VPP2_YEAST
ID VPP2_YEAST Reviewed; 890 AA.
AC P37296; D6VZM9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 201.
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; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=7514599; DOI=10.1016/s0021-9258(17)36755-8;
RA Manolson M.F., Wu B., Proteau D., Taillon B.E., Roberts B.T., Hoyt M.A.,
RA 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., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION, AND SUBUNIT.
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 a-
RT 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., 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 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 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 BY
RP 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 BY
RP 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 phosphoproteome
RT 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 insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
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: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons (PubMed:7514599, PubMed:11278748). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments
CC (PubMed:11278748, PubMed:7514599). Is present only in Golgi- and
CC endosome-residing V-ATPase complexes; enzymes containing this subunit
CC have a 4-fold lower ratio of proton transport to ATP hydrolysis than
CC complexes containing the vacuolar isoform and do not dissociate V1 and
CC V0 in response to glucose depletion (PubMed:11278748, PubMed:7514599).
CC {ECO:0000269|PubMed:11278748, ECO:0000269|PubMed:7514599}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC VOA1). {ECO:0000269|PubMed:11278748, ECO:0000269|PubMed:7514599}.
CC -!- INTERACTION:
CC P37296; P32366: VMA6; NbExp=2; IntAct=EBI-18479, EBI-20201;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:7514599};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:7514599}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- PTM: Glycosylated.
CC -!- MISCELLANEOUS: Present with 1084 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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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 PDB; 6O7U; EM; 3.10 A; a=1-890.
DR PDB; 6O7V; EM; 6.60 A; a=1-890.
DR PDB; 6O7W; EM; 7.00 A; a=1-890.
DR PDB; 6O7X; EM; 8.70 A; a=1-890.
DR PDBsum; 6O7U; -.
DR PDBsum; 6O7V; -.
DR PDBsum; 6O7W; -.
DR PDBsum; 6O7X; -.
DR AlphaFoldDB; P37296; -.
DR BMRB; P37296; -.
DR SMR; P37296; -.
DR BioGRID; 35230; 131.
DR ComplexPortal; CPX-1192; Vacuolar proton translocating ATPase complex, Golgi variant.
DR DIP; DIP-4450N; -.
DR IntAct; P37296; 2.
DR MINT; P37296; -.
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 PaxDb; P37296; -.
DR PRIDE; P37296; -.
DR EnsemblFungi; YMR054W_mRNA; YMR054W; YMR054W.
DR GeneID; 855076; -.
DR KEGG; sce:YMR054W; -.
DR SGD; S000004658; STV1.
DR VEuPathDB; FungiDB:YMR054W; -.
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_0_1; -.
DR InParanoid; P37296; -.
DR OMA; MIFFKWL; -.
DR BioCyc; YEAST:G3O-32759-MON; -.
DR Reactome; R-SCE-1222556; ROS and 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 Reactome; R-SCE-9639288; Amino acids regulate mTORC1.
DR PRO; PR:P37296; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P37296; protein.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
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; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
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:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0048388; P:endosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0007035; P:vacuolar acidification; IMP:SGD.
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 3D-structure; Acetylation; Coiled coil; Endosome; Glycoprotein;
KW Golgi apparatus; Hydrogen ion transport; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..890
FT /note="V-type proton ATPase subunit a, Golgi isoform"
FT /id="PRO_0000119225"
FT TOPO_DOM 1..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..471
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..580
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 601..618
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..682
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..779
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 780..804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 805..828
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 829..867
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 868..890
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 113..154
FT /evidence="ECO:0000255"
FT COILED 297..347
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 805
FT /note="Q -> E (in Ref. 1; AAA20596)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 16..24
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 58..77
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 119..163
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:6O7U"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:6O7U"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 321..351
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 354..371
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 392..405
FT /evidence="ECO:0007829|PDB:6O7U"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 434..443
FT /evidence="ECO:0007829|PDB:6O7U"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 457..468
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 472..487
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 489..493
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 499..506
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 508..524
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 574..597
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 599..607
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 611..625
FT /evidence="ECO:0007829|PDB:6O7U"
FT TURN 626..628
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 629..641
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 644..647
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 655..663
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 676..688
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 690..702
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 768..790
FT /evidence="ECO:0007829|PDB:6O7U"
FT TURN 791..794
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 795..814
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:6O7U"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 827..846
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 847..851
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 853..865
FT /evidence="ECO:0007829|PDB:6O7U"
FT TURN 866..871
FT /evidence="ECO:0007829|PDB:6O7U"
FT HELIX 885..887
FT /evidence="ECO:0007829|PDB:6O7U"
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
