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Database: UniProt
Entry: Q6BZT1_YARLI
LinkDB: Q6BZT1_YARLI
Original site: Q6BZT1_YARLI 
ID   Q6BZT1_YARLI            Unreviewed;       804 AA.
AC   Q6BZT1;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   ORFNames=YALI0_F31119g {ECO:0000313|EMBL:CAG78894.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG78894.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG78894.1, 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., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., 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-ATPase), a
CC       multimeric enzyme that catalyzes the translocation of protons across
CC       the membranes. Required for assembly and activity of the V-ATPase.
CC       {ECO:0000256|RuleBase:RU361189}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00009904, ECO:0000256|RuleBase:RU361189}.
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DR   EMBL; CR382132; CAG78894.1; -; Genomic_DNA.
DR   RefSeq; XP_506081.1; XM_506081.1.
DR   AlphaFoldDB; Q6BZT1; -.
DR   STRING; 284591.Q6BZT1; -.
DR   EnsemblFungi; CAG78894; CAG78894; YALI0_F31119g.
DR   GeneID; 2907662; -.
DR   KEGG; yli:YALI0F31119g; -.
DR   VEuPathDB; FungiDB:YALI0_F31119g; -.
DR   HOGENOM; CLU_005230_0_2_1; -.
DR   InParanoid; Q6BZT1; -.
DR   OMA; FYLWFFL; -.
DR   OrthoDB; 1967517at2759; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
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:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0071474; P:cellular hyperosmotic response; IEA:EnsemblFungi.
DR   GO; GO:0071469; P:cellular response to alkaline pH; IEA:EnsemblFungi.
DR   GO; GO:0006797; P:polyphosphate metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0065003; P:protein-containing complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR   PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 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   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW   ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM        389..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        435..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        511..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        540..560
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        603..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        709..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        732..762
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          658..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          110..137
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   804 AA;  91132 MW;  BC4EBFFBDBEAED57 CRC64;
     MPESNQSGEA IFRSAEMSLV QLYIASEIGR ETVMSLGELG LVQFRDLNKK VNVFQRNFIQ
     EVRRLDNVDR QLRLFERECE KEGLTLEDGD PHSAASASDI DALVALGDTL EKRITELRDA
     EERVTESQTE SQELRAVLTE TAKFFDQRAG GGSRDIESQS LRNVQFVAGV IPRDRVEVLE
     RILWRVLRGN LFLETAEFGG DDGDKSVFIV FSHGAEIISK VERIAKTLDA HLYWIADDVR
     ERENQLQEVN QKLSDIDIVS QRTRHTLNTE LRLIAQKLPN WRVIVIKEKS VYSTLNLFQY
     DTNRKVLIGE GWVPKDDISK VKTTLKSITD EADVEIPSVL NVLETSRTPP TYHRTNKFTS
     AFQLIVDAYG ISSYREVNPG LPTIVTFPFM FAIMFGDIGH GFILFLAAFA LVYYEAKIGK
     MKRDEIFDMA YQGRYILLLM GAFSMYTGFM YNDIFSKSMT LFKPGWAWPE SWKEGQTIQA
     HQTGVYAFGL DPTWHGTDNN LLFTNSYKMK LSVLMGHVHM TYSFFLSLVN YIFFGSVVDF
     WGNFVPGLLF MQGIFGYLAL TIVYKWTVDW VAIGQQPPSL LDTLINMFLA PGKVPVPLYP
     GQAYVQVILV VIALICVPWL LLVKPLWLRR DMQKHEYERV SGNGGPLDLL DAPDQLEETV
     GDTPGDATGG DDFDDEEEEE HGFGDIVIHQ VIHTIEFCLN CVSHTASYLR LWALSLAHAQ
     LSTVLWDMTL QAAFGFSGVV GVIMTVILFG MWFVLTVVIL VCMEGTSAML HSLRLHWVES
     MSKFFEGEGT PYEPFSFKDE LATN
//
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