ID G8B5N6_CANPC Unreviewed; 920 AA.
AC G8B5N6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN OrderedLocusNames=CPAR2_603460 {ECO:0000313|CGD:CAL0000145149,
GN ECO:0000313|EMBL:CCE39928.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE39928.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
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; HE605202; CCE39928.1; -; Genomic_DNA.
DR AlphaFoldDB; G8B5N6; -.
DR STRING; 578454.G8B5N6; -.
DR EnsemblFungi; CPAR2_603460-T; CPAR2_603460-T-p1; CPAR2_603460.
DR CGD; CAL0000145149; CPAR2_603460.
DR VEuPathDB; FungiDB:CPAR2_603460; -.
DR eggNOG; KOG2189; Eukaryota.
DR Proteomes; UP000005221; Chromosome 6.
DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblFungi.
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:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; 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:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR Pfam; PF01496; V_ATPase_I; 2.
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:UP000005221};
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 477..501
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 522..540
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 606..628
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 635..659
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 699..718
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 827..846
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 858..881
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT COILED 283..310
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 920 AA; 105413 MW; 4BC67EF1468BB9BC CRC64;
MNASNEAIFR SAPMTLVQFY VTIELAREMV GMLGNLGAVQ FRDLNSKLTP FQRTFISELK
SIDAMISQLT FLRSTMDKLG TVTGDLHVNL RADMRPMPST SEMDEFRTKL NDYHERIRHL
NHSYGNLDSQ KLKYIENRYV INTLNNFHRS SLVDNEHDHF DDHHENTELD SEIALLATRQ
NNSLELGLEV HNWEESNFNS IAGTIARDKV PVLRNILWRL LRGNLYFHDI PIDEEFPVND
KSTEMVYKNV FIIFIHGDIL RSRVRKIIQS LDGIIFNNAS GNADARRATL DEINDRIEEL
TNVVDNTKDQ LITELKVFQE LYPDYSYIVQ REKLVYETLD KFDEDSTRRC LVGEGWIPSV
DFEKIRGALR KLVKEKTRRD RRSSNQSSES LDISVDAETD TFVIDDSDHD VSGFEFNGEE
AGSLIAVVNK LSTNRTPPTY HKTNKFTAAF QSIIDAYGIA TYEEVNPGLA TIITFPFMFA
IMFGDLGHGF IVLLMALYLI VNEVAFGAMR NKDEIFEMAF NGRYIILLMG IFSMYTGFIY
NDIFSKSMAI FGSGWEYVFP DNYDPQKGGT LTATKIKGKT YPIGLDWAWH GTENNLLFTN
SYKMKLSVLM GYVHMNYSLM FSLVNYLYFK RRVDIIGNFI PGFLFMTSIF GYLALTIVYK
WSVDWLGTGR QPPGLLNMLI NMFLSPGTVE EQLYPGQKFI QVVLVLIALI CVPWLLIYKP
LTLKRQNDKA IKLGYTDLHS QRNHSMMLHE EEAALELERE LNNDPTDEEV ETDDEFRFPN
DIEPMFHSAA AHGDDHGEFN FGDIVIHQVI HTIEFCLNCV SHTASYLRLW ALSLAHAQLS
TVLWSMTIQN AFGKTGAVGI IATVCLFAMW FSLTVCILVL MEGTSAMLHS LRLHWVEAMS
KFFEGEGYAY EPFNFKSIDV
//
