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VPS3_YEAST
ID   VPS3_YEAST              Reviewed;        1011 AA.
AC   P23643; D6VTB7;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Vacuolar protein sorting-associated protein 3;
DE   AltName: Full=Vacuolar protein-targeting protein 17;
GN   Name=VPS3; Synonyms=VPT17; OrderedLocusNames=YDR495C; ORFNames=D9719.1;
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].
RX   PubMed=2202738; DOI=10.1083/jcb.111.3.877;
RA   Raymond C.K., O'Hara P.J., Eichinger G., Rothman J.H., Stevens T.H.;
RT   "Molecular analysis of the yeast VPS3 gene and the role of its product in
RT   vacuolar protein sorting and vacuolar segregation during the cell cycle.";
RL   J. Cell Biol. 111:877-892(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   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., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., 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   [3]
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   [4]
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).
CC   -!- FUNCTION: Required for sorting and processing of soluble vacuolar
CC       proteins, integrity of vacuolar morphology, efficient segregation of
CC       vacuolar material into the bud during the cell cycle, acidification of
CC       the vacuolar lumen, and assembly of the vacuolar H(+)-ATPase.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 2270 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the VPS3 family. {ECO:0000305}.
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DR   EMBL; X53871; CAA37865.1; -; Genomic_DNA.
DR   EMBL; U33057; AAB64937.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12327.1; -; Genomic_DNA.
DR   PIR; S11177; S11177.
DR   RefSeq; NP_010783.3; NM_001180803.3.
DR   AlphaFoldDB; P23643; -.
DR   BioGRID; 32546; 132.
DR   ComplexPortal; CPX-1626; CORVET complex.
DR   ELM; P23643; -.
DR   IntAct; P23643; 1.
DR   MINT; P23643; -.
DR   STRING; 4932.YDR495C; -.
DR   iPTMnet; P23643; -.
DR   MaxQB; P23643; -.
DR   PaxDb; P23643; -.
DR   PRIDE; P23643; -.
DR   EnsemblFungi; YDR495C_mRNA; YDR495C; YDR495C.
DR   GeneID; 852106; -.
DR   KEGG; sce:YDR495C; -.
DR   SGD; S000002903; VPS3.
DR   VEuPathDB; FungiDB:YDR495C; -.
DR   eggNOG; KOG2063; Eukaryota.
DR   GeneTree; ENSGT00530000063596; -.
DR   HOGENOM; CLU_005205_0_0_1; -.
DR   InParanoid; P23643; -.
DR   OMA; EFAPVPN; -.
DR   BioCyc; YEAST:G3O-30018-MON; -.
DR   PRO; PR:P23643; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P23643; protein.
DR   GO; GO:0033263; C:CORVET complex; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031901; C:early endosome membrane; IDA:ComplexPortal.
DR   GO; GO:0005768; C:endosome; IDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0006914; P:autophagy; IBA:GO_Central.
DR   GO; GO:0034058; P:endosomal vesicle fusion; IBA:GO_Central.
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:0007035; P:vacuolar acidification; IMP:SGD.
DR   GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
DR   GO; GO:0099022; P:vesicle tethering; IDA:ComplexPortal.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR032914; Vam6/VPS39/TRAP1.
DR   PANTHER; PTHR12894; PTHR12894; 1.
DR   PROSITE; PS50219; CNH; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..1011
FT                   /note="Vacuolar protein sorting-associated protein 3"
FT                   /id="PRO_0000065904"
FT   DOMAIN          143..418
FT                   /note="CNH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1011 AA;  116922 MW;  36521AF4A0718CEF CRC64;
     MVKKKTNNDK GKEVKENEGK LDIDSESSPH ERENDKKKTE DDSLRATESE ETNTHNANPN
     ETVRADKFSQ EESRPIEDSP HTDKNTAQES CQPSSAEDNV INTDITSLNE KTSTNDEQEK
     GLPLKISEGP FTISTLLDNV PSDLIYTCCE AYENHIFLGT TTGDLLHYFE LERGNYMLVS
     QTKFDAESNS KIDKILLLPK VEGALILCDN ELVLFILPEF APRPNTTRLK GISDVVICNF
     SRSSKAYRIY AFHAEGVRLL KISADSLVLT KAFNFKLIDK ACAHEETLMV SKLNSYELIN
     LKSSQVIPLF RISETDEDLE PIITSFNEQS EFLVCSGGGS YDSGAMALVV NHHGDIIKGT
     IVLKNYPRNV IVEFPYIIAE SAFQSVDIYS ALPSEKSQLL QSITTSGSDL KISKSDNVFT
     NTNNSEEFKE KIFNKLRLEP LTHSDNKFRI ERERAFVEES YEEKTSLIVY NNLGIHLLVP
     TPMVLRFTSC EESEIDNIED QLKKLAKKDL TKFEHIEAKY LMSLLLFLMT LHYDHIEDEV
     MKKWCDFSDK VDIRILFYMF GWKVYSEIWC FHGLINIVER LKSLKLTNKC ENILKMLLMM
     KNELKKKNKT GLLTNDFDDI MKTIDITLFK LRLEKKETIT VDMFERESYD EIIREINLHD
     DKLPRIELLI EIYKEKGEYL KALNLLREAG DYISLVSFIE ENLKKLPEDY IKERIADDLL
     LTLKQGDENT EECAIKKVLK ILDMACINKN DFLNKIPAEE TSLKVSFIEQ LGVQNSNDSK
     FLFNYYLAKL REIINQSNIW SILGDFIKEY KDDFAYDKTD ITNFIHIKLK HSLQCENFSK
     YYEKCENLKS ENEKDDEFIN FTFDEISKID KEHILTLLFF PNELTNWVSS EELLKIYLSF
     NDFRSVEKYI GKQNLVAVMK QYLDISSLNY SVELVTNLLQ RNFELLDDTD IQLKILETIP
     SVFPVQTISE LLLKVLIKYQ EKKEESNLRK CLLKNQISIS DELSRNFDSQ G
 
 
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