VATA_AEDAL
ID VATA_AEDAL Reviewed; 614 AA.
AC Q2TJ56;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=VhaA;
OS Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7160;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16579815; DOI=10.1111/j.1550-7408.2005.00086.x;
RA Huang C.G., Tsai K.H., Wu W.J., Chen W.J.;
RT "Intestinal expression of H+ V-ATPase in the mosquito Aedes albopictus is
RT tightly associated with gregarine infection.";
RL J. Eukaryot. Microbiol. 53:127-135(2006).
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:0000305}.
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DR EMBL; AY864912; AAX58113.1; -; mRNA.
DR RefSeq; XP_019537311.1; XM_019681766.1.
DR RefSeq; XP_019549163.1; XM_019693618.1.
DR AlphaFoldDB; Q2TJ56; -.
DR SMR; Q2TJ56; -.
DR PRIDE; Q2TJ56; -.
DR EnsemblMetazoa; AALF006486-RA; AALF006486-PA; AALF006486.
DR GeneID; 109419385; -.
DR KEGG; aalb:109419385; -.
DR VEuPathDB; VectorBase:AALC636_017108; -.
DR VEuPathDB; VectorBase:AALC636_031209; -.
DR VEuPathDB; VectorBase:AALF006486; -.
DR VEuPathDB; VectorBase:AALFPA_045970; -.
DR Proteomes; UP000069940; Unplaced.
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..614
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000284399"
FT BINDING 247..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 614 AA; 68229 MW; F10BCA8E46CF083C CRC64;
MSTLKKISDE DRESKFGYVF AVSGPVVTAE RMSGSAMYEL VRVGYYELVG EIIRLEGDMA
TIQVYEETSG VTVGDPVLRT GKPLSVELGP GIMGSIFDGI QRPLKDINEL TSSIYIPKGV
NIPCLSRTQS WGFNPLNVKV GSHITGGDLY GLVHENTLVK HKLLVPPRAK GTVRYIAPPG
NYTVDDIILE TEFDGEINKW SMLQVWPVRQ PRPVTEKLPA NHPLLTGQRV LDSLFPCVQG
GTTAIPGAFG CGKTVISQAL SKYSNSDVII YVGCGERGNE MSEVLRDFPE LSVEIDGVTE
SIMKRTALVA NTSNMPVAAR EASIYTGITL SEYFRDMGYN VSMMADSTSR WAEALREISG
RLAEMPADSG YPAYLGARLA SFYERAGRVK CLGNPEREGS VSIVGAVSPP GGDFSDPVTS
ATLGIVQVFW GLDKKLAQRK HFPSINWLIS YSKYMRALDD FYDKNFQEFV PLRTKVKEIL
QEEEDLSEIV QLVGKASLAE TDKITLEVAK LLKDDFLQQN SYSAYDRFCP FYKTVGMLRN
MIGFYDMARH AVETTAQSEN KITWNVIRDS MGNILYQLSS MKFKDPVKDG EAKIKADFDQ
LYEDLQQAFR NLED
