ID   VATA_DICDI              Reviewed;         618 AA.
AC   P54647; O00779;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 148.
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;
GN   Name=vatA; ORFNames=DDB_G0287127;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=AX4;
RA   Burdine V., Liu T., Clarke M.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 69-197.
RC   STRAIN=AX3;
RA   Rauchenberger R., Maniak M.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
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; U49169; AAB50981.1; -; mRNA.
DR   EMBL; AAFI02000098; EAL63838.1; -; Genomic_DNA.
DR   EMBL; L43963; AAA70420.1; -; mRNA.
DR   RefSeq; XP_637351.1; XM_632259.1.
DR   AlphaFoldDB; P54647; -.
DR   SMR; P54647; -.
DR   STRING; 44689.DDB0201563; -.
DR   PaxDb; P54647; -.
DR   ABCD; P54647; 1 sequenced antibody.
DR   EnsemblProtists; EAL63838; EAL63838; DDB_G0287127.
DR   GeneID; 8625973; -.
DR   KEGG; ddi:DDB_G0287127; -.
DR   dictyBase; DDB_G0287127; vatA.
DR   eggNOG; KOG1352; Eukaryota.
DR   HOGENOM; CLU_008162_3_1_1; -.
DR   InParanoid; P54647; -.
DR   OMA; RIVKTFW; -.
DR   PhylomeDB; P54647; -.
DR   Reactome; R-DDI-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-DDI-77387; Insulin receptor recycling.
DR   Reactome; R-DDI-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-DDI-9639288; Amino acids regulate mTORC1.
DR   PRO; PR:P54647; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:dictyBase.
DR   GO; GO:0140220; C:pathogen-containing vacuole; HDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
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:0044877; F:protein-containing complex binding; IDA:dictyBase.
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   GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
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; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..618
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000144565"
FT   BINDING         251..258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        69
FT                   /note="E -> Q (in Ref. 3; AAA70420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="K -> F (in Ref. 3; AAA70420)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   618 AA;  68201 MW;  775A7C04C02F02B9 CRC64;
     MSKNSGLPSF ASTEADNSQG FVLSVSGPVV IANQLAGAAM YELVRVGHNQ LVGEIIRLEE
     DTATIQVYEE TSGLTVGDPV LRTHKPLTVE LGPGIMNNIF DGIQRPLNAI AEITKGIYIP
     RGINTPSLNR TIKWPYQPDT KLKVGDNVSG GDIFGQVVEN NLIIHKIMVP PKEMGTIVEI
     APAGEYTLDH ALLTIEFDGK RKQLTMVHNW PVRSARPVIE KLPCNYPLLT GQRVLDSLFP
     CVQGGTCAIP GAFGCGKTVI SQSLSKFSNS DAIVYVGCGE RGNEMAEVLM EFPELHTKVG
     DKEEPIMQRT CLVANTSNMP VAAREASIYT GITLAEYFRD MGLNVAMMAD STSRWAEALR
     EISGRLAEMP ADSGYPAYLG ARLASFYERA GRVSCIGHPT RIGSVTIVGA VSPPGGDFAD
     PVTAATLGIV QVFWGLDKKL AQRKHFPSIN WLISFSKYMQ ALDTHYDQMD PEFVPLRTRA
     KEILQMEEDL SEIVQLVGQD SLGESEKITI EVARIIRDDF LQQNGFSPYD KCCPFFKTVW
     MLKNMMTFYN LAQKAVESST ADNKVTWNQI KNELKEIIHR ITSMKFQDPT DGEQTLTAHF
     STLNEDIITA FRNFSDLV