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Database: UniProt
Entry: Q6FU51_CANGA
LinkDB: Q6FU51_CANGA
Original site: Q6FU51_CANGA 
ID   Q6FU51_CANGA            Unreviewed;       910 AA.
AC   Q6FU51;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-SEP-2017, entry version 77.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=STV1 {ECO:0000313|CGD:CAL0129296};
GN   OrderedLocusNames=CAGL0F06347g {ECO:0000313|CGD:CAL0129296,
GN   ECO:0000313|EMBL:CAG59167.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG59167.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
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DR   EMBL; CR380952; CAG59167.1; -; Genomic_DNA.
DR   RefSeq; XP_446243.1; XM_446243.1.
DR   ProteinModelPortal; Q6FU51; -.
DR   STRING; 284593.XP_446243.1; -.
DR   EnsemblFungi; CAG59167; CAG59167; CAGL0F06347g.
DR   GeneID; 2887756; -.
DR   KEGG; cgr:CAGL0F06347g; -.
DR   CGD; CAL0129296; STV1.
DR   EuPathDB; FungiDB:CAGL0F06347g; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   HOGENOM; HOG000037059; -.
DR   InParanoid; Q6FU51; -.
DR   KO; K02154; -.
DR   OMA; TIPSFMN; -.
DR   OrthoDB; EOG092C0YCY; -.
DR   Proteomes; UP000002428; Chromosome F.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; IEA:EnsemblFungi.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:EnsemblFungi.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    499    522       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    543    561       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    621    639       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    651    673       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    713    732       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    816    836       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    848    871       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   COILED      162    189       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   910 AA;  104446 MW;  7EC8204A32DE634A CRC64;
     MAKHEAIYRS ADMTYIQLYI PQEIVREVVC LLGKLGNVMF RDLNSDLSAF QRGYVARLRR
     LEDVGRSVDY MKRVSEKHRE ATARYMPQLF EDEELDDLEF NATNDNPGSN TGDDNESLLS
     QQNLDNLVRP SRRVNPHALF PQLLRSLEVH SMDTINDIIH EITEFESRVK QLDDSLESLR
     DKLNVLIEKR HIVFECSRYI KFNPGILGRI SNSNDANVSG SQLDVTDFTA LPEEANDNLS
     DFSFDIDEDT AEDNQNNNND DDILMLEQGF HNKFMIAGAI RRDKVMILNR ILWRLLRGNL
     FFQNFPVEKP MMENGELVEK DCFLIFTHGD TLSAKIKRVV DSLGGSMISL DQISQQTIQE
     LNDRISDLEQ VLESTERTLH TELLLINDQL SVWHAVFRRE TYIYATLNLF RQETQGLVAE
     GWIPYEELQT LKNTLKDYSE SIGSEYTTVI SVIITNRSPP TYHRVNKFTQ AFQSIVDAYG
     IATYKEINPG LATVVTFPFM FAIMFGDAGH GFIVLLIALY LVMNERKFDN MKREEMFDMA
     YTGRYVLLLM GAFSIYTGLM YNDIFSRSMT LFSSGWEWPT TFKKGETLEA KQVGTYAFGL
     DWAWHGTENN LIFTNSYKMK LSILMGFIHM SYSYMFSYIN YRHRKSRVDI IGNFIPGLIF
     MQSIFGYLSW AIVFKWSKDW IKDGKPAPGL LNMLINMFLA PGTIDEQLYS GQAVLQTILL
     LAALVCVPWL LLYKPLMLRK QHANGETNYS SLQHPTADDT MTSESIIDNE VVITDFDTDE
     SESHGFNFGD VMIHQVIHTI EFCLNCISHT ASYLRLWALS LAHAQLSTVL WNMTIANSFS
     SKDPGSPLAV FMVVFLFAFW FILTVAVLVL MEGTSAMLHA LRLHWVEAMS KFFEGNGYAY
     EPFSFDLLTE
//
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