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Database: UniProt
Entry: STV1_YEAST
LinkDB: STV1_YEAST
Original site: STV1_YEAST 
ID   STV1_YEAST              Reviewed;         890 AA.
AC   P37296; D6VZM9;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   22-NOV-2017, entry version 168.
DE   RecName: Full=V-type proton ATPase subunit a, Golgi isoform;
DE            Short=V-ATPase a 2 subunit;
DE   AltName: Full=Similar to VPH1 protein 1;
DE   AltName: Full=V-ATPase 101 kDa subunit;
DE   AltName: Full=V-ATPase subunit AC115;
DE   AltName: Full=Vacuolar proton translocating ATPase subunit a 2;
GN   Name=STV1; OrderedLocusNames=YMR054W; ORFNames=YM9796.07;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 26109 / X2180;
RX   PubMed=7514599;
RA   Manolson M.F., Wu B., Proteau D., Taillon B.E., Roberts B.T.,
RA   Hoyt M.A., Jones E.W.;
RT   "STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-
RT   ATPase subunit Vph1p.";
RL   J. Biol. Chem. 269:14064-14074(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   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   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=11278748; DOI=10.1074/jbc.M010790200;
RA   Kawasaki-Nishi S., Nishi T., Forgac M.;
RT   "Yeast V-ATPase complexes containing different isoforms of the 100-kDa
RT   a-subunit differ in coupling efficiency and in vivo dissociation.";
RL   J. Biol. Chem. 276:17941-17948(2001).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   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 [LARGE SCALE ANALYSIS].
RX   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   [7]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane
RT   proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND SER-228, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides
RT   insights into evolution.";
RL   Science 325:1682-1686(2009).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Subunit of the integral membrane V0 complex of vacuolar
CC       ATPase essential for assembly and catalytic activity. Is present
CC       only in Golgi- and endosome-residing V-ATPase complexes. Enzymes
CC       containing this subunit have a 4-fold lower ratio of proton
CC       transport to ATP hydrolysis than complexes containing the vacuolar
CC       isoform and do not dissociate V1 and V0 in response to glucose
CC       depletion. V-ATPase is responsible for acidifying a variety of
CC       intracellular compartments in eukaryotic cells.
CC       {ECO:0000269|PubMed:11278748, ECO:0000269|PubMed:7514599}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC       peripheral catalytic V1 complex (components A to H) attached to an
CC       integral membrane V0 proton pore complex (components: a, c, c',
CC       c'', d and e).
CC   -!- SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane
CC       protein. Golgi apparatus membrane; Multi-pass membrane protein.
CC   -!- PTM: Glycosylated.
CC   -!- MISCELLANEOUS: Present with 1084 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000305}.
DR   EMBL; U06465; AAA20596.1; -; Genomic_DNA.
DR   EMBL; Z49703; CAA89764.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09953.1; -; Genomic_DNA.
DR   PIR; S54554; S54554.
DR   RefSeq; NP_013770.1; NM_001182552.1.
DR   ProteinModelPortal; P37296; -.
DR   BioGrid; 35230; 120.
DR   DIP; DIP-4450N; -.
DR   IntAct; P37296; 2.
DR   MINT; MINT-568679; -.
DR   STRING; 4932.YMR054W; -.
DR   TCDB; 3.A.2.2.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; P37296; -.
DR   MaxQB; P37296; -.
DR   PRIDE; P37296; -.
DR   EnsemblFungi; YMR054W; YMR054W; YMR054W.
DR   GeneID; 855076; -.
DR   KEGG; sce:YMR054W; -.
DR   EuPathDB; FungiDB:YMR054W; -.
DR   SGD; S000004658; STV1.
DR   GeneTree; ENSGT00390000004941; -.
DR   HOGENOM; HOG000037059; -.
DR   InParanoid; P37296; -.
DR   KO; K02154; -.
DR   OMA; TIPSFMN; -.
DR   OrthoDB; EOG092C0YCY; -.
DR   BioCyc; YEAST:G3O-32759-MONOMER; -.
DR   Reactome; R-SCE-1222556; ROS, RNS production in phagocytes.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-77387; Insulin receptor recycling.
DR   Reactome; R-SCE-917977; Transferrin endocytosis and recycling.
DR   PRO; PR:P37296; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; IDA:SGD.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:SGD.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IGI:SGD.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
DR   GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
DR   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IBA:GO_Central.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Complete proteome; Endosome; Glycoprotein;
KW   Golgi apparatus; Hydrogen ion transport; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    890       V-type proton ATPase subunit a, Golgi
FT                                isoform.
FT                                /FTId=PRO_0000119225.
FT   TOPO_DOM      1    450       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    451    469       Helical. {ECO:0000255}.
FT   TOPO_DOM    470    471       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    472    488       Helical. {ECO:0000255}.
FT   TOPO_DOM    489    502       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    503    532       Helical. {ECO:0000255}.
FT   TOPO_DOM    533    580       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    581    600       Helical. {ECO:0000255}.
FT   TOPO_DOM    601    618       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    619    639       Helical. {ECO:0000255}.
FT   TOPO_DOM    640    682       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    683    702       Helical. {ECO:0000255}.
FT   TOPO_DOM    703    779       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    780    804       Helical. {ECO:0000255}.
FT   TOPO_DOM    805    828       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    829    867       Helical. {ECO:0000255}.
FT   TOPO_DOM    868    890       Cytoplasmic. {ECO:0000255}.
FT   COILED      113    154       {ECO:0000255}.
FT   COILED      297    347       {ECO:0000255}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   MOD_RES     223    223       Phosphoserine.
FT                                {ECO:0000244|PubMed:17330950,
FT                                ECO:0000244|PubMed:18407956,
FT                                ECO:0000244|PubMed:19779198}.
FT   MOD_RES     228    228       Phosphoserine.
FT                                {ECO:0000244|PubMed:19779198}.
FT   CONFLICT    805    805       Q -> E (in Ref. 1; AAA20596).
FT                                {ECO:0000305}.
SQ   SEQUENCE   890 AA;  101661 MW;  7CA12E37C1E42C67 CRC64;
     MNQEEAIFRS ADMTYVQLYI PLEVIREVTF LLGKMSVFMV MDLNKDLTAF QRGYVNQLRR
     FDEVERMVGF LNEVVEKHAA ETWKYILHID DEGNDIAQPD MADLINTMEP LSLENVNDMV
     KEITDCESRA RQLDESLDSL RSKLNDLLEQ RQVIFECSKF IEVNPGIAGR ATNPEIEQEE
     RDVDEFRMTP DDISETLSDA FSFDDETPQD RGALGNDLTR NQSVEDLSFL EQGYQHRYMI
     TGSIRRTKVD ILNRILWRLL RGNLIFQNFP IEEPLLEGKE KVEKDCFIIF THGETLLKKV
     KRVIDSLNGK IVSLNTRSSE LVDTLNRQID DLQRILDTTE QTLHTELLVI HDQLPVWSAM
     TKREKYVYTT LNKFQQESQG LIAEGWVPST ELIHLQDSLK DYIETLGSEY STVFNVILTN
     KLPPTYHRTN KFTQAFQSIV DAYGIATYKE INAGLATVVT FPFMFAIMFG DMGHGFILFL
     MALFLVLNER KFGAMHRDEI FDMAFTGRYV LLLMGAFSVY TGLLYNDIFS KSMTIFKSGW
     QWPSTFRKGE SIEAKKTGVY PFGLDFAWHG TDNGLLFSNS YKMKLSILMG YAHMTYSFMF
     SYINYRAKNS KVDIIGNFIP GLVFMQSIFG YLSWAIVYKW SKDWIKDDKP APGLLNMLIN
     MFLAPGTIDD QLYSGQAKLQ VVLLLAALVC VPWLLLYKPL TLRRLNKNGG GGRPHGYQSV
     GNIEHEEQIA QQRHSAEGFQ GMIISDVASV ADSINESVGG GEQGPFNFGD VMIHQVIHTI
     EFCLNCISHT ASYLRLWALS LAHAQLSSVL WDMTISNAFS SKNSGSPLAV MKVVFLFAMW
     FVLTVCILVF MEGTSAMLHA LRLHWVEAMS KFFEGEGYAY EPFSFRAIIE
//
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