VATA_CANAL
ID VATA_CANAL Reviewed; 617 AA.
AC Q5AJB1; A0A1D8PJ97;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=V-type proton ATPase catalytic subunit A;
DE Short=V-ATPase subunit A;
DE EC=7.1.2.2 {ECO:0000250|UniProtKB:P17255};
GN Name=TFP1 {ECO:0000303|PubMed:25220074};
GN OrderedLocusNames=CAALFM_C301630WA; ORFNames=CaO19.9249;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUMOYLATION.
RX PubMed=21209325; DOI=10.1091/mbc.e10-07-0632;
RA Leach M.D., Stead D.A., Argo E., Brown A.J.;
RT "Identification of sumoylation targets, combined with inactivation of SMT3,
RT reveals the impact of sumoylation upon growth, morphology, and stress
RT resistance in the pathogen Candida albicans.";
RL Mol. Biol. Cell 22:687-702(2011).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25220074; DOI=10.1016/j.fgb.2014.08.012;
RA Jia C., Yu Q., Xu N., Zhang B., Dong Y., Ding X., Chen Y., Zhang B.,
RA Xing L., Li M.;
RT "Role of TFP1 in vacuolar acidification, oxidative stress and filamentous
RT development in Candida albicans.";
RL Fungal Genet. Biol. 71:58-67(2014).
CC -!- FUNCTION: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase
CC (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1)
CC that hydrolyzes ATP and a membrane integral complex (V0) that
CC translocates protons (PubMed:25220074). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments
CC (PubMed:25220074). Mediates oxidative stress response, filamentous
CC growth, and plays an important role in virulence (PubMed:25220074).
CC {ECO:0000269|PubMed:25220074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000250|UniProtKB:P17255};
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC VOA1). {ECO:0000250|UniProtKB:P17255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25220074}.
CC Endomembrane system {ECO:0000250|UniProtKB:P17255}; Peripheral membrane
CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Vacuole membrane
CC {ECO:0000269|PubMed:25220074}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Localizes in
CC cytoplasm under glucose deprivation conditions and to the vacuolar
CC membrane in presence of glucose. {ECO:0000269|PubMed:25220074}.
CC -!- PTM: Is a probable target for sumoylation.
CC {ECO:0000269|PubMed:21209325}.
CC -!- DISRUPTION PHENOTYPE: Leads to a defect in vacuolar acidification and
CC higher sensitivity to oxidants such as H(2)O(2) or menadione. Reduces
CC strongly virulence in mice. {ECO:0000269|PubMed:25220074}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|RuleBase:RU000339}.
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DR EMBL; CP017625; AOW28205.1; -; Genomic_DNA.
DR RefSeq; XP_019330831.1; XM_019475286.1.
DR AlphaFoldDB; Q5AJB1; -.
DR SMR; Q5AJB1; -.
DR STRING; 237561.Q5AJB1; -.
DR PRIDE; Q5AJB1; -.
DR GeneID; 3636662; -.
DR KEGG; cal:CAALFM_C301630WA; -.
DR CGD; CAL0000187512; TFP1.
DR VEuPathDB; FungiDB:C3_01630W_A; -.
DR eggNOG; KOG1352; Eukaryota.
DR HOGENOM; CLU_008162_3_1_1; -.
DR InParanoid; Q5AJB1; -.
DR OMA; RIVKTFW; -.
DR OrthoDB; 241249at2759; -.
DR PHI-base; PHI:3321; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0090465; P:arginine homeostasis; IEA:EnsemblFungi.
DR GO; GO:0090464; P:histidine homeostasis; IEA:EnsemblFungi.
DR GO; GO:0090463; P:lysine homeostasis; IEA:EnsemblFungi.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR005725; ATPase_V1-cplx_asu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR PANTHER; PTHR43607; PTHR43607; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport;
KW Ubl conjugation; Vacuole; Virulence.
FT CHAIN 1..617
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000431486"
FT BINDING 257..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT SITE 460
FT /note="Required for activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10106"
SQ SEQUENCE 617 AA; 67607 MW; D1573ED986E7807F CRC64;
MAGALENATK EIKRLSLEDT HESQYGQIYS VSGPVVVAEN MIGCAMYELV KVGHDNLVGE
VIRINGDKAT IQVYEETAGV TVGDPVLRTG KPLSVELGPG LMETIYDGIQ RPLKAIKDES
QSIYIPRGID VPALSRTTQY DFTPGKLKVG DHITGGDIFG SIYENSLLDD HKILLPPRAR
GTITSIAESG SYNVEDTVLE VEFDGKKHKY SMMHTWPVRV PRPVAEKLSA DYPLLTGQRV
LDSLFPCVQG GTTCIPGAFG CGKTVISQSL SKFSNSDVII YVGCGERGNE MAEVLMEFPE
LYTEISGRKE PIMKRTTLVA NTSNMPVAAR EASIYTGITL AEYFRDQGKN VSMIADSSSR
WAEALREISG RLGEMPADQG FPAYLGAKLA SFYERAGKAT ALGSPDRIGS VSIVAAVSPA
GGDFSDPVTT ATLGITQVFW GLDKKLAQRK HFPSINTSVS YSKYTNVLNK YYDSNYPEFA
QLRDKIREIL SNAEELEQVV QLVGKSALSD SDKITLDVAT LIKEDFLQQN GYSSYDAFCP
IWKTFDMMRA FISYYDEAQK AVANGAQWSK LAESTSDVKH SVSSAKFFEP SRGQKEGEKE
FSELLSTISE RFAEASE
