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VPS8_YEAST
ID   VPS8_YEAST              Reviewed;        1274 AA.
AC   P39702; D6VPL4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Vacuolar protein sorting-associated protein 8;
DE   AltName: Full=Vacuolar protein-targeting protein 8;
GN   Name=VPS8; Synonyms=VPT8; OrderedLocusNames=YAL002W; ORFNames=FUN15;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=7941740; DOI=10.1002/yea.320100413;
RA   Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA   Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT   "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT   kbp SPO7-CENI-CDC15 region.";
RL   Yeast 10:535-541(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN   [3]
RP   SEQUENCE REVISION.
RA   Fisk D., Cherry J.M.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-1274.
RX   PubMed=8864656;
RA   Chen Y.-J., Stevens T.H.;
RT   "The VPS8 gene is required for localization and trafficking of the CPY
RT   sorting receptor in Saccharomyces cerevisiae.";
RL   Eur. J. Cell Biol. 70:289-297(1996).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Required for localization and recycling of the CPY sorting
CC       receptor (VPS10) to the late-Golgi compartment. Involved in the
CC       retention of proteins to the late-Golgi. Plays an integral role in the
CC       complex vacuolar protein sorting process.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack. Note=Associated
CC       with the late-Golgi membranes.
CC   -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the VPS8 family. {ECO:0000305}.
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DR   EMBL; L22015; AAC04955.2; -; Genomic_DNA.
DR   EMBL; U44026; AAB49810.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06984.1; -; Genomic_DNA.
DR   PIR; S40899; S40899.
DR   RefSeq; NP_009399.2; NM_001178149.1.
DR   AlphaFoldDB; P39702; -.
DR   BioGRID; 31788; 611.
DR   ComplexPortal; CPX-1626; CORVET complex.
DR   DIP; DIP-6298N; -.
DR   IntAct; P39702; 13.
DR   STRING; 4932.YAL002W; -.
DR   iPTMnet; P39702; -.
DR   MaxQB; P39702; -.
DR   PaxDb; P39702; -.
DR   PRIDE; P39702; -.
DR   EnsemblFungi; YAL002W_mRNA; YAL002W; YAL002W.
DR   GeneID; 851261; -.
DR   KEGG; sce:YAL002W; -.
DR   SGD; S000000002; VPS8.
DR   VEuPathDB; FungiDB:YAL002W; -.
DR   eggNOG; KOG2079; Eukaryota.
DR   GeneTree; ENSGT00390000010672; -.
DR   HOGENOM; CLU_000917_0_1_1; -.
DR   InParanoid; P39702; -.
DR   OMA; WAHQDKH; -.
DR   BioCyc; YEAST:G3O-28817-MON; -.
DR   PRO; PR:P39702; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P39702; protein.
DR   GO; GO:0033263; C:CORVET complex; IDA:SGD.
DR   GO; GO:0031901; C:early endosome membrane; IDA:ComplexPortal.
DR   GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR   GO; GO:0030897; C:HOPS complex; IBA:GO_Central.
DR   GO; GO:0005770; C:late endosome; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IDA:SGD.
DR   GO; GO:0051020; F:GTPase binding; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043495; F:protein-membrane adaptor activity; IMP:SGD.
DR   GO; GO:0034058; P:endosomal vesicle fusion; IBA:GO_Central.
DR   GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IMP:SGD.
DR   GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR   GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IDA:ComplexPortal.
DR   GO; GO:0099022; P:vesicle tethering; IDA:ComplexPortal.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR045111; Vps41/Vps8.
DR   InterPro; IPR025941; Vps8_central_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12616; PTHR12616; 1.
DR   Pfam; PF12816; Vps8; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50236; CHCR; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Golgi apparatus; Metal-binding; Protein transport;
KW   Reference proteome; Repeat; Transport; WD repeat; Zinc; Zinc-finger.
FT   CHAIN           1..1274
FT                   /note="Vacuolar protein sorting-associated protein 8"
FT                   /id="PRO_0000055901"
FT   REPEAT          75..119
FT                   /note="WD 1"
FT   REPEAT          131..170
FT                   /note="WD 2"
FT   REPEAT          193..233
FT                   /note="WD 3"
FT   REPEAT          507..665
FT                   /note="CHCR 1"
FT   REPEAT          915..1092
FT                   /note="CHCR 2"
FT   ZN_FING         1198..1266
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   1274 AA;  144962 MW;  E4476C7C64BFF2CE CRC64;
     MEQNGLDHDS RSSIDTTIND TQKTFLEFRS YTQLSEKLAS SSSYTAPPLN EDGPKGVASA
     VSQGSESVVS WTTLTHVYSI LGAYGGPTCL YPTATYFLMG TSKGCVLIFN YNEHLQTILV
     PTLSEDPSIH SIRSPVKSIV ICSDGTHVAA SYETGNICIW NLNVGYRVKP TSEPTNGMTP
     TPALPAVLHI DDHVNKEITG LDFFGARHTA LIVSDRTGKV SLYNGYRRGF WQLVYNSKKI
     LDVNSSKEKL IRSKLSPLIS REKISTNLLS VLTTTHFALI LLSPHVSLMF QETVEPSVQN
     SLVVNSSISW TQNCSRVAYS VNNKISVISI SSSDFNVQSA SHSPEFAESI LSIQWIDQLL
     LGVLTISHQF LVLHPQHDFK ILLRLDFLIH DLMIPPNKYF VISRRSFYLL TNYSFKIGKF
     VSWSDITLRH ILKGDYLGAL EFIESLLQPY CPLANLLKLD NNTEERTKQL MEPFYNLSLA
     ALRFLIKKDN ADYNRVYQLL MVVVRVLQQS SKKLDSIPSL DVFLEQGLEF FELKDNAVYF
     EVVANIVAQG SVTSISPVLF RSIIDYYAKE ENLKVIEDLI IMLNPTTLDV DLAVKLCQKY
     NLFDLLIYIW NKIFDDYQTP VVDLIYRISN QSEKCVIFNG PQVPPETTIF DYVTYILTGR
     QYPQNLSISP SDKCSKIQRE LSAFIFSGFS IKWPSNSNHK LYICENPEEE PAFPYFHLLL
     KSNPSRFLAM LNEVFEASLF NDDNDMVASV GEAELVSRQY VIDLLLDAMK DTGNSDNIRV
     LVAIFIATSI SKYPQFIKVS NQALDCVVNT ICSSRVQGIY EISQIALESL LPYYHSRTTE
     NFILELKEKN FNKVLFHIYK SENKYASALS LILETKDIEK EYNTDIVSIT DYILKKCPPG
     SLECGKVTEV IETNFDLLLS RIGIEKCVTI FSDFDYNLHQ EILEVKNEET QQKYLDKLFS
     TPNINNKVDK RLRNLHIELN CKYKSKREMI LWLNGTVLSN AESLQILDLL NQDSNFEAAA
     IIHERLESFN LAVRDLLSFI EQCLNEGKTN ISTLLESLRR AFDDCNSAGT EKKSCWILLI
     TFLITLYGKY PSHDERKDLC NKLLQEAFLG LVRSKSSSQK DSGGEFWEIM SSVLEHQDVI
     LMKVQDLKQL LLNVFNTYKL ERSLSELIQK IIEDSSQDLV QQYRKFLSEG WSIHTDDCEI
     CGKKIWGAGL DPLLFLAWEN VQRHQDMISV DLKTPLVIFK CHHGFHQTCL ENLAQKPDEY
     SCLICQTESN PKIV
 
 
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