ID   VATA_MAIZE              Reviewed;         561 AA.
AC   P49087; Q41775;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 124.
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;
DE   Flags: Fragment;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Perotti E., Gavin O., Chanson A., Fraichard A.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 47-258.
RC   STRAIN=cv. Lixis; TISSUE=Coleoptile;
RX   PubMed=8617373; DOI=10.1016/0014-5793(96)00336-5;
RA   Viereck R., Kirsch M., Loew R., Rausch T.;
RT   "Down-regulation of plant V-type H+ -ATPase genes after light-induced
RT   inhibition of growth.";
RL   FEBS Lett. 384:285-288(1996).
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10106};
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   -!- TISSUE SPECIFICITY: High expression in the mesocotyl tip of etiolated
CC       seedlings compared to the base.
CC   -!- DEVELOPMENTAL STAGE: Expression is strongly linked to extension growth.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; U36436; AAA80346.1; -; mRNA.
DR   EMBL; X92373; CAA63117.1; -; mRNA.
DR   PIR; S65525; S65525.
DR   AlphaFoldDB; P49087; -.
DR   SMR; P49087; -.
DR   STRING; 4577.GRMZM2G421857_P04; -.
DR   PaxDb; P49087; -.
DR   PRIDE; P49087; -.
DR   ProMEX; P49087; -.
DR   MaizeGDB; 120463; -.
DR   eggNOG; KOG1352; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P49087; baseline and differential.
DR   GO; GO:0000325; C:plant-type vacuole; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR031686; ATP-synth_a_Xtn.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
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; PF16886; ATP-synt_ab_Xtn; 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   Reference proteome; Translocase; Transport.
FT   CHAIN           <1..561
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000144582"
FT   BINDING         190..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        187
FT                   /note="A -> C (in Ref. 2; CAA63117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237..239
FT                   /note="TLP -> QFA (in Ref. 2; CAA63117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="E -> R (in Ref. 2; CAA63117)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   561 AA;  61952 MW;  F398AF2A614D9E0C CRC64;
     ARATIQVYEE TAGLMVNDPV LRTRKPLSVE LGPGILGNIF DGIQRPLKTI AIKSGDVYIP
     RGVSVPALDK DVLWEFQPTK LGVGDVITGG DLYATVFENT LMQHHVALPP GSMGKISYIA
     PAGQYNLQDT VLELEFQGIK KKFTMLQTWP VRSPRPVASK LAADTPLLTG QRVLDALFPS
     VLGGTCAIPG AFGCGKTVIS QALSKYSNSE AVVYVGCGER GNEMAEVLMD FPQLTMTLPD
     GREESVMKRT TLVANTSNMP VAAREASIYT GITIAEYFRD MGYNVSMMAD STSRWAEALR
     EISGRLAEMP ADSGYPAYLA ARLASFYERA GKVKCLGSPD RNGSVTIVGA VSPPGGDFSD
     PVTSATLSIV QVFWGLDKKL AQRKHFPSVN WLISYSKYSK ALESFYEKFD PDFIDIRTKA
     REVLQREDDL NEIVQLVGKD ALAESDKITL ETAKLLREDY LAQNAFTPYD KFCPFYKSVW
     MMRNIIHFNT LANQAVERAA GTDGHKITYS VIKHRLGDLF YRLVSQKFED PAEGEEALVG
     KFKKLYDDLT TGFRNLEDEA R