ID   VATA_VIGRR              Reviewed;         623 AA.
AC   P13548; Q41683;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=V-type proton ATPase catalytic subunit A;
DE            Short=V-ATPase subunit A;
DE            EC=7.1.2.2;
DE   AltName: Full=V-ATPase 69 kDa subunit;
DE   AltName: Full=VAA3-1;
DE   AltName: Full=Vacuolar proton pump subunit alpha;
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chiu S.-J., Hung S.-H., Lin L.-Y., Pan R.L.;
RT   "A cDNA clone encoding the A subunit of the vacuolar H+-ATPase from
RT   etiolated mung bean seedlings.";
RL   (er) Plant Gene Register PGR95-083(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-26.
RC   STRAIN=cv. Wilczek;
RX   PubMed=2137412; DOI=10.1111/j.1432-1033.1990.tb15362.x;
RA   Matuura-Endo C., Maeshima M., Shizuo Y.;
RT   "Subunit composition of vacuolar membrane H(+)-ATPase from mung bean.";
RL   Eur. J. Biochem. 187:745-751(1990).
CC   -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of vacuolar
CC       ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a
CC       variety of intracellular compartments in eukaryotic cells.
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   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (main components: subunits A, B, C, D, E, and F)
CC       attached to an integral membrane V0 proton pore complex (main
CC       component: the proteolipid protein).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; U26709; AAC49174.1; -; mRNA.
DR   RefSeq; NP_001304241.1; NM_001317312.1.
DR   AlphaFoldDB; P13548; -.
DR   SMR; P13548; -.
DR   STRING; 3916.P13548; -.
DR   GeneID; 106773955; -.
DR   KEGG; vra:106773955; -.
DR   Proteomes; UP000087766; Chromosome 9.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
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; IEA:UniProtKB-EC.
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; Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Nucleotide-binding; Reference proteome; Translocase;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2137412"
FT   CHAIN           2..623
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000144583"
FT   BINDING         252..259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        20
FT                   /note="E -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   623 AA;  68681 MW;  2D0E0492CE7D7826 CRC64;
     MPAVYGARLT TFEDSEKESE YGYVRKVSGP VVVADGMAGA AMYELVRVGR DNLIGEIIRL
     EGDSATIQVY EETAGLMVND PVLRTHKPLS VELGPGILGN IFDGIQRPLK TIAKRSGDVY
     IPRGVSVPAL DKDTLWEFQP KKIGEGDLLT GGDLYATVFE NTLMQHHIAL PPDAMGKITY
     IAPPGQYSIT DTVLELEFQG VKKKFTMLQT WPVRTPRPVA SKLAADTPLL TGQRVLDALF
     PSVLGGTCAI PGAFGCGKTV ISQALSKYSN SDAVVYVGCG ERGNEMAEVL MDFPQLTMTL
     PDGREESVMK RTTLVANTSN MPVAAREASI YTGITLAEYF RDMGYNVSMM ADSTSRWAEA
     LREISGRLAE MPADSGYPAY LAARLASFYE RPGKVKCLGG PERTGSVTIV GAVSPPGGDF
     SDPVTSATLS IVQVFWGLDK KLAQRKHFPS VNWLISYSKY STALESFYEQ FDPDFINIRT
     KAREVLQRED DLNEIVQLVG KDALAEGDKI TLETAKLLRE DYLAQNAFTP YDKFCPFYKS
     VWMMRNIIHF YNLANQAVER GAGSDGQKIT YSLIKHRVGD LFYRLVSQKF EDPAEGEAAL
     VGQFQKLHED LSTGFRNLED ETR