSLG FFLNVCIFAY FVFFKSLPDL PKPQPRFVDI VPESSNTVDV DKELKSVEGL IQDGNAQIGK ELESIVNLII KDFVQPWFTK IDKNSDAEFL KVIKWRLLQT LLVVKDKLMK NDSASLIVLK LLPIFNKHFS TFCDAREAVL SDLTLERHKS ANIDLQIAVE FNKNYKIHKS LSLKPNALQK EIEKSIRKTV IGLLPHLFDN DELDSLLVFT LMTEVLTTCI ISPLIFKFTD PDSWNLRIVS LSQNYFEEKH KVHKIRRMLS KELQDHRKVM NDVANKDVGE PSSEKLELNA EYTGKQFEHY LNQLDSLLDL SDIKYVAYSL ALKIYQLKEN EHLTKENLKY KKRLLLSLNL IESKLSFPGS EIDTASKKLA REANYPDLNM DNGIVLKEMA SFLTSITLKD IVDDSEFLPF FESFLGSVPE TQGSTFLEYS QTIESFKNPL EDATSEDIIS GYSGISTMQL QEISSKFFHN NNLQNMKLLD EGLVKNIILF RNSFQINNDE DTFILARKSV LLLQTEAIKY LDDRFLPLFK KTPSFLKMLS TSHIISTDIY AHFLSRIGGV NNPEQNKIIK DNVKTDFMNP VRIFANPGIT DALDNIVNGS GSKPHKSRIS SNPRYSQLFG SENDNIFKDK LFDDENDNTS EISVVEDQLD HPRNMEKVSV SSGNSGLNPS QFYGSNNFRD NIASLTISID QIEKELELLR HLILKADLTN NQMQLKILKK SQRTLLKELE MKELLKQQYM VQENGNSLFR KTKIYIRSYF SENSSNGLKE ITYYIINIHH FNNGQVSSWD MARRYNEFFE LNTYLKKNFR DLMRQLQDLF PSKVKMSLKY HVTKTLLYEE RKQKLEKYLR ELLSISEICE DNIFRRFLTD PTPFKLNKEY MHDDILEEPL HEPIGSSNST SNSSSVVDLQ SSEDGGELNF YEDERHFFTD SGYPFYSQNK SFVKQICDLF ISLFALNKAN AGWLRGRAII TVLQQLLGST IEKYIKVSIQ KLRSEDQVFE AIVTFKNMLW GDNGLFERKR NETAEATRSE GERLRTEQLA LTSLQRLFAD TCGRVVGLRD SHEAAGRVHA MLQNPYLNAS LLLEALDAIL LDIICND // ID MVP1_ASHGO STANDARD; PRT; 524 AA. AC Q75CC3; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 30-MAY-2006, entry version 17. DE Sorting nexin MVP1. GN Name=MVP1; OrderedLocusNames=ACL014C; OS Ashbya gossypii (Yeast) (Eremothecium gossypii). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=33169; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient RT Saccharomyces cerevisiae genome."; RL Science 304:304-307(2004). CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016816; AAS51214.1; -; Genomic_DNA. DR AGD; ACL014C; -. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Complete proteome; Protein transport; Transport. FT CHAIN 1 524 Sorting nexin MVP1. FT /FTId=PRO_0000238593. FT DOMAIN 141 260 PX. SQ SEQUENCE 524 AA; 60802 MW; DEA40CA0C452E2BA CRC64; MMDLDSQELW GRGPSMESPN NAWASVQRTP ADSARTQQIV SPVVRQAESL GSLTLTDSSL SAEVKETMRN NYNERKMYEP GTPALEQTVW GAPPSQLDAS ISGLDTSMAP VASQSSMCDE LHSEDLENWM NSRRKTYNPL AKNIVVVEEI PEREGILFKH TNYLVKHLVV LPNTNPSSNQ TVIRRYSDFN WLQEVLLKKY PFRMIPELPP KKIGAQNADP IFLARRRKGL CRFINLVIMH PVLKQDDLVL TFLTVPTDLG SWRKQANYDT TEEFTDQKID KAFISLWHKE LSNQWNKADA KIDELLESWI KTSVLVERYE RRMRQVSEER RLLGRVIEEF ADNSVTLYPL EEGHLFHDIN SHISTISKHL NSLADTSKKE RQEVEEHLSV KFKTFIDIII ALKGVFDRYK IMAGNNIAHL QRRVEINMDK LQSMESNPDV KGAEYDKLRQ TIQRDKRTIA EQLNRSWLIR KCILEEFVIF QETQFCITHV FQEWAKMHVK YANETTESWE KVYANLQDMP LSRS // ID MVP1_ASPFU STANDARD; PRT; 729 AA. AC Q4WZF1; Q876N2; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 30-MAY-2006, entry version 8. DE Sorting nexin mvp1. GN Name=mvp1; ORFNames=Afu2g17180, 25d9-1; OS Aspergillus fumigatus (Sartorya fumigata). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5085; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=22131470; PubMed=12136012; RA Firon A., Beauvais A., Latge J.-P., Couve E., RA Grosjean-Cournoyer M.-C., D'Enfert C.; RT "Characterization of essential genes by parasexual genetics in the RT human fungal pathogen Aspergillus fumigatus: impact of genomic RT rearrangements associated with electroporation of DNA."; RL Genetics 161:1077-1087(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Af293 / CBS 101355 / FGSC A1100; RX PubMed=16372009; DOI=10.1038/nature04332; RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., RA Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., RA Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., RA Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., RA Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., RA Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., RA Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., RA Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., RA Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., RA Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., RA Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., RA Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., RA Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., RA Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., RA White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., RA Machida M., Hall N., Barrell B.G., Denning D.W.; RT "Genomic sequence of the pathogenic and allergenic filamentous fungus RT Aspergillus fumigatus."; RL Nature 438:1151-1156(2005). CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY080962; AAM08674.1; -; Genomic_DNA. DR EMBL; AAHF01000001; EAL94014.1; -; Genomic_DNA. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Complete proteome; Protein transport; Transport. FT CHAIN 1 729 Sorting nexin mvp1. FT /FTId=PRO_0000238594. FT DOMAIN 356 464 PX. FT COMPBIAS 206 210 Poly-Pro. FT CONFLICT 162 162 E -> K (in Ref. 1). SQ SEQUENCE 729 AA; 80642 MW; 0430C2396A6B3271 CRC64; MSLFGTSPDD PSMGDSVHQR SRSSLFADEP LPGGAGAGNS ANLGSSSLFA DDDGFQSSSP WNSNANKRAA RHELVKTLLP DADVPESYID AYDLVLNEGD RVGGVVGLTS VREILSSSGL SASDQAKIFN LVVSGDGDSA NGLGRGQFNV LLALIGLAQE GEDLTFDAVD DRRKKLPLPK SSYLDRLRDR QQPSAPSHPE ERPTTPPPPP AAINDPPSAR SRQSRETLGG LDADPWGSPQ LHRGHNHVQT EPEPPVLNGF GSVRSATNAW SSGAGEDETQ HEVPSGLRAN GRTDGAPSTS SGSGWGGSYR NTTAGDGFGG PIRAGLGNLG APSSGQEEPN ARRRLGIGIS TSSQVEETVT VNLLPEKEGM FMFQHRNYEV KSSRRGSTVI RRYSDFVWLL DCLQKRYPFR QLPLLPPKRI AADSNSFLEK RRRGLVRFTN ALVRHPVLSQ EQLVVMFLTV PTELSVWRKQ ATISVQDEFT GRVLPPDLED SLPANLTDIF ETVRSGVKRS AEIYINLCTL LERLAKRNEG LAADHLRFSL ALQSLTEVTK DTYAVDTNDV PILNEGIMAT ARHLSNSQSL LEDEARAWEN GILEDLKFQR DCLVSVREMF DRRDRYARNN IPQLERRIES NERKLEELRT RPQGAVKPGE IEKVEESIFK DKESIVQQHA RGVFIKECIR DELVHFQRSQ YHISRLHQDW SQERVKYSEL QADNWRSLSD QVEGMPLGE // ID MVP1_ASPOR STANDARD; PRT; 724 AA. AC Q2UB56; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 30-MAY-2006, entry version 7. DE Sorting nexin mvp1. GN Name=mvp1; ORFNames=AO090102000101; OS Aspergillus oryzae. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5062; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RIB 40 / ATCC 42149; RX PubMed=16372010; DOI=10.1038/nature04300; RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., RA Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., RA Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., RA Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W., RA Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., RA Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., RA Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., RA Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., RA Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., RA Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., RA Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., RA Kuhara S., Ogasawara N., Kikuchi H.; RT "Genome sequencing and analysis of Aspergillus oryzae."; RL Nature 438:1157-1161(2005). CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP007162; BAE61209.1; -; Genomic_DNA. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Complete proteome; Protein transport; Transport. FT CHAIN 1 724 Sorting nexin mvp1. FT /FTId=PRO_0000238595. FT DOMAIN 351 459 PX. SQ SEQUENCE 724 AA; 79918 MW; 3130221F2E2D28B5 CRC64; MSLFGTSPED SSAGNSAHRS KSSLFADEPS LGTGSNANLG SSSLFADDDD LSSGSPWNSN VNKRTARHKL VKTLLSDSDA PESYIDAYDL VLSAGDRVGA GIGLTSVREI LSGSGISASD QEKILNIVVS GDIDSANGLG RGEFNVLLAL VGLAQEGEDL TLDAVDDRRK KLPAPKSLYL DALRANQESG TPAPSQERPI TPPRPASPQQ APNSAHSRRE SMTGLESDPW GSPELHRGHA HAQLESDHPV LNGYGSVRSA TNAWSSRVGE DNNPNEISNS NRANSQTDSA PSHGSGFGWG ESLGNTPSDG GLGGTARAGL GGFGPPSSVH SDSNPRRRSL GIGRVASPPV EEHVTVTLLP EKEGMFMFQH RNYEVKSARR GSTVVRRYSD FVWLLDCLQK RYPFRQLPLL PPKRLSADSN AFLEKRRRGL VRFTNALVRH PVLSQEQLVI MFLTVPTELS VWRKQATISV QDEFTGRDLP PDLEDSLPST LPDTFETVRG GVKRSAEIYI NLCTLLERLA KRNEGLAADH LRFSLALQSL TEVTRDTYAI DTNDVPLLNE GIRATANHLS VSQSLLEDEA RAWEEGVLED LKRQRDCLVS VREMFDRRDR YARNNIPQLE RRIENNERKL QDLRSRPQGT VKPGEIEKVE DAIIKDKESI VQQHARGVFI KECIRDEIVY FQQSQYHISR LHQEWSQERV KYAELQADNW RSLSDQVESM PLSG // ID MVP1_CANAL STANDARD; PRT; 745 AA. AC Q3MPQ4; Q5AFM9; Q5AFN0; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 30-MAY-2006, entry version 5. DE Sorting nexin MVP1. GN Name=MVP1; ORFNames=CaJ7.0093, CaO19.7038, CaO19.7039; OS Candida albicans (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5476; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15937140; DOI=10.1534/genetics.104.034652; RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T., RA Mikami Y.; RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 RT and syntenic analysis against the Saccharomyces cerevisiae genome."; RL Genetics 170:1525-1537(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., RA Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., RA Davis R.W., Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC -!- CAUTION: Ref.2 (EAL01486) sequence differs from that shown due to CC erroneous gene model prediction. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AP006852; BAE44606.1; -; Genomic_DNA. DR EMBL; AACQ01000024; EAL01486.1; ALT_SEQ; Genomic_DNA. DR EMBL; AACQ01000024; EAL01485.1; -; Genomic_DNA. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Protein transport; Transport. FT CHAIN 1 745 Sorting nexin MVP1. FT /FTId=PRO_0000238596. FT DOMAIN 326 445 PX. FT COMPBIAS 18 25 Poly-Asn. FT COMPBIAS 57 66 Poly-Gly. FT COMPBIAS 101 121 Asn-rich. FT COMPBIAS 245 298 Gly-rich. FT COMPBIAS 551 558 Poly-Val. SQ SEQUENCE 745 AA; 84996 MW; 90ACE875652C6DF1 CRC64; MNSNIEDDPW SSGWNDDNDN NNNNNTSIND PLTGATATTT PYQSSYLTSS QLFTSTGGGG SGSGGGYNSG VNTYNTTIPP NLINVPSSYE TIYSHFITKY NNNNNNNNSN STFTLNDFEI NIIDKLISLN YLTNYQKQKI LDIIYENNLL PINQSFKFYQ ILGLLALEID VPGTGDYVTL QFRLNNNLPD LPEKFINEII NEENEQEEQT SGLLGNRNRS IQSHSHFGPN NQDDWNIDDS TTISGGGGGG GGNFGDPLLV DHSYIHDDLI DESRSVGGTQ PQQGGGGGSG GGSGSGSGTI APNVDSSYIE KYINDIKDQF KPLFSGIDLI KIKEVPEKEG IIFKHINYMI THDLKIGGTS SGTKKVIRRY SDFVWLMEYL LEKYPFRVIP GLPPKKFTVG ASPDSQFLQR RRRGLHRFLN QLIKHPILSQ EPIVQSFLTV PTDLTTWKKQ AKIDSSLEFK GQKIQTDFIN VIWPIMGEPF LKKWRQAEEN IQFIIDKWVK IIILVERYER RQQQISFDNG KFAEMLNGFS KLNTKIYPDN EDNNNSTRND VNVNVVVVDN NENYKQDFDF NSSGDIININ QCLNSIGEFF NKSSQVLIDE SYIINTKTLE KFKNYLDYLN SLQELFERTK QLSINQIDLL DKRIKDQEIK FKKISEENPD IKGGELIKLR QSIINDKQEI FQQLNKDWLI KQCCLQEFII FQETQFLITE LWVEWCKDRL KCQEKLVGLY DNLNQEIIHD MPLER // ID MVP1_CANGA STANDARD; PRT; 509 AA. AC Q6FNH2; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 30-MAY-2006, entry version 14. DE Sorting nexin MVP1. GN Name=MVP1; OrderedLocusNames=CAGL0J11704g; OS Candida glabrata (Yeast) (Torulopsis glabrata). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5478; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR380956; CAG61173.1; -; Genomic_DNA. DR InterPro; IPR011028; Cyclin_like. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Complete proteome; Protein transport; Transport. FT CHAIN 1 509 Sorting nexin MVP1. FT /FTId=PRO_0000238597. FT DOMAIN 126 245 PX. SQ SEQUENCE 509 AA; 59105 MW; 345C5EA2EE87ABB3 CRC64; MDTYSGQNGW ADTSNASPWG DTNDTMPIDN SLSNSLSGLQ LNEDINTVRA NLTESIWGTE RTGAPNNVET GLEAKDSLNV STNFNELNTA ILSPTSSTSN IEEQNSFTES LESWINEVRK TYNPQQLDII SIEEIPEREG LLFKHANYSV KHLIDLPNTE PPKNRTVVRR YSDFLWLQEV LLKRYPFRMI PDLPPKKIGS QNLDPVFLNK RRIGLSKFIN LVMKHPKLSK DDLVLTFLTV PTDLTSWRKQ VSYDTADEFT DKRISKDFVK IWKKDLAEIW NNTANCIDEL IDKWTKISIL VDRHEKRLQI IANERKIMND LIHDVGNLTK SVYPIDQNPT ILDINSGMTV ISKHIEKTNE NYNQQALDTK QKVLPKFRMY TDILRALKNV FERYKMLATN NVSMLQKHID LNLQKLEDMK GKPDASGQEY DRIKTTIRKD RKIMYEQSNR AWLIRECILE EFTIFQETQF MITGCFQEWA KVQSTYSSLN LNEWENVTNH ILEMPLSRE // ID MVP1_CRYNE STANDARD; PRT; 612 AA. AC Q5KF05; Q55R65; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 30-MAY-2006, entry version 10. DE Sorting nexin MVP1. GN Name=MVP1; OrderedLocusNames=CNF03550, CNBF1250; OS Cryptococcus neoformans (Filobasidiella neoformans). OC Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Heterobasidiomycetes; OC Tremellomycetidae; Tremellales; Tremellaceae; Filobasidiella. OX NCBI_TaxID=5207; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-3501A, and JEC21; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., RA D'Souza C.A., Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., RA Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., RA Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., RA Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., RA Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., RA Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., RA Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., RA Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen RT Cryptococcus neoformans."; RL Science 307:1321-1324(2005). CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE017346; AAW44126.1; -; Genomic_DNA. DR EMBL; AAEY01000030; EAL20314.1; -; Genomic_DNA. DR UniGene; Fne.187; -. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Complete proteome; Protein transport; Transport. FT CHAIN 1 612 Sorting nexin MVP1. FT /FTId=PRO_0000238598. FT DOMAIN 226 334 PX. SQ SEQUENCE 612 AA; 67744 MW; F2959B9C3A1855D1 CRC64; MFNAPRPMAS SYSYTDPLSN SAAAGAAFGE LDPWSSAPSP AGSVTPARAT ASASEGRNIA ANGNKEEGLN GLINDPPALY VSLLDQLDTS GTGEVSLAAV HRLLGTSKLP AVVVEKIIHL TSRDKSTLTR PEFFCALALV SLAQSSPDPN DISIEKLSFS LSNLPLPKLK PSDPPSVSSG VAASTAAATG FNAWDGTINK GTTYSANNST FRSTDPMVDN AEDRWWKDQE RIVVTLIPEK EGWFLQKYRI ESDKRGEGPV ARRYSDFVWL MDVLEKRYPF RILPPLPPKR INPSSAFLEA RRLALIRLLS FLTAHPVLRT DACLNIFLTS SSFESWRKRT PVSTDEESLS KKLTTAQEMS IPSDLELKLD NLRERLPAML GHYTRLVVMA ERSLVRLQVQ AAEAARMAMS TQSIGELVPR CCWRSVQGDD GESGRGVARE CGLCEGVGRG WGDVGDGWVS VGEELEKGVQ LLQKHIESLK SQRDLYSSFH ALFYRHNKLS LDNVDVLRKR VDSRFSKIES LKSAKKPGWE GEVDKLASQS DRDTAEIQRL LARRVFVRAC MWHELSVVFH SMQAAQGTMG WKDFVKDQKE RTKRLNGVWQ GLEETLESMP LE // ID MVP1_KLULA STANDARD; PRT; 512 AA. AC Q6CUC4; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 30-MAY-2006, entry version 12. DE Sorting nexin MVP1. GN Name=MVP1; OrderedLocusNames=KLLA0C06006g; OS Kluyveromyces lactis (Yeast) (Candida sphaerica). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=28985; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 2359 / IFO 1267 / NRRL Y-1140 / WM37; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR382123; CAH01316.1; -; Genomic_DNA. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Complete proteome; Protein transport; Transport. FT CHAIN 1 512 Sorting nexin MVP1. FT /FTId=PRO_0000238599. FT DOMAIN 130 248 PX. SQ SEQUENCE 512 AA; 59656 MW; BA0B610DFBBF1A02 CRC64; MDLEADPWRV NSEENGNNIS GSVWEPDNSS VNALKSYSAD SLQQEANKRV NDDYLGVNIF SNGDNIVRGT ASNVYQNDVL WDRPNIGSTT QETDIRGVNR FQATDTPQYA ANDEYKNWVE SVRKTYFPLA EDIVSVEEIP EREGLVFKHT NYLVKHLTPL PNTDPSDDRT VVRRYSDFDW LQDVLLRKYP FRMVPELPPK KIGSQNADPL FLAKRRKGLS RFINLVMKHP VLRSDDLVLT FLTVPTDLSG WRKQAHYDTT DEFTDKHISS SFMNLWRKEF SEQWNKADER IDIALDTWVK VTVLIERYEK RMKQVAHERK LLGQILNAIP DTTEALYPQS TATVSQINEG VGLIVEHLNS CADVIERENE EVDSGLSVRF KAFIDVIIAL KGLFERYKMM AGNNIPQLQR RVEINQERLN TLESNPDVKG AEYDRVKQSI SRDKRSILDQ MNRSWLIREC ILEEFTIFHE TQFLITDCFQ RWIEINLRYT NNNVDNWEKI CKKLRDMPLQ RH // ID MVP1_NEUCR STANDARD; PRT; 780 AA. AC Q7SB97; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 30-MAY-2006, entry version 14. DE Sorting nexin mvp-1. GN Name=mvp-1; ORFNames=NCU05715; OS Neurospora crassa. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=5141; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=74-OR23-1A / FGSC 987; RX MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554; RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., RA Jaffe D., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., RA Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., RA Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., RA Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., RA Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., RA Mauceli E., Bielke C., Rudd S., Frishman D., Krystofova S., RA Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., RA Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., RA Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.; RT "The genome sequence of the filamentous fungus Neurospora crassa."; RL Nature 422:859-868(2003). CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABX01000171; EAA33665.1; -; Genomic_DNA. DR HSSP; Q08826; 1OCS. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Protein transport; Transport. FT CHAIN 1 780 Sorting nexin mvp-1. FT /FTId=PRO_0000238600. FT DOMAIN 411 515 PX. FT COMPBIAS 102 158 Ala-rich. FT COMPBIAS 242 249 Poly-Gln. SQ SEQUENCE 780 AA; 85051 MW; 1FC1F7CC5D9735F8 CRC64; MSLFGSSPPN DGSAALNPAK TANSSRSTLF DNEAPTTRSG SALFADDDHD SPWDMPTPRK QRSRADLIRN LLPSGDVPES YIETFDAVVR TENRSTNGRI TAGGVARTLA AAKLGADDQA RIMGIIAPAS ASATGAGGGG DGAHGGEANS SAAAAAAAVG LGDLGRNEFN VLLALIGLVQ EGEVASLDGV DERRRNLPQP KLQGLVNENV QPMLPNLSEL GAKPPQRPVT PPKAPTPSPP KQQQQQQHQP PTLRKVSMEY PEDPWNAPDL HKGHNHGPLE HSTGHNGAAD VPRSVANDLN GNDAVSYSTS PEVTTTSSAL PGRTTSTFTT SQPPSGPSSI HNVAESIQES NGAWNYFPGS SSGGGFGEPA DNAITGPFGD SGGPGQSVSG SVGGSNPNRS IGHVRSGSNV EENILVTLMP EKEGVFMFQH HNYEVSSIRR GSKVVRRYSD FVWLLDCLHK RYPFRVLPLL PPKRVASFIE KRRRGLARFL NALVRHPVLG QEQLVIMFLT VPTELSVWRK QATISVQDEF TGRTLPPGLE DSLPPTLEEL FARTRVGVRR SAELYISTCT IMDRLIKRSE GVAADHARMA VSLISLTETS ADTYATDHND VPLLNDGLQA MGRHLRTAQT LMEDEAKAWE EGVLEDLKRQ RDALVSLRDM FDRRDRLDKD NIPFLQRRIE TNEAKLQALN AKPEGMVKPG EKERVVEAII KDKESIVTQH NRSVFVKECI RDELRFFQNT QYNVSRLTQD WAQERVKYSE MLADNWRRLL DDLEGMPLGD // ID MVP1_SCHPO STANDARD; PRT; 664 AA. AC O14120; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 3. DT 30-MAY-2006, entry version 26. DE Sorting nexin mvp1. GN Name=mvp1; ORFNames=SPAC3A11.06; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z99260; CAB16392.2; -; Genomic_DNA. DR PIR; T11628; T11628. DR GeneDB_Spombe; SPAC3A11.06; -. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Complete proteome; Protein transport; Transport. FT CHAIN 1 664 Sorting nexin mvp1. FT /FTId=PRO_0000238601. FT DOMAIN 279 395 PX. SQ SEQUENCE 664 AA; 76861 MW; FB4E9F1C312FA85C CRC64; MGDNVFLEPD PWASSSNWGS PVKPLNYKTA IGNSSIPLQY RNYWDVFQAN NVLLFPEEES YSDIFHVPQD VMKEFFTLIE SSSNQPLRQI QFFVLLALVA CYQLGVPSTL EQIFKQRNVL PILQRFNPEL FNRSSDNETP LFPNNSPPAS TTALNLSSNI VPSINESKIL EQEDDDVSNK SLPHAQQSII RSFPDIQKQP KGFFSYPSST VSSIAPSTLE AGNLHSQQPP KFSVDSSVDD NAITPRKPFS KIPNRLSPST QPLLSNSRHS SFRLASSSTS FPASLEMNVD IDLEPSGYFF YRHNNYIISD SSNTREVLRR YSDFFWLHSY LMKKYPFRRV PLIPLKKFHS KCFNSKQFFR TPPPGLSDFV NDLSHHPIFS NDEVVRVFFT EPNVFKNWRR ENQKRIDQEI EQFLVVPQSQ VPDASETVKE RLLKLNMSTT TAINNQLNIF RIFEKMIFTL QHFHEDFLRL QNSFNCLLDS GLYHQVFTST FAQNESKIMS MASGHFYNID SLLHQQNDAV KHTFLLGLSK EIKILISLRL LIERISEVFS TDLTKVRHTI SNDENLLRET ANSDESGRNR TFLNRSSKKR AENSLKSKKE LYLKNLNQRY QIAHELEQEL SYLQDYVFSL GNPYVEYCKQ HVKLEEESLK IWHTLESDFS RLET // ID MVP1_USTMA STANDARD; PRT; 683 AA. AC Q4PHC3; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 30-MAY-2006, entry version 5. DE Sorting nexin MVP1. GN Name=MVP1; ORFNames=UM00490; OS Ustilago maydis (Smut fungus). OC Eukaryota; Fungi; Basidiomycota; Ustilaginomycetes; OC Ustilaginomycetidae; Ustilaginales; Ustilaginaceae; Ustilago. OX NCBI_TaxID=5270; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=521; RA Birren B.W., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., RA Ait-Zahra M., Allen N., Allen T., An P., Anderson M., Anderson S., RA Arachchi H.M., Armbruster J., Bachantsang P., Baldwin J., Barry A., RA Bayul T., Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., RA Borowsky M., Boukhgalter B., Brunache A., Butler J., Calixte N., RA Calvo S.E., Camarata J., Campo K., Chang J., Cheshatsang Y., RA Citroen M., Collymore A., Considine T., Cook A., Cooke P., Corum B., RA Cuomo C., David R., Dawoe T., Degray S., Dodge S., Dooley K., RA Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Elkins T., RA Engels R., Erickson J., Farina A., Faro S., Ferreira P., Fischer H., RA Fitzgerald M., Foley K., Gage D., Galagan J.E., Gearin G., Gnerre S., RA Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., RA Hagopian D., Hagos B., Hall J., Hatcher B., Heller A., Higgins H., RA Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E., Iliev I., RA Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M., Karlsson E., RA Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E., Labutti K., RA Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T., RA Lindblad-Toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., RA Lui A., Ma L.-J., Mabbitt R., MacDonald J., MacLean C., Major J., RA Manning J., Marabella R., Maru K., Matthews C., Mauceli E., RA McCarthy M., McDonough S., McGhee T., Meldrim J., Meneus L., RA Mesirov J., Mihalev A., Mihova T., Mikkelsen T., Mlenga V., Moru K., RA Mozes J., Mulrain L., Munson G., Naylor J., Newes C., Nguyen C., RA Nguyen N., Nguyen T., Nicol R., Nielsen C.B., Nizzari M., Norbu C., RA Norbu N., O'Donnell P., Okoawo O., O'Leary S., Omotosho B., RA O'Neill K., Osman S., Parker S., Perrin D., Phunkhang P., Piqani B., RA Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V., Raymond C., RA Retta R., Richardson S., Rise C., Rodriguez J., Rogers J., Rogov P., RA Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T., RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C., RA Spencer B., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stetson K., Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., RA Tenzing P., Tesfaye S., Theodore J., Thoulutsang Y., Topham K., RA Towey S., Tsamla T., Tsomo N., Vallee D., Vassiliev H., RA Venkataraman V.S., Vinson J., Vo A., Wade C., Wang S., Wangchuk T., RA Wangdi T., Whittaker C., Wilkinson J., Wu Y., Wyman D., Yadav S., RA Yang S., Yang X., Yeager S., Yee E., Young G., Zainoun J., Zembeck L., RA Zimmer A., Zody M., Lander E.S.; RT "The genome sequence of Ustilago maydis."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AACP01000010; EAK80810.1; -; Genomic_DNA. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Protein transport; Transport. FT CHAIN 1 683 Sorting nexin MVP1. FT /FTId=PRO_0000238602. FT DOMAIN 302 418 PX. SQ SEQUENCE 683 AA; 77206 MW; 1B66D9E79172DA09 CRC64; MSRHHRPFTW GGAQPGASFS NPTSPTLEAS TFGFEPSVPD IYRRAWILVT KDASAELFAD TSDADIHLGL LHKLLTSAGG LGPGSAEQIV NSACKGSRCS RSDFYCALGL LHQMQQGEEL DVHLVQQRLT MGSLSAPVLD LSDATLNPHS HHTFPPTAPS GPSRIDPRPS TFMREMSDPW NANSSGSYNG IDTRPAYNQY DAMPQQYDTL NSHDSALPAG FAGNVSSGSF ERIKFNAGDD RRSHQLLAHN QGSSTDTFLA PDRTEARARQ PNTRQERPFS YMSDTAETNA VDAAEDPAAD LPEDQVTVRL RSELEGFIIK HNVYIVSSSL RKSQVTRRYS DWLWLAECLV KRYPFRCLPV LPPKRIAMPI AGRHLSADDL FIERRRRGLE RFLRMLTCHP MLREDKLVEV FFTEPRPIAE WKSSAPALFL DEEGLIKTVD EAERMSIPED LQLKLTQQRQ AIPELLERWT AMVALFERIV KRNDAAAADY SRLNFSLLSV IETSARRWRP GSDNGKKTEE IMSTMASIFQ DHSDTTSSRV SAVSLSTLEG MKAQRDLILS FRDLIGRIDR QLVDPIDMLK KRIEASQKRI TTLAASANSN SASIQQEQAT LSAQVKQDTQ SIQKYLNRRI HAKKTVWEEL IWFHHRFKAV EEDMQKFVRD ETFFLSTLTR MWEATEMKMK MIR // ID MVP1_YARLI STANDARD; PRT; 605 AA. AC Q6CHY6; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 30-MAY-2006, entry version 14. DE Sorting nexin MVP1. GN Name=MVP1; OrderedLocusNames=YALI0A03443g; OS Yarrowia lipolytica (Candida lipolytica). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Dipodascaceae; Yarrowia. OX NCBI_TaxID=4952; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CLIB 122 / E 150; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., RA Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., RA Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., RA Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C., RA Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., RA Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., RA Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., RA Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., RA Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., RA Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., RA Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., RA Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). CC -!- FUNCTION: Required for vacuolar protein sorting (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR382127; CAG83648.1; -; Genomic_DNA. DR InterPro; IPR001034; HTH_DeoR. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Complete proteome; Protein transport; Transport. FT CHAIN 1 605 Sorting nexin MVP1. FT /FTId=PRO_0000238603. FT DOMAIN 226 343 PX. SQ SEQUENCE 605 AA; 68061 MW; 9BAC71F8550D1DD2 CRC64; MSLFSAATTA VERTGYGSRY DHIFDMFHPI DGRIPAVCYK RLLETINVSG EDKDRLATLA GSILEGGDGS GGILTSSFTR ESWRAALLLA NVAQDGLPFD DPSQLVNVDT LTPMDFSEEG ERSSINFSAS TTGRSQTPLF GDDLDDHSIQ SSRSESIIHN NGHSRGHSAL DWNPEEQEAL QQSQLSQSQL SRSTTPPPLN PQALVPESES GVWTAPPRPD FAPNKADSVT LAIVPEREGM FLFRHVNYSI SSVSGTDRIT VIRRYSDFSW LQDYLLKKYC FRQVPLLPPK RLAVNGHYLS SDNYFLERRR RGLTRFINQV LRHPVLGQDE AVRTFVTLRN DISGWKKSVF NTAREEFNGR TIDPKFVQQW DEQQATALWA GLIVELDRSH DSVVQLCVLL DRVAKRQEAQ AVDSAKIAYN LGAALPPSAR VLYSVADDGC VQQITRGLSR ASARIETDCQ LQQDEARGSQ VGVLEEAKKY REALGSMREL FDRLEKYGGN NIPLLEKRIQ QNQGRVTLAR QRKALMSEIE KLDRAIKMDT EMIAAHKNRT WLIRECITEE IGLFQKTQLQ ISKLLQEFCV DKIKYAELYS DNWGGLDNDV MDLPV // ID MVP1_YEAST STANDARD; PRT; 511 AA. AC P40959; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 30-MAY-2006, entry version 42. DE Sorting nexin MVP1. GN Name=MVP1; OrderedLocusNames=YMR004W; ORFNames=YM8270.06; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH VPS1, RP AND SUBCELLULAR LOCATION. RX MEDLINE=95166252; PubMed=7862158; RA Ekena K., Stevens T.H.; RT "The Saccharomyces cerevisiae MVP1 gene interacts with VPS1 and is RT required for vacuolar protein sorting."; RL Mol. Cell. Biol. 15:1671-1678(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c / AB972; RX MEDLINE=97313268; PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., RA Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., RA Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome RT XIII."; RL Nature 387:90-93(1997). RN [3] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Required for vacuolar protein sorting. CC -!- SUBUNIT: Interacts with VPS1. CC -!- INTERACTION: CC P43603:YFR024C; NbExp=1; IntAct=EBI-11636, EBI-22980; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Present with 2210 molecules/cell. CC -!- SIMILARITY: Belongs to the sorting nexin family. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U16137; AAA67884.1; -; Genomic_DNA. DR EMBL; Z48613; CAA88519.1; -; Genomic_DNA. DR PIR; S53033; S53033. DR IntAct; P40959; -. DR GermOnline; 142672; -. DR Ensembl; YMR004W; Saccharomyces cerevisiae. DR GenomeReviews; Z71257_GR; YMR004W. DR SGD; S000004606; MVP1. DR BioCyc; SCER-S28-01:SCER-S28-01-004510-MONOMER; -. DR LinkHub; P40959; -. DR GO; GO:0005737; C:cytoplasm; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0006623; P:protein targeting to vacuole; IMP. DR InterPro; IPR001683; PX. DR Pfam; PF00787; PX; 1. DR SMART; SM00312; PX; 1. DR PROSITE; PS50195; PX; 1. KW Complete proteome; Protein transport; Transport. FT CHAIN 1 511 Sorting nexin MVP1. FT /FTId=PRO_0000213802. FT DOMAIN 128 247 PX. FT CONFLICT 85 85 Q -> N (in Ref. 1). SQ SEQUENCE 511 AA; 59657 MW; 0EBB10FBCBB1DD78 CRC64; MDNYEGSDPW NTSSNAWTKD DDHVVSTTNS EPSLNGISGE FNTLNFSTPL DTNEEDTGFL PTNDVLEESI WDDSRNPLGA TGMSQTPNIA ANETVIDKND ARDQNIEESE ADLLDWTNNV RKTYRPLDAD IIIIEEIPER EGLLFKHANY LVKHLIALPS TSPSEERTVV RRYSDFLWLR EILLKRYPFR MIPELPPKRI GSQNADQLFL KKRRIGLSRF INLVMKHPKL SNDDLVLTFL TVRTDLTSWR KQATYDTSNE FADKKISQEF MKMWKKEFAE QWNQAASCID TSMELWYRIT LLLERHEKRI MQMVHERNFF ETLVDNFSEV TPKLYPVQQN DTILDINNNL SIIKKHLETT SSICKQETEE ISGTLSPKFK IFTDILLSLR SLFERYKIMA ANNVVELQRH VELNKEKLES MKGKPDVSGA EYDRIKKIIQ KDRRSIIEQS NRAWLIRQCI LEEFTIFQET QFLITRAFQD WAKLNSNHAG LKLNEWEKLV TSIMDMPISR E // ID NCF1_BOVIN STANDARD; PRT; 392 AA. AC O77774; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 04-APR-2006, entry version 39. DE Neutrophil cytosol factor 1 (NCF-1) (Neutrophil NADPH oxidase factor DE 1) (47 kDa neutrophil oxidase factor) (p47-phox) (NCF-47K). GN Name=NCF1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=20112525; PubMed=10647999; RA Bunger P.L., Swain S.D., Clements M.K., Siemsen D.W., Davis A.R., RA Gauss K.A., Quinn M.T.; RT "Cloning and expression of bovine p47-phox and p67-phox: comparison RT with the human and murine homologs."; RL J. Leukoc. Biol. 67:63-72(2000). CC -!- FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are CC required for activation of the latent NADPH oxidase (necessary for CC superoxide production). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC -!- SIMILARITY: Contains 2 SH3 domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF079302; AAC82462.1; -; mRNA. DR UniGene; Bt.142; -. DR HSSP; P14598; 1UEC. DR SMR; O77774; 1-123, 157-333. DR InterPro; IPR001655; P47PHOX. DR InterPro; IPR001683; PX. DR InterPro; IPR001452; SH3. DR Pfam; PF00787; PX; 1. DR Pfam; PF00018; SH3_1; 2. DR PRINTS; PR00498; P47PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 2. DR SMART; SM00312; PX; 1. DR SMART; SM00326; SH3; 2. DR PROSITE; PS50195; PX; 1. DR PROSITE; PS50002; SH3; 2. KW Phosphorylation; Repeat; SH3 domain. FT CHAIN 1 392 Neutrophil cytosol factor 1. FT /FTId=PRO_0000096761. FT DOMAIN 4 125 PX. FT DOMAIN 156 215 SH3 1. FT DOMAIN 226 285 SH3 2. FT COMPBIAS 211 254 Asp/Glu-rich (highly acidic). FT COMPBIAS 292 392 Arg/Lys-rich (highly basic). FT MOD_RES 304 304 Phosphoserine (By similarity). FT MOD_RES 305 305 Phosphoserine (By similarity). FT MOD_RES 321 321 Phosphoserine (By similarity). FT MOD_RES 329 329 Phosphoserine (By similarity). FT MOD_RES 348 348 Phosphoserine (By similarity). SQ SEQUENCE 392 AA; 45346 MW; 79199BD86AE80DB7 CRC64; MGDHFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKILKEMFPI EAGDINPENR IIPHLPAPRW YDGQRVAESR QGTLTEYCST LMSLPVKISR CPHLLNFFKV RPDDLKLPTD SQVKKPETYL MPKDGKNNAA DITGPIILQT YRAIADYEKG SSSQMALATG DVVDVVEKNE SGWWFCQMKT KRGWVPASYL EPLDSPDEAE DPEPNYAGEP YITIKAYTAV LEDEISLEEG EAIEVIHKLL DGWWVIRKED VTGYFPSMYL QKAGQDVAQA KSQIKSRGAP PRRSSIRNAH SIHQRSRKRL SQDTYRRNSV RFMQQRRHQR PEPQRSRSAL REQQQPKTER PKPQPAVPPR PSADLILHRC SESTKRKLAS AV // ID NCF1_HUMAN STANDARD; PRT; 390 AA. AC P14598; O43842; Q2PP07; Q9BU90; Q9BXI7; Q9BXI8; Q9UDV9; Q9UMU2; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 2. DT 30-MAY-2006, entry version 78. DE Neutrophil cytosol factor 1 (NCF-1) (Neutrophil NADPH oxidase factor DE 1) (47 kDa neutrophil oxidase factor) (p47-phox) (NCF-47K) (47 kDa DE autosomal chronic granulomatous disease protein) (NOXO2). GN Name=NCF1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89332501; PubMed=2547247; RA Lomax K.J., Leto T.L., Nunoi H., Gallin J.I., Malech H.L.; RT "Recombinant 47-kilodalton cytosol factor restores NADPH oxidase in RT chronic granulomatous disease."; RL Science 245:409-412(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=89386707; PubMed=2550933; RA Volpp B.D., Nauseef W.M., Clark R.A.; RT "Cloning of the cDNA and functional expression of the 47-kilodalton RT cytosolic component of human neutrophil respiratory burst oxidase."; RL Proc. Natl. Acad. Sci. U.S.A. 86:7195-7199(1989). RN [3] RP ERRATUM, AND SEQUENCE REVISION. RA Volpp B.D., Nauseef W.M., Clark R.A.; RL Proc. Natl. Acad. Sci. U.S.A. 86:9563-9563(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90377229; PubMed=2398896; RA Rodaway A.R.F., Teahan C.G., Casimir C.M., Segal A.W., Bentley D.L.; RT "Characterization of the 47-kilodalton autosomal chronic granulomatous RT disease protein: tissue-specific expression and transcriptional RT control by retinoic acid."; RL Mol. Cell. Biol. 10:5388-5396(1990). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=97474758; PubMed=9329953; RA Gorlach A., Lee P.L., Roesler J., Hopkins P.J., Christensen B., RA Green E.D., Chanock S.J., Curnutte J.T.; RT "A p47-phox pseudogene carries the most common mutation causing p47- RT phox-deficient chronic granulomatous disease."; RL J. Clin. Invest. 100:1907-1918(1997). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=20238075; PubMed=10772875; DOI=10.1006/bcmd.2000.0274; RA Chanock S.J., Roesler J., Zhan S., Hopkins P., Lee P., Barrett D.T., RA Christensen B.L., Curnutte J.T., Goerlach A.; RT "Genomic structure of the human p47-phox (NCF1) gene."; RL Blood Cells Mol. Dis. 26:37-46(2000). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-258. RC TISSUE=Umbilical vein; RX MEDLINE=21606173; PubMed=11740866; DOI=10.1006/excr.2001.5404; RA Gu Y., Xu Y.C., Wu R.F., Souza R.F., Nwariaku F.E., Terada L.S.; RT "TNFalpha activates c-jun amino terminal kinase through p47(phox)."; RL Exp. Cell Res. 272:62-74(2002). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLY-99 AND RP ASN-166. RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-99 AND RP ASN-166. RC TISSUE=Lymph; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-31. RC TISSUE=Ovary; RX MEDLINE=96090243; PubMed=7581362; RA Harshman K., Bell R., Rosenthal J., Katcher H., Miki Y., Swenson J., RA Gholami Z., Frye C., Ding W., Dayananth P., Eddington K., Norris F.H., RA Bristow P.K., Phelps R., Hattier T., Stone S., Shaffer D., Bayer S., RA Hussey C., Tran T., Lai M., Rosteck P.R. Jr., Skolnick M.H., RA Shattuck-Eidens D., Kamb A.; RT "Comparison of the positional cloning methods used to isolate the RT BRCA1 gene."; RL Hum. Mol. Genet. 4:1259-1266(1995). RN [11] RP NUCLEOTIDE SEQUENCE OF 14-24, AND INVOLVEMENT IN CHRONIC GRANULOMATOUS RP DISEASE. RX PubMed=2011585; RA Casimir C.M., Bu-Ghanim H.N., Rodaway A.R., Bentley D.L., Rowe P., RA Segal A.W.; RT "Autosomal recessive chronic granulomatous disease caused by deletion RT at a dinucleotide repeat."; RL Proc. Natl. Acad. Sci. U.S.A. 88:2753-2757(1991). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-390. RG NHLBI resequencing and genotyping service (RSnG); RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [13] RP PHOSPHORYLATION AT SER-303; SER-304; SER-320; SER-328; SER-345 AND RP SER-348. RX PubMed=8089108; RA el Benna J., Faust L.P., Babior B.M.; RT "The phosphorylation of the respiratory burst oxidase component RT p47phox during neutrophil activation. Phosphorylation of sites RT recognized by protein kinase C and by proline-directed kinases."; RL J. Biol. Chem. 269:23431-23436(1994). RN [14] RP STRUCTURE BY NMR OF 1-128. RX MEDLINE=21267481; PubMed=11373621; DOI=10.1038/88591; RA Hiroaki H., Ago T., Ito T., Sumimoto H., Kohda D.; RT "Solution structure of the PX domain, a target of the SH3 domain."; RL Nat. Struct. Biol. 8:526-530(2001). RN [15] RP VARIANT CGD GLN-42, AND VARIANT SER-262. RX MEDLINE=20575420; PubMed=11133775; DOI=10.1182/blood.V97.1.305; RA Noack D., Rae J., Cross A.R., Ellis B.A., Newburger P.E., RA Curnutte J.T., Heyworth P.G.; RT "Autosomal recessive chronic granulomatous disease caused by defects RT in NCF1, the gene encoding the phagocyte p47-phox: mutations not RT arising in the NCF1 pseudogenes."; RL Blood 97:305-311(2001). CC -!- FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are CC required for activation of the latent NADPH oxidase (necessary for CC superoxide production). CC -!- INTERACTION: CC Q8IZP0:ABI1; NbExp=4; IntAct=EBI-395044, EBI-375446; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DISEASE: Defects in NCF1 are the cause of autosomal cytochrome-b- CC positive chronic granulomatous disease type 1 (CGD) [MIM:233700]; CC an autosomal recessive form. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC -!- SIMILARITY: Contains 2 SH3 domains. CC -!- WEB RESOURCE: NAME=NCF1base; NOTE=NCF1 deficiency database; CC URL="http://www.uta.fi/imt/bioinfo/NCF1base/". CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=NCF1". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M25665; AAA57209.1; -; mRNA. DR EMBL; M55067; AAA59901.1; -; mRNA. DR EMBL; U57835; AAB95193.1; -; Genomic_DNA. DR EMBL; U57833; AAB95193.1; JOINED; Genomic_DNA. DR EMBL; U57834; AAB95193.1; JOINED; Genomic_DNA. DR EMBL; AF184614; AAF34737.1; -; Genomic_DNA. DR EMBL; AF330625; AAK19516.1; -; mRNA. DR EMBL; AF330626; AAK19517.1; -; mRNA. DR EMBL; AF330627; AAK19518.1; -; mRNA. DR EMBL; AC004883; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC083884; AAS07465.1; -; Genomic_DNA. DR EMBL; BC002816; AAH02816.1; -; mRNA. DR EMBL; BC065731; AAH65731.1; -; mRNA. DR EMBL; U25793; AAA93232.1; -; mRNA. DR EMBL; DQ314878; ABC40737.1; -; Genomic_DNA. DR PIR; A35926; A39249. DR UniGene; Hs.416436; -. DR UniGene; Hs.520459; -. DR UniGene; Hs.559477; -. DR PDB; 1GD5; NMR; A=1-128. DR PDB; 1K4U; NMR; P=359-390. DR PDB; 1KQ6; X-ray; A=1-141. DR PDB; 1NG2; X-ray; A=156-340. DR PDB; 1O7K; X-ray; A/B/C=1-123. DR PDB; 1OV3; X-ray; A/B=156-285. DR PDB; 1UEC; X-ray; A=149-340. DR PDB; 1W70; X-ray; C/D=360-372. DR PDB; 1WLP; NMR; B=151-286. DR IntAct; P14598; -. DR Ensembl; ENSG00000158517; Homo sapiens. DR H-InvDB; HIX0006771; -. DR HGNC; HGNC:7660; NCF1. DR MIM; 233700; phenotype. DR MIM; 608512; gene. DR GO; GO:0005829; C:cytosol; TAS. DR GO; GO:0005625; C:soluble fraction; TAS. DR GO; GO:0005489; F:electron transporter activity; TAS. DR GO; GO:0005525; F:GTP binding; TAS. DR GO; GO:0003924; F:GTPase activity; TAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0006968; P:cellular defense response; TAS. DR InterPro; IPR001655; P47PHOX. DR InterPro; IPR001683; PX. DR InterPro; IPR001452; SH3. DR Pfam; PF00787; PX; 1. DR Pfam; PF00018; SH3_1; 2. DR PRINTS; PR00498; P47PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 2. DR SMART; SM00312; PX; 1. DR SMART; SM00326; SH3; 2. DR PROSITE; PS50195; PX; 1. DR PROSITE; PS50002; SH3; 2. KW 3D-structure; Chronic granulomatous disease; Disease mutation; KW Phosphorylation; Polymorphism; Repeat; SH3 domain. FT CHAIN 1 390 Neutrophil cytosol factor 1. FT /FTId=PRO_0000096762. FT DOMAIN 4 125 PX. FT DOMAIN 156 215 SH3 1. FT DOMAIN 226 285 SH3 2. FT COMPBIAS 211 254 Asp/Glu-rich (highly acidic). FT COMPBIAS 292 390 Arg/Lys-rich (highly basic). FT MOD_RES 303 303 Phosphoserine. FT MOD_RES 304 304 Phosphoserine. FT MOD_RES 320 320 Phosphoserine. FT MOD_RES 328 328 Phosphoserine. FT MOD_RES 345 345 Phosphoserine. FT MOD_RES 348 348 Phosphoserine. FT VARIANT 42 42 R -> Q (in CGD). FT /FTId=VAR_012476. FT VARIANT 90 90 R -> H (in dbSNP:13447). FT /FTId=VAR_014735. FT VARIANT 99 99 S -> G. FT /FTId=VAR_018479. FT VARIANT 160 160 T -> S. FT /FTId=VAR_012477. FT VARIANT 166 166 D -> N (in dbSNP:4868). FT /FTId=VAR_012478. FT VARIANT 258 258 K -> E. FT /FTId=VAR_018476. FT VARIANT 262 262 G -> S. FT /FTId=VAR_012479. FT VARIANT 308 308 A -> V (in dbSNP:13739). FT /FTId=VAR_012480. FT CONFLICT 200 200 A -> T (in Ref. 7; AAK19516). FT STRAND 4 4 FT STRAND 6 17 FT STRAND 19 21 FT STRAND 23 32 FT TURN 33 34 FT STRAND 37 42 FT HELIX 44 57 FT TURN 59 63 FT STRAND 64 65 FT HELIX 67 69 FT STRAND 72 72 FT STRAND 83 83 FT HELIX 84 101 FT TURN 102 103 FT STRAND 104 104 FT HELIX 106 109 FT TURN 110 110 FT HELIX 112 118 FT STRAND 119 119 FT HELIX 122 125 FT STRAND 126 126 FT TURN 131 132 FT STRAND 133 133 FT STRAND 137 140 FT STRAND 159 165 FT STRAND 167 167 FT STRAND 170 171 FT TURN 172 173 FT STRAND 174 174 FT STRAND 177 177 FT TURN 179 180 FT STRAND 182 187 FT TURN 190 191 FT STRAND 192 198 FT STRAND 202 206 FT HELIX 207 209 FT STRAND 210 214 FT STRAND 216 217 FT STRAND 219 219 FT TURN 226 227 FT STRAND 229 235 FT STRAND 237 237 FT STRAND 241 241 FT TURN 242 243 FT STRAND 244 244 FT STRAND 247 247 FT TURN 249 250 FT STRAND 252 257 FT TURN 260 261 FT STRAND 262 268 FT TURN 269 270 FT STRAND 271 276 FT HELIX 277 279 FT STRAND 280 282 FT TURN 283 284 FT STRAND 285 285 FT HELIX 287 292 FT TURN 293 293 FT STRAND 296 296 FT HELIX 302 304 FT STRAND 306 307 FT STRAND 311 311 FT STRAND 313 314 FT HELIX 321 328 FT TURN 329 330 FT STRAND 377 378 FT HELIX 380 385 SQ SEQUENCE 390 AA; 44683 MW; B11B256516F3AA9B CRC64; MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIADYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG EAVEVIHKLL DGWWVIRKDD VTGYFPSMYL QKSGQDVSQA QRQIKRGAPP RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV // ID NCF1_MOUSE STANDARD; PRT; 390 AA. AC Q09014; O70144; Q9JI34; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 2. DT 16-MAY-2006, entry version 48. DE Neutrophil cytosol factor 1 (NCF-1) (Neutrophil NADPH oxidase factor DE 1) (47 kDa neutrophil oxidase factor) (p47-phox) (NCF-47K). GN Name=Ncf1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Macrophage; RX MEDLINE=94164697; PubMed=8119734; DOI=10.1007/BF00188790; RA Jackson S.H., Malech H.L., Kozak C.A., Lomax K.J., Gallin J.I., RA Holland S.M.; RT "Cloning and functional expression of the mouse homologue of RT p47phox."; RL Immunogenetics 39:272-275(1994). RN [2] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leukemia; RX MEDLINE=98149672; PubMed=9490028; RA Mizuki K., Kadomatsu K., Hata K., Ito T., Fan Q.-W., Kage Y., RA Fukumaki Y., Sakaki Y., Takeshige K., Sumimoto H.; RT "Functional modules and expression of mouse p40(phox) and p67(phox), RT SH3-domain-containing proteins involved in the phagocyte NADPH oxidase RT complex."; RL Eur. J. Biochem. 251:573-582(1998). RN [3] RP NUCLEOTIDE SEQUENCE. RA Green E.D.; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are CC required for activation of the latent NADPH oxidase (necessary for CC superoxide production). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Contains 1 PX (phox homology) domain. CC -!- SIMILARITY: Contains 2 SH3 domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L11455; AAA50469.1; -; mRNA. DR EMBL; AB002663; BAA25649.1; -; mRNA. DR EMBL; AF267747; AAF90134.1; -; Genomic_DNA. DR UniGene; Mm.261570; -. DR HSSP; P14598; 1UEC. DR SMR; Q09014; 1-123, 157-333. DR Ensembl; ENSMUSG00000015950; Mus musculus. DR MGI; MGI:97283; Ncf1. DR GO; GO:0005829; C:cytosol; TAS. DR GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; IDA. DR GO; GO:0008283; P:cell proliferation; IMP. DR GO; GO:0016066; P:cellular defense response (sensu Vertebrata); IMP. DR GO; GO:0006954; P:inflammatory response; IMP. DR GO; GO:0006691; P:leukotriene metabolism; IMP. DR GO; GO:0009617; P:response to bacteria; IMP. DR InterPro; IPR001655; P47PHOX. DR InterPro; IPR001683; PX. DR InterPro; IPR001452; SH3. DR Pfam; PF00787; PX; 1. DR Pfam; PF00018; SH3_1; 2. DR PRINTS; PR00498; P47PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 2. DR SMART; SM00312; PX; 1. DR SMART; SM00326; SH3; 2. DR PROSITE; PS50195; PX; 1. DR PROSITE; PS50002; SH3; 2. KW Phosphorylation; Repeat; SH3 domain. FT CHAIN 1 390 Neutrophil cytosol factor 1. FT /FTId=PRO_0000096763. FT DOMAIN 4 125 PX. FT DOMAIN 162 215 SH3 1. FT DOMAIN 226 285 SH3 2. FT COMPBIAS 211 254 Asp/Glu-rich (highly acidic). FT COMPBIAS 292 390 Arg/Lys-rich (highly basic). FT MOD_RES 304 304 Phosphoserine (By similarity). FT MOD_RES 321 321 Phosphoserine (By similarity). FT MOD_RES 329 329 Phosphoserine (By similarity). FT MOD_RES 346 346 Phosphoserine (By similarity). FT CONFLICT 161 161 Y -> H (in Ref. 1). FT CONFLICT 343 345 GQL -> RAA (in Ref. 1). FT CONFLICT 344 344 Q -> P (in Ref. 3). SQ SEQUENCE 390 AA; 44698 MW; A383DB953839CFCB CRC64; MGDTFIRHIA LLGFEKRFIP SQHYVYMFLV KWQDLSEKVV YRKFTEIYEF HKMLKEMFPI EAGEIHTENR VIPHLPAPRW FDGQRAAESR QGTLTEYFNG LMGLPVKISR CPHLLDFFKV RPDDLKLPTD SQAKKPETYL VPKDGKNNVA DITGPIILQT YRAIADYEKS SGTEMTVATG DVVDVVEKSE SGWWFCQMKT KRGWVPASYL EPLDSPDEAE DPDPNYAGEP YVTIKAYAAV EEDEMSLSEG EAIEVIHKLL DGWWVVRKGD ITGYFPSMYL QKAGEEITQA QRQIRGRGAP PRRSTIRNAQ SIHQRSRKRL SQDTYRRNSV RFLQQRRRPG RPGQLSTDGT KDNPSTPRVK PQPAVPPRPS SDLILHRCTE STKRKLTSAV // ID NCF4_HUMAN STANDARD; PRT; 339 AA. AC Q15080; O60808; Q86U56; Q9BU98; Q9NP45; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2006, sequence version 2. DT 30-MAY-2006, entry version 65. DE Neutrophil cytosol factor 4 (NCF-4) (Neutrophil NADPH oxidase factor DE 4) (p40-phox) (p40phox). GN Name=NCF4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-147, AND PARTIAL RP PROTEIN SEQUENCE. RX MEDLINE=94107216; PubMed=8280052; RA Wientjes F.B., Hsuan J.J., Totty N.F., Segal A.W.; RT "p40phox, a third cytosolic component of the activation complex of the RT NADPH oxidase to contain src homology 3 domains."; RL Biochem. J. 296:557-561(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-147. RX MEDLINE=96437051; PubMed=8839867; RA Zhan S., Vazquez N., Zhan S., Wientjes F.B., Budarf M.L., Schrock E., RA Ried T., Green E.D., Chanock S.J.; RT "Genomic structure, chromosomal localization, start of transcription, RT and tissue expression of the human p40-phox, a new component of the RT nicotinamide adenine dinucleotide phosphate-oxidase complex."; RL Blood 88:2714-2721(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX MEDLINE=99364495; PubMed=10437784; DOI=10.1016/S0014-5793(99)00905-9; RA Hasebe T., Someya A., Nagaoka I.; RT "Identification of a splice variant mRNA of p40phox, an NADPH oxidase RT component of phagocytes."; RL FEBS Lett. 455:257-261(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RSnG); RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=20057165; PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H.