VATH_DROME
ID VATH_DROME Reviewed; 468 AA.
AC Q9V3J1; Q8IP12; Q960C9; Q9VJJ2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=V-type proton ATPase subunit H;
DE Short=V-ATPase subunit H;
DE AltName: Full=Vacuolar proton pump subunit H;
DE AltName: Full=Vacuolar proton pump subunit SFD;
GN Name=VhaSFD; ORFNames=CG17332;
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] (ISOFORM D).
RA Westhoff M.A., Dow J.A.T.;
RT "Characterization of vhaSFD, the gene encoding a SFD subunit of the
RT Drosophila V-ATPase.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM A).
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).
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). Subunit H is
CC essential for V-ATPase activity, but not for the assembly of the
CC complex (By similarity). {ECO:0000250|UniProtKB:O46563,
CC ECO:0000250|UniProtKB:P41807, ECO:0000250|UniProtKB:Q9UI12}.
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:Q9UI12}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q9V3J1-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9V3J1-2; Sequence=VSP_010332;
CC Name=D;
CC IsoId=Q9V3J1-3; Sequence=VSP_010333, VSP_010334;
CC -!- SIMILARITY: Belongs to the V-ATPase H subunit family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD47254.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF159457; AAD47254.1; ALT_SEQ; mRNA.
DR EMBL; AE014134; AAF53555.2; -; Genomic_DNA.
DR EMBL; AE014134; AAF53556.3; -; Genomic_DNA.
DR EMBL; AE014134; AAN10957.1; -; Genomic_DNA.
DR EMBL; AY052122; AAK93546.1; -; mRNA.
DR RefSeq; NP_001260510.1; NM_001273581.1. [Q9V3J1-1]
DR RefSeq; NP_523585.2; NM_078861.3. [Q9V3J1-1]
DR RefSeq; NP_723992.1; NM_165177.2. [Q9V3J1-2]
DR RefSeq; NP_723993.1; NM_165178.2. [Q9V3J1-3]
DR AlphaFoldDB; Q9V3J1; -.
DR SMR; Q9V3J1; -.
DR BioGRID; 61004; 13.
DR IntAct; Q9V3J1; 19.
DR PaxDb; Q9V3J1; -.
DR PRIDE; Q9V3J1; -.
DR EnsemblMetazoa; FBtr0080940; FBpp0080494; FBgn0027779. [Q9V3J1-1]
DR EnsemblMetazoa; FBtr0080941; FBpp0080495; FBgn0027779. [Q9V3J1-2]
DR EnsemblMetazoa; FBtr0080942; FBpp0080496; FBgn0027779. [Q9V3J1-3]
DR EnsemblMetazoa; FBtr0335143; FBpp0307142; FBgn0027779. [Q9V3J1-1]
DR GeneID; 34997; -.
DR KEGG; dme:Dmel_CG17332; -.
DR CTD; 34997; -.
DR FlyBase; FBgn0027779; VhaSFD.
DR VEuPathDB; VectorBase:FBgn0027779; -.
DR eggNOG; KOG2759; Eukaryota.
DR GeneTree; ENSGT00390000003289; -.
DR HOGENOM; CLU_025709_2_0_1; -.
DR InParanoid; Q9V3J1; -.
DR OMA; KDQNVRY; -.
DR PhylomeDB; Q9V3J1; -.
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; Q9V3J1; -.
DR BioGRID-ORCS; 34997; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34997; -.
DR PRO; PR:Q9V3J1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0027779; Expressed in adult hindgut (Drosophila) and 33 other tissues.
DR ExpressionAtlas; Q9V3J1; baseline and differential.
DR Genevisible; Q9V3J1; DM.
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:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0033227; P:dsRNA transport; IMP:FlyBase.
DR GO; GO:1902600; P:proton transmembrane transport; IC:FlyBase.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 1.25.40.150; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004908; ATPase_V1-cplx_hsu.
DR InterPro; IPR011987; ATPase_V1-cplx_hsu_C.
DR InterPro; IPR038497; ATPase_V1-cplx_hsu_C_sf.
DR PANTHER; PTHR10698; PTHR10698; 1.
DR Pfam; PF11698; V-ATPase_H_C; 1.
DR Pfam; PF03224; V-ATPase_H_N; 1.
DR PIRSF; PIRSF032184; ATPase_V1_H; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrogen ion transport; Ion transport;
KW Reference proteome; Transport.
FT CHAIN 1..468
FT /note="V-type proton ATPase subunit H"
FT /id="PRO_0000124196"
FT VAR_SEQ 172
FT /note="N -> NGLAYLQEMAQLAKRTQTILVHTHGKDKDHHGHQYSPTLAQLQQQHE
FT LAERANESYREVGVGSDHQQQDGKCVIP (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_010332"
FT VAR_SEQ 441
FT /note="H -> Q (in isoform D)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010333"
FT VAR_SEQ 442..468
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010334"
FT CONFLICT 404..440
FT /note="Missing (in Ref. 1; AAD47254)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 53734 MW; 9F0B2D86795B795A CRC64;
MTTALYLPEE NIDMIAATSV LQQQAADIRT RTINWASYMQ SQMISEEDYK AISALDKSRA
SFLAQNSSQV VKTLLNLVSH LSKDSTIQYI LVLLDDLLQE DRSRVDLFHD TAGKLKQCIW
GPFLNLLNRQ DGFIVNMSSR ILAKFACWGH ETMPKSDLNF YLQFLKDQLA SNNNEYIQSV
ARCLQMMLRV DEYRFAFVGV DGISTLIRIL STRVNFQVQY QLIFCLWVLT FNPLLAAKMN
KFSVIPILAD ILSDCAKEKV TRIILAVFRN LIEKPEDSSV AKDHCIAMVQ CKVLKQLSIL
EQRRFDDEDI TADVEYLSEK LQNSVQDLSS FDEYATEVRS GRLEWSPVHK SAKFWRENAQ
RLNEKNYELL RILVHLLETS KDAIILSVAC FDIGEYVRHY PRGKHVLEQL GGKQIVMQHL
GHEDPNVRYE ALLAVQKLMV HNWEYLGKQL EKENENQKQG AAPIAGKA
