ID   VATA_BRANA              Reviewed;         623 AA.
AC   Q39291;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=BN59;
DE   AltName: Full=Tonoplast ATPase 70 kDa subunit;
DE   AltName: Full=V-ATPase 69 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit alpha;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Jet neuf; TISSUE=Leaf;
RX   PubMed=7640365; DOI=10.1007/bf00042078;
RA   Orr W., White T.C., Iu B., Robert L., Singh J.;
RT   "Characterization of a low-temperature-induced cDNA from winter Brassica
RT   napus encoding the 70 kDa subunit of tonoplast ATPase.";
RL   Plant Mol. Biol. 28:943-948(1995).
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; U15604; AAA82881.1; -; mRNA.
DR   PIR; S57790; S57790.
DR   AlphaFoldDB; Q39291; -.
DR   SMR; Q39291; -.
DR   PRIDE; Q39291; -.
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   2: Evidence at transcript level;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Translocase; Transport.
FT   CHAIN           1..623
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000144576"
FT   BINDING         252..259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   623 AA;  68731 MW;  7C172246EB91418D CRC64;
     MPAFYGGKLT TFEDDEKESE YGYVRKVSGP VVVADGMAGA AMYELVRVGH DNLIGEIIRL
     EGDSATIQVY EETAGLTVND PVLRTHKPLS VELGPGILGN IFDGIQRPLK TIAKRSGDVY
     IPRGVSVPAL DKDCLWEFQP KDFVEGDTIT GGDLYATVFE NSLMQHHVAL PPDAMGKITY
     LAPAGQYSLK DTVLELEFQG VKKSFTMLQT WPVRTPRPVA SKLAADTPLL TGQRVLDALF
     PSVLGGTCAI PGAFGCGKTV ISQALSKYSN SDAVVYVGCG ERGNEMAEVL MDFPQLTMTL
     PDGREESVMK RTTLVANTSN MPVAAREASI YTGITIAEYF RDMGYNVSMM ADSTSRWAEA
     LREISGRLAE MPADSGYPAY LAARLASFYE RAGKVKCLGG PERNGSVTIV GAVSPPGGDF
     SDPVTSATLS IVQVFWGLDK KLAQRKHFPS VNWLISYSKY STALESFYEK FDSDFIDIRT
     KAREVLQRED DLNEIVQLVG KDALAEGDKI TLETAKLLRE DYLAQNAFTP YDKFCPFYKS
     VWMMRNIIHF YNLANQAVER GAGMDGQKIS YSLIKHRLGD LFYRLVSQKF EDPAEGEDVL
     VGKFKKLHDD LTSGFRNLED ETR