(data stored in SCRATCH zone)

SWISSPROT: Q6FK70_CANGA

ID   Q6FK70_CANGA            Unreviewed;       345 AA.
AC   Q6FK70;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 72.
DE   RecName: Full=V-type proton ATPase subunit {ECO:0000256|PIRNR:PIRNR018497};
GN   OrderedLocusNames=CAGL0M00660g {ECO:0000313|CGD:CAL0136767,
GN   ECO:0000313|EMBL:CAG62350.1};
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:CAG62350.1, 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: Vacuolar ATPase is responsible for acidifying a variety
CC       of intracellular compartments in eukaryotic cells. The active
CC       enzyme consists of a catalytic V1 domain attached to an integral
CC       membrane V0 proton pore complex. This subunit is a non-integral
CC       membrane component of the membrane pore domain and is required for
CC       proper assembly of the V0 sector. Might be involved in the
CC       regulated assembly of V1 subunits onto the membrane sector or
CC       alternatively may prevent the passage of protons through V0 pores.
CC       {ECO:0000256|PIRNR:PIRNR018497}.
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.
CC       {ECO:0000256|PIRNR:PIRNR018497}.
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC       {ECO:0000256|PIRNR:PIRNR018497}.
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DR   EMBL; CR380959; CAG62350.1; -; Genomic_DNA.
DR   RefSeq; XP_449374.1; XM_449374.1.
DR   ProteinModelPortal; Q6FK70; -.
DR   STRING; 284593.XP_449374.1; -.
DR   EnsemblFungi; CAG62350; CAG62350; CAGL0M00660g.
DR   KEGG; cgr:CAGL0M00660g; -.
DR   CGD; CAL0136767; CAGL0M00660g.
DR   EuPathDB; FungiDB:CAGL0M00660g; -.
DR   eggNOG; KOG2957; Eukaryota.
DR   eggNOG; COG1527; LUCA.
DR   HOGENOM; HOG000199065; -.
DR   InParanoid; Q6FK70; -.
DR   KO; K02146; -.
DR   OMA; FMDFITY; -.
DR   OrthoDB; EOG092C3P8T; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0007034; P:vacuolar transport; IEA:EnsemblFungi.
DR   Gene3D; 1.20.1690.10; -; 2.
DR   InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR   InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR   InterPro; IPR035067; V-type_ATPase_suC.
DR   PANTHER; PTHR11028; PTHR11028; 1.
DR   Pfam; PF01992; vATP-synt_AC39; 1.
DR   PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR   SUPFAM; SSF103486; SSF103486; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FK70.
DR   SWISS-2DPAGE; Q6FK70.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Hydrogen ion transport {ECO:0000256|PIRNR:PIRNR018497};
KW   Ion transport {ECO:0000256|PIRNR:PIRNR018497};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Transport {ECO:0000256|PIRNR:PIRNR018497}.
SQ   SEQUENCE   345 AA;  39849 MW;  9717B46D9CEA27A1 CRC64;
     MEGLYFNVDN GFLEGLIRGY RNGLLTNNQY INLTQCDNLD DLKLQLSSTD YGNFLSQVSN
     DALTTSVMQE KASEKLYKEF GYIRDQSSGL TRKFIDYITY SYMIDNVALM ITGTIHERDK
     SEILSRCHPL GWFDTLPTLS VATDLESLYE TVLVDTPLAP FFRDCFDAAD ELDDLNIEII
     RNKLYKAYLE DFYKFVSEEI DEPSREIMQT LLGFEADRRS INIALNSLQS PDLDPALKKQ
     LLPEIGKLYP VATEQLANAK DFESIRAVLG QVPDYRNALE SGSLEDHFYK LEMDLCRDAF
     TQQFTISTIW AWMKSREQEV RNITWIAECI AQNQRERINN YISVY
//

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