ID   VATA_ANOGA              Reviewed;         614 AA.
AC   Q5TTG1;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, 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 {ECO:0000250|UniProtKB:P50516};
DE   AltName: Full=V-ATPase 69 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit alpha;
GN   Name=Vha68-2 {ECO:0000250|UniProtKB:Q27331}; ORFNames=AGAP003153;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:EAA44781.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST {ECO:0000312|EMBL:EAA44781.1};
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
CC   -!- FUNCTION: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase
CC       (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1)
CC       that hydrolyzes ATP and a membrane integral complex (V0) that
CC       translocates protons (By similarity). V-ATPase is responsible for
CC       acidifying and maintaining the pH of intracellular compartments and in
CC       some cell types, is targeted to the plasma membrane, where it is
CC       responsible for acidifying the extracellular environment (By
CC       similarity). {ECO:0000250|UniProtKB:P38606,
CC       ECO:0000250|UniProtKB:P50516}.
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:0000250|UniProtKB:P50516};
CC   -!- ACTIVITY REGULATION: ATP hydrolysis occurs at the interface between the
CC       nucleotide-binding domains of subunits A and B (By similarity). ATP
CC       hydrolysis triggers a conformational change in the subunits D and F,
CC       which induces a shift of subunit d (By similarity). The c-ring is
CC       subsequently rotated and results in a continuous proton translocation
CC       across the membrane (By similarity). {ECO:0000250|UniProtKB:P31404}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits VhaAC45 and ATP6AP2 (By similarity).
CC       {ECO:0000250|UniProtKB:P38606}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255}.
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DR   EMBL; AAAB01008879; EAA44781.1; -; Genomic_DNA.
DR   RefSeq; XP_003436409.1; XM_003436361.1.
DR   RefSeq; XP_003436410.1; XM_003436362.1.
DR   RefSeq; XP_003436411.1; XM_003436363.1.
DR   RefSeq; XP_312843.1; XM_312843.5.
DR   AlphaFoldDB; Q5TTG1; -.
DR   SMR; Q5TTG1; -.
DR   STRING; 7165.AGAP003153-PB; -.
DR   PaxDb; Q5TTG1; -.
DR   GeneID; 1273824; -.
DR   KEGG; aga:AgaP_AGAP003153; -.
DR   CTD; 1273824; -.
DR   VEuPathDB; VectorBase:AGAP003153; -.
DR   eggNOG; KOG1352; Eukaryota.
DR   HOGENOM; CLU_008162_3_1_1; -.
DR   InParanoid; Q5TTG1; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 241249at2759; -.
DR   PhylomeDB; Q5TTG1; -.
DR   Proteomes; UP000007062; Chromosome 2R.
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; 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   3: Inferred from homology;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..614
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000232901"
FT   BINDING         247..254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   614 AA;  68209 MW;  F0C40A4FED49DA1E CRC64;
     MSNLKKISDE DRESKFGYVF AVSGPVVTAE RMSGSAMYEL VRVGYYELVG EIIRLEGDMA
     TIQVYEETSG VTVGDPVLRT GKPLSVELGP GIMGSIFDGI QRPLKDINEM TSSIYIPKGI
     NVPCLSRTQS WSFNPLNVKA GSHITGGDLY GIVHENTLVK HKLMVPPRAK GTVKYIAPSG
     NYTVDDVILE TEFDGEISKF TMLQVWPVRQ PRPVTEKLPA NHPLLTGQRV LDSLFPCVQG
     GTTAIPGAFG CGKTVISQSL SKYSNSDVIV YVGCGERGNE MSEVLRDFPE LSVEIDGVTE
     SIMKRTALVA NTSNMPVAAR EASIYTGITL SEYFRDMGYN VSMMADSTSR WAEALREISG
     RLAEMPADSG YPAYLGARLA SFYERAGRVK CLGNPEREGS VSIVGAVSPP GGDFSDPVTS
     ATLGIVQVFW GLDKKLAQRK HFPSINWLIS YSKYMRALED FYDKNFPEFV PMRTKVKEIL
     QEEEDLSEIV QLVGKASLAE TDKITLEVAK LLKDDFLQQN SYSAYDRFCP FYKTVGMLKN
     MIGFYDMARH AVETTAQSEN KITWNVIRDS MGQILYQLSS MKFKDPVKDG EPKIKADFDQ
     LYEDMQQAFR NLED