VATA_ASHGO
ID VATA_ASHGO Reviewed; 617 AA.
AC Q9UVJ8; Q75AG6;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 3.
DT 03-AUG-2022, entry version 154.
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};
DE AltName: Full=V-ATPase 69 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit alpha;
GN Name=VMA1; OrderedLocusNames=ADR102W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=10092625; DOI=10.1074/jbc.274.14.9442;
RA Foerster C., Santos M.A., Ruffert S., Kraemer R., Revuelta J.L.;
RT "Physiological consequence of disruption of the VMA1 gene in the riboflavin
RT overproducer Ashbya gossypii.";
RL J. Biol. Chem. 274:9442-9448(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 241.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 (By similarity). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments (By
CC similarity). {ECO:0000250|UniProtKB:P17255}.
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: Endomembrane system
CC {ECO:0000250|UniProtKB:P17255}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P17255}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Membranes of
CC various intracellular acidic compartments.
CC {ECO:0000250|UniProtKB:P17255}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AJ009881; CAB51771.1; -; Genomic_DNA.
DR EMBL; AE016817; AAS52022.2; -; Genomic_DNA.
DR RefSeq; NP_984198.2; NM_209551.2.
DR AlphaFoldDB; Q9UVJ8; -.
DR SMR; Q9UVJ8; -.
DR STRING; 33169.AAS52022; -.
DR PRIDE; Q9UVJ8; -.
DR EnsemblFungi; AAS52022; AAS52022; AGOS_ADR102W.
DR GeneID; 4620347; -.
DR KEGG; ago:AGOS_ADR102W; -.
DR eggNOG; KOG1352; Eukaryota.
DR HOGENOM; CLU_008162_3_1_1; -.
DR InParanoid; Q9UVJ8; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000000591; Chromosome IV.
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:0019538; P:protein metabolic process; IEA:EnsemblFungi.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW ATP-binding; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport; Vacuole.
FT CHAIN 1..617
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000144588"
FT BINDING 257..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
SQ SEQUENCE 617 AA; 67800 MW; B3B224AC6C9F222F CRC64;
MAGALENARK EIKRISLEDH NENEYGQIYS VSGPVVVAEN MVGCAMYELV KVGHHNLVGE
VIRLDGDKAT IQVYEETAGV TVGDPVLRTG KPLSVELGPG LMETIYDGIQ RPLKAIKEQS
QSIYIPRGVD APALSREVKW AFKPGKLGVG DHISGGDIFG SIFENSLLED HKILLPPRAR
GTITWIAPAG EYTVDETVLE VEFDGKKYSY SMFHTWPVRV PRPVTEKLSA DYPLLTGQRV
LDSLFPCVQG GTTCIPGAFG CGKTVISQSL SKYSNSDAII YVGCGERGNE MAEVLMEFPE
LFTEVNGRKE PIMKRTTLVA NTSNMPVAAR EASIYTGITL AEYFRDQGKN VSMIADSSSR
WAEALREISG RLGEMPADQG FPAYLGAKLA SFYERAGKAV ALGSPDRVGS VSIVAAVSPA
GGDFSDPVTT STLGITQVFW GLDKKLAQRK HFPSINTSVS YSKYTNVLNK YYDSNYPEFP
VLRDRIKEIL SNAEELEQVV QLVGKSALSD KDKIVLDVAT LIKEDFLQQN GYSTYDAFCP
IWKTYDMMKA FVSYFDEAQK SVSNGANWAV LSEATGDVKH AVSSSKFFEP SRGEREVHAE
FEKLFASIQE RFAESTD
