VATF1_DROME
ID VATF1_DROME Reviewed; 124 AA.
AC Q24583; C4XVH6; Q9V7E2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=V-type proton ATPase subunit F 1;
DE Short=V-ATPase subunit F 1;
DE AltName: Full=V-ATPase 14 kDa subunit;
DE AltName: Full=Vacuolar H+ ATPase subunit 14-1;
DE AltName: Full=Vacuolar proton pump subunit F 1;
GN Name=Vha14-1; Synonyms=Vha14; ORFNames=CG8210;
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=Oregon-R; TISSUE=Head;
RX PubMed=8682310; DOI=10.1016/0378-1119(96)00057-1;
RA Guo Y., Kaiser K., Wieczorek H., Dow J.A.T.;
RT "The Drosophila melanogaster gene vha14 encoding a 14-kDa F-subunit of the
RT vacuolar ATPase.";
RL Gene 172:239-243(1996).
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;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, 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: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons (By similarity). V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments and in some cell
CC types, is targeted to the plasma membrane, where it is responsible for
CC acidifying the extracellular environment (By similarity).
CC {ECO:0000250|UniProtKB:Q16864, ECO:0000250|UniProtKB:Q28029}.
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:Q16864}.
CC -!- SIMILARITY: Belongs to the V-ATPase F subunit family. {ECO:0000305}.
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DR EMBL; Z26918; CAA81541.1; -; mRNA.
DR EMBL; AE013599; AAF58115.1; -; Genomic_DNA.
DR EMBL; BT088780; ACR82505.1; -; mRNA.
DR PIR; JC4849; JC4849.
DR RefSeq; NP_476969.1; NM_057621.5.
DR AlphaFoldDB; Q24583; -.
DR SMR; Q24583; -.
DR BioGRID; 62464; 15.
DR DIP; DIP-22853N; -.
DR STRING; 7227.FBpp0086474; -.
DR iPTMnet; Q24583; -.
DR PaxDb; Q24583; -.
DR PRIDE; Q24583; -.
DR DNASU; 36731; -.
DR EnsemblMetazoa; FBtr0087341; FBpp0086474; FBgn0262512.
DR GeneID; 36731; -.
DR KEGG; dme:Dmel_CG8210; -.
DR CTD; 36731; -.
DR FlyBase; FBgn0262512; Vha14-1.
DR VEuPathDB; VectorBase:FBgn0262512; -.
DR eggNOG; KOG3432; Eukaryota.
DR GeneTree; ENSGT00390000013208; -.
DR HOGENOM; CLU_135754_0_0_1; -.
DR InParanoid; Q24583; -.
DR OMA; YTNAFPA; -.
DR OrthoDB; 1483558at2759; -.
DR PhylomeDB; Q24583; -.
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 BioGRID-ORCS; 36731; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36731; -.
DR PRO; PR:Q24583; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0262512; Expressed in adult Malpighian tubule (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q24583; baseline and differential.
DR Genevisible; Q24583; DM.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IC:FlyBase.
DR Gene3D; 3.40.50.10580; -; 1.
DR InterPro; IPR008218; ATPase_V1-cplx_f_g_su.
DR InterPro; IPR005772; ATPase_V1-cplx_fsu_euk.
DR InterPro; IPR036906; ATPase_V1_fsu_sf.
DR Pfam; PF01990; ATP-synt_F; 1.
DR PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR SUPFAM; SSF159468; SSF159468; 1.
DR TIGRFAMs; TIGR01101; V_ATP_synt_F; 1.
PE 1: Evidence at protein level;
KW Hydrogen ion transport; Ion transport; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..124
FT /note="V-type proton ATPase subunit F 1"
FT /id="PRO_0000144805"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 124 AA; 13850 MW; 1D8DC23808090A96 CRC64;
MALHSAIKGK LISVIGDEDT CVGFLLGGVG EINKNRHPNF MVVDKNTAVS ELEDCFKRFL
KRDDIDIILI NQNCAELIRH VIDAHTSPVP AVLEIPSKDH PYDASKDSIL RRARGMFNPE
DLVR
