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