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Database: UniProt
Entry: Q6C6F6_YARLI
LinkDB: Q6C6F6_YARLI
Original site: Q6C6F6_YARLI 
ID   Q6C6F6_YARLI            Unreviewed;       820 AA.
AC   Q6C6F6;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   05-JUL-2017, entry version 67.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=YALI0_E09933g {ECO:0000313|EMBL:CAG79347.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG79347.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG79347.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
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; CR382131; CAG79347.1; -; Genomic_DNA.
DR   RefSeq; XP_503756.1; XM_503756.1.
DR   ProteinModelPortal; Q6C6F6; -.
DR   STRING; 4952.XP_503756.1; -.
DR   EnsemblFungi; CAG79347; CAG79347; YALI0_E09933g.
DR   GeneID; 2912577; -.
DR   KEGG; yli:YALI0E09933g; -.
DR   HOGENOM; HOG000037059; -.
DR   InParanoid; Q6C6F6; -.
DR   KO; K02154; -.
DR   OMA; TIPSFMN; -.
DR   OrthoDB; EOG092C0YCY; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
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: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; IEA:EnsemblFungi.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
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; IBA:GO_Central.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001300};
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:UP000001300};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    413    437       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    458    476       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    536    556       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    568    589       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    629    648       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    730    753       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    759    782       Helical. {ECO:0000256|RuleBase:RU361189}.
SQ   SEQUENCE   820 AA;  93030 MW;  DE3515B781F4DF7C CRC64;
     MEREAIFRSA EMSLVQLYVA SEIGRDVVAA LGELGVVMFR DLNTSVNVFQ RSFIKEIRRV
     DGVERQLRGL RAHIDKHGVA IDEQPEGVAA PTLDEVDNMC HQVGALEERV GHLDTTWNEL
     VDKRALILER REMVQTAGIF FADARENRHE IRASLEGDRA GLLYDLDDPQ PDVEAATVTW
     NSVAGLSFVT GVIPSTKTAI FERILWRSLR GNLYFRHQAI EKPLAGVRKD VFIVFGHGES
     LLAKIKRIAL TLDATLYPVS EDFDTRREQV EELNIKLADV DNVLGSTNNA LMTELALAAN
     TLPHWEVLAN KEKAIYHTLN MFNYDQTRRC LIAEGWIPKA DFRAVQEVLR DVTLSSGVAI
     NSILNEIKTS KTPPTFHRTN KFTAAFQLIV DAYGIASYQE INPGLATVVT FPFMFAIMFG
     DLGHGVILAL AGLVMVLKEK SILKMRNRDE IFDMAFSGRY IVLLMGIFSL YTGLMYNDIF
     SKSMTLFRSG WAWPESWEEK ERITAHQTGV YPFGLDPAWH GTDNNLLFTN SYKMKLSILM
     GFTHMSYSFF FSFLNYKFFN SQIDIWGNFV PGLLFMQSIF GYLSLTIVYK WCVDWIAKDK
     TPPGLLNMLI NMFLSPGTID APLYPGQKFV QIILVLIALV CVPWLLLLKP LYLRRQHKQT
     QYDAIRQPNA YHIGDTDDDA DSFDMTIEEF EEEGEGHEQF EFGEVMIHQV IHTIEFCLNC
     VSHTASYLRL WALSLAHAQL STVLWDMTIQ GAFGPTGPAG VAMVVIMFAM WFVLTVVILV
     MMEGTSAMLH SLRLHWVEAM SKFFEGEGYA YAPFNFKDQQ
//
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