ID   VATA_DAUCA              Reviewed;         623 AA.
AC   P09469;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=Vacuolar proton pump subunit alpha;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2897965; DOI=10.1016/s0021-9258(19)76514-4;
RA   Zimniak L., Dittrich R., Gogarten J.P., Kibak H., Taiz L.;
RT   "The cDNA sequence of the 69-kDa subunit of the carrot vacuolar H+-ATPase.
RT   Homology to the beta-chain of F0F1-ATPases.";
RL   J. Biol. Chem. 263:9102-9112(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RX   PubMed=2139875; DOI=10.1016/s0021-9258(19)39020-9;
RA   Struve I., Rausch T., Bernasconi P., Taiz L.;
RT   "Structure and function of the promoter of the carrot V-type H(+)-ATPase
RT   catalytic subunit gene.";
RL   J. Biol. Chem. 265:7927-7932(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; J03769; AAA33139.1; -; mRNA.
DR   EMBL; J05429; AAA33135.1; -; Genomic_DNA.
DR   PIR; A28105; PXPZV9.
DR   AlphaFoldDB; P09469; -.
DR   SMR; P09469; -.
DR   PRIDE; P09469; -.
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_0000144579"
FT   BINDING         252..259
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        40
FT                   /note="A -> S (in Ref. 2; AAA33135)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   623 AA;  68835 MW;  2CE91AE8D0EFF7E5 CRC64;
     MPSVYGDRLT TFEDSEKESE YGYVRKVSGP VVVADGMGGA AMYELVRVGH DNLIGEIIRL
     EGDSATIQVY EETAGLMVND PVLRTHKPLS VELGPGILGN IFDGIQRPLK TIAKRSGDVY
     IPRGVSVPAL DKDTLWEFQP KKIGEGDLLT GGDLYATVFE NSLMQHHVAL PPDAMGKITY
     VAPAGQYSLK DTVLELEFQG VKKQFTMLQT WPVRTPRPVA SKLAADTPLL TGQRVLDALF
     PSVLGGTCAI PGAFGCGKTV ISQALSKYSN SDTVVYVGCG ERGNEMAEVL MDFPQLTMTL
     PDGREESVMK RTTLVANTSN MPVAAREASI YTGITIAEYF RDMGYNVSMM ADSTSRWAEA
     LREISGRLAE MPADSGYPAY LAARLASFYE RAGKVKCLGG PERNGSVTIV GAVSPPGGDF
     SDPVTSATLS IVQVFWGLDK KLAQRKHFPS VNWLISYSKY STALESFYEK FDSDFIDIRT
     KAREVLQRED DLNEIVQLVG KDALAETDKI TLETAKLLRE DYLAQNAFTP YDKFCPFYKS
     VWMMRNIIHF YNLANQAVER GAGMDGQKIS YTLIKHRLGD LFYRLVSQKF EDPAEGEDVL
     VGKFKKLHDD LTSGFRNLED ETR