ID   VATA_HORVU              Reviewed;         580 AA.
AC   Q40002;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 108.
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   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. CM 72; TISSUE=Root;
RA   Dupont F.M., Chan R.;
RL   Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
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; U36939; AAB60306.1; -; mRNA.
DR   PIR; T04409; T04409.
DR   AlphaFoldDB; Q40002; -.
DR   SMR; Q40002; -.
DR   PRIDE; Q40002; -.
DR   ExpressionAtlas; Q40002; baseline and differential.
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; 3.40.50.300; -; 1.
DR   HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR   InterPro; IPR031686; ATP-synth_a_Xtn.
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..580
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000144581"
FT   BINDING         209..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   580 AA;  64098 MW;  0F328B7020955624 CRC64;
     ELVRVGHDSL IGEIIRLEGD SATIQVYEET AGLTVNDPVL RTKKPLSCEL GPGILGNIFD
     GIQRPLKTIA IKSRDVYIPR GVSVPALDKD QLWEFQPNKL GVGDNITNGD LYATVFENTL
     MKHHIALPPG AMGKISYIAP AGQYSLQDTV LELEFQGIKK EFTMLHTWPV RTPRPVASKL
     AADTPLLTGQ RVLDALFPSV LGGTCAIPGA FGCGKTVISQ ALSKYSNSDT VVYVGCGERG
     NEMAEVLMDF PQLTMTLPDG REESVMKRTT LVANTSNMPV AAREASIYTG ITIAEYFRDM
     GYNVSMMADS TSRWAEALRE ISGRLAEMPA DSGYPAYLAS RLASFYERAG KVQCLGSPDR
     TGSVTIVGAV SPPGGDFSDP VTSATLSIVQ VFWGLDKKLA QRKHFPSVNW LISYSKYSTA
     LEGYYEKFDP GFIDMRTKAR EVLQREDDLN EIVQLVGKDA LGESDKITLE TAKLLREDYL
     AQNAFTPYDK YCPFYKSVWM MRNIIHFNQL ANQAVERAAN ADGHKITYAV VKSRMGDLFY
     RLVSQKFEDP AEGEDVLVAK FQKLYDDLTA GFRNLEDEAR