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Database: UniProt
Entry: Q6FWT8_CANGA
LinkDB: Q6FWT8_CANGA
Original site: Q6FWT8_CANGA 
ID   Q6FWT8_CANGA            Unreviewed;       889 AA.
AC   Q6FWT8;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-SEP-2017, entry version 74.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   OrderedLocusNames=CAGL0C02959g {ECO:0000313|CGD:CAL0127310,
GN   ECO:0000313|EMBL:CAG58212.1};
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:CAG58212.1, 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; CR380949; CAG58212.1; -; Genomic_DNA.
DR   RefSeq; XP_445306.1; XM_445306.1.
DR   ProteinModelPortal; Q6FWT8; -.
DR   STRING; 284593.XP_445306.1; -.
DR   EnsemblFungi; CAG58212; CAG58212; CAGL0C02959g.
DR   GeneID; 2886830; -.
DR   KEGG; cgr:CAGL0C02959g; -.
DR   CGD; CAL0127310; CAGL0C02959g.
DR   EuPathDB; FungiDB:CAGL0C02959g; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   HOGENOM; HOG000037059; -.
DR   InParanoid; Q6FWT8; -.
DR   KO; K02154; -.
DR   OMA; WTAYDAH; -.
DR   OrthoDB; EOG092C0YCY; -.
DR   Proteomes; UP000002428; Chromosome C.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:EnsemblFungi.
DR   GO; GO:0016049; P:cell growth; IEA:EnsemblFungi.
DR   GO; GO:0043623; P:cellular protein complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0006797; P:polyphosphate metabolic process; IEA:EnsemblFungi.
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   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    424    448       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    469    486       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    546    567       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    579    601       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    640    658       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    746    769       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    775    798       Helical. {ECO:0000256|RuleBase:RU361189}.
SQ   SEQUENCE   889 AA;  101705 MW;  3F150F47777B4903 CRC64;
     MVRSEEEAIF RSAEMSLVQF YIPQEIARDT AYTLGQLGLV QFRDLNAKKQ AFQRAYVDDI
     RRLDNVERVY RYLYSLLQKH RIQLFENGEL RDGSVGGDAV AEPPSGSAID DHVQNATFLE
     ERLMEMEDGC DQIKRQRTDL EQYRFLLRTA DEFFSQDMDA PQSQANDTPQ PTDEEMGNAE
     TTRYGGANSS VNYVSGVIPS EKTHILEQIL WRTLRGNLLF KHVAIEKPLY DEKTGKYVKK
     DAFIVFSHGD LIIKRIRKIA ESLDAKLYFV DSRSDLRSEK LLEINRNLQD LNTVLQTAMV
     TLESELYAIS KELNLWFHEV SKEKAVFETL NKFNNDENRK TLIAEGWIPM DQIDILRAKL
     EEMVNRLGID FPSTLQVLET TSTPPTYHRT NKFTEAFQAI CDCYGIAQYR EVNPGLPTVV
     TFPFMFAIMF GDLGHGCIMF LAALTLVLNE KALGKMKRDE IFDMAYSGRY ILLLMGLFSM
     YTGFLYNDIF SKSMTFFKSG WEWPESWHKG EAIFAKQVGT YPIGLDWAWH GAENNLLFTN
     SYKMKLSILM GFIHMTYSYM FSLVNHLHFN SFIDIVGNFI PGLLFMQGIF GYLSICIVYK
     WTKDWIKDGK AAPSLLNMLI NMFLSPGNID EPLYPHQAKV QMVLLVTALI CVPWLLFVKP
     LHFKFTHSDN SGKASSNDGE YHEETENLLP DVNDALDLIE EEEIAEGEES HEEHSEEFGD
     VMIHQVIHTI EFCLNCVSHT ASYLRLWALS LAHAQLSSVL WSMTIGLSFG MSGFMGVFAV
     VFLFALWFIL TVCVLVVMEG TSAMLHSLRL HWVESMSKFF VGDGTLYEPF KLIDRDLIEE
     SIEAGVVSTI DVDTEESVED FSNLDEDGSP RDEPGFIRRF SGIFTRSSD
//
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