VATA2_DROME
ID VATA2_DROME Reviewed; 614 AA.
AC Q27331; Q8SXT2; Q9VK48;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=V-type proton ATPase catalytic subunit A isoform 2;
DE Short=V-ATPase subunit A 2;
DE EC=7.1.2.2 {ECO:0000250|UniProtKB:P50516};
DE AltName: Full=V-ATPase 69 kDa subunit 2;
DE AltName: Full=Vacuolar proton pump subunit alpha 2;
GN Name=Vha68-2; Synonyms=VHAA2; ORFNames=CG3762;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S, and Oregon-R;
RX PubMed=9050231; DOI=10.1242/jeb.200.2.237;
RA Dow J.A.T., Davies S.A., Guo Y., Graham S., Finbow M.E., Kaiser K.;
RT "Molecular genetic analysis of V-ATPase function in Drosophila
RT melanogaster.";
RL J. Exp. Biol. 200:237-245(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
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; U59146; AAB02270.1; -; mRNA.
DR EMBL; U59147; AAB02271.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53231.1; -; Genomic_DNA.
DR EMBL; AY084150; AAL89888.1; -; mRNA.
DR RefSeq; NP_001246015.1; NM_001259086.2.
DR RefSeq; NP_001260424.1; NM_001273495.1.
DR RefSeq; NP_001260425.1; NM_001273496.1.
DR RefSeq; NP_652004.2; NM_143747.3.
DR RefSeq; NP_723775.1; NM_165021.2.
DR RefSeq; NP_723776.1; NM_165022.2.
DR AlphaFoldDB; Q27331; -.
DR SMR; Q27331; -.
DR BioGRID; 69430; 49.
DR IntAct; Q27331; 8.
DR STRING; 7227.FBpp0079999; -.
DR iPTMnet; Q27331; -.
DR PaxDb; Q27331; -.
DR PRIDE; Q27331; -.
DR DNASU; 45012; -.
DR EnsemblMetazoa; FBtr0080418; FBpp0079999; FBgn0263598.
DR EnsemblMetazoa; FBtr0080419; FBpp0080000; FBgn0263598.
DR EnsemblMetazoa; FBtr0080420; FBpp0080001; FBgn0263598.
DR EnsemblMetazoa; FBtr0305551; FBpp0294002; FBgn0263598.
DR EnsemblMetazoa; FBtr0336613; FBpp0307596; FBgn0263598.
DR EnsemblMetazoa; FBtr0336614; FBpp0307597; FBgn0263598.
DR GeneID; 45012; -.
DR KEGG; dme:Dmel_CG3762; -.
DR UCSC; CG3762-RA; d. melanogaster.
DR CTD; 45012; -.
DR FlyBase; FBgn0263598; Vha68-2.
DR VEuPathDB; VectorBase:FBgn0263598; -.
DR eggNOG; KOG1352; Eukaryota.
DR GeneTree; ENSGT00550000074787; -.
DR HOGENOM; CLU_008162_3_1_1; -.
DR InParanoid; Q27331; -.
DR OMA; RIVKTFW; -.
DR OrthoDB; 241249at2759; -.
DR PhylomeDB; Q27331; -.
DR Reactome; R-DME-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-DME-77387; Insulin receptor recycling.
DR Reactome; R-DME-917977; Transferrin endocytosis and recycling.
DR Reactome; R-DME-9639288; Amino acids regulate mTORC1.
DR Reactome; R-DME-983712; Ion channel transport.
DR SignaLink; Q27331; -.
DR BioGRID-ORCS; 45012; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 45012; -.
DR PRO; PR:Q27331; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0263598; Expressed in adult hindgut (Drosophila) and 43 other tissues.
DR ExpressionAtlas; Q27331; baseline and differential.
DR Genevisible; Q27331; DM.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IMP:FlyBase.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:FlyBase.
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:0048388; P:endosomal lumen acidification; IMP:FlyBase.
DR GO; GO:0016197; P:endosomal transport; IMP:FlyBase.
DR GO; GO:0007446; P:imaginal disc growth; IMP:FlyBase.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase.
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 1: Evidence at protein level;
KW ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Translocase; Transport.
FT CHAIN 1..614
FT /note="V-type proton ATPase catalytic subunit A isoform 2"
FT /id="PRO_0000144567"
FT BINDING 247..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 210..212
FT /note="QPR -> HHA (in Ref. 1; AAB02270/AAB02271)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="A -> R (in Ref. 1; AAB02270/AAB02271)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 614 AA; 68302 MW; 63DC9CA01CCDE275 CRC64;
MSNLKRFDDE ERESKYGRVF AVSGPVVTAE AMSGSAMYEL VRVGYYELVG EIIRLEGDMA
TIQVYEETSG VTVGDPVLRT GKPLSVELGP GIMGSIFDGI QRPLKDINEL TESIYIPKGV
NVPSLSRVAS WEFNPLNVKV GSHITGGDLY GLVHENTLVK HKMIVNPRAK GTVRYIAPSG
NYKVDDVVLE TEFDGEITKH TMLQVWPVRQ 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 FYDKNFPEFV PLRTKVKEIL
QEEEDLSEIV QLVGKASLAE TDKITLEVAK LLKDDFLQQN SYSSYDRFCP FYKTVGMLRN
IIDFYDMARH SVESTAQSEN KITWNVIREA MGNIMYQLSS MKFKDPVKDG EAKIKADFEQ
LHEDLQQAFR NLED
