VAS1_DROME
ID VAS1_DROME Reviewed; 379 AA.
AC Q7JR49;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=V-type proton ATPase subunit S1 {ECO:0000305};
DE AltName: Full=Vacuolar H(+) ATPase AC45 accessory subunit {ECO:0000312|FlyBase:FBgn0262515};
DE Flags: Precursor;
GN Name=VhaAC45 {ECO:0000312|FlyBase:FBgn0262515};
GN Synonyms=ATP6AP1 {ECO:0000303|PubMed:29995586,
GN ECO:0000312|FlyBase:FBgn0262515};
GN ORFNames=CG8029 {ECO:0000312|FlyBase:FBgn0262515};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAO25036.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO25036.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAO25036.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=29127204; DOI=10.1084/jem.20170453;
RA Rujano M.A., Cannata Serio M., Panasyuk G., Peanne R., Reunert J.,
RA Rymen D., Hauser V., Park J.H., Freisinger P., Souche E., Guida M.C.,
RA Maier E.M., Wada Y., Jaeger S., Krogan N.J., Kretz O., Nobre S., Garcia P.,
RA Quelhas D., Bird T.D., Raskind W.H., Schwake M., Duvet S., Foulquier F.,
RA Matthijs G., Marquardt T., Simons M.;
RT "Mutations in the X-linked ATP6AP2 cause a glycosylation disorder with
RT autophagic defects.";
RL J. Exp. Med. 214:3707-3729(2017).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH ATP6AP2.
RX PubMed=29995586; DOI=10.1091/mbc.e18-04-0234;
RA Guida M.C., Hermle T., Graham L.A., Hauser V., Ryan M., Stevens T.H.,
RA Simons M.;
RT "ATP6AP2 functions as a V-ATPase assembly factor in the endoplasmic
RT reticulum.";
RL Mol. Biol. Cell 29:2156-2164(2018).
CC -!- FUNCTION: Accessory subunit of the proton-transporting vacuolar (V)-
CC ATPase protein pump, which is required for luminal acidification of
CC secretory vesicles. {ECO:0000269|PubMed:29127204,
CC ECO:0000269|PubMed:29995586}.
CC -!- SUBUNIT: Accessory component of the multisubunit proton-transporting
CC vacuolar (V)-ATPase protein pump (By similarity). May interact with
CC ATP6AP2 (PubMed:29995586). {ECO:0000250|UniProtKB:Q15904,
CC ECO:0000269|PubMed:29995586}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15904}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the vacuolar ATPase subunit S1 family.
CC {ECO:0000305}.
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DR EMBL; AE013599; AAF58965.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58966.2; -; Genomic_DNA.
DR EMBL; BT003279; AAO25036.1; -; mRNA.
DR RefSeq; NP_610470.1; NM_136626.5.
DR RefSeq; NP_724770.1; NM_165665.2.
DR AlphaFoldDB; Q7JR49; -.
DR IntAct; Q7JR49; 1.
DR STRING; 7227.FBpp0087668; -.
DR TCDB; 8.A.107.1.3; the v-type atpase assembly factor, atp6ap1 (atp6ap1) family.
DR GlyGen; Q7JR49; 2 sites.
DR SwissPalm; Q7JR49; -.
DR PaxDb; Q7JR49; -.
DR PRIDE; Q7JR49; -.
DR DNASU; 35944; -.
DR EnsemblMetazoa; FBtr0088587; FBpp0087668; FBgn0262515.
DR EnsemblMetazoa; FBtr0088588; FBpp0087669; FBgn0262515.
DR GeneID; 35944; -.
DR KEGG; dme:Dmel_CG8029; -.
DR UCSC; CG8029-RA; d. melanogaster.
DR CTD; 35944; -.
DR FlyBase; FBgn0262515; VhaAC45.
DR VEuPathDB; VectorBase:FBgn0262515; -.
DR eggNOG; KOG3868; Eukaryota.
DR GeneTree; ENSGT00940000170675; -.
DR HOGENOM; CLU_039408_1_0_1; -.
DR InParanoid; Q7JR49; -.
DR OMA; QSCYAQL; -.
DR OrthoDB; 1111170at2759; -.
DR PhylomeDB; Q7JR49; -.
DR Reactome; R-DME-77387; Insulin receptor recycling.
DR Reactome; R-DME-917977; Transferrin endocytosis and recycling.
DR Reactome; R-DME-983712; Ion channel transport.
DR BioGRID-ORCS; 35944; 0 hits in 3 CRISPR screens.
DR ChiTaRS; VhaAC45; fly.
DR GenomeRNAi; 35944; -.
DR PRO; PR:Q7JR49; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0262515; Expressed in second segment of antenna (Drosophila) and 30 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IMP:UniProtKB.
DR GO; GO:0030641; P:regulation of cellular pH; IBA:GO_Central.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IGI:UniProtKB.
DR InterPro; IPR008388; Ac45_acc_su.
DR PANTHER; PTHR12471; PTHR12471; 1.
DR Pfam; PF05827; ATP-synt_S1; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..379
FT /note="V-type proton ATPase subunit S1"
FT /evidence="ECO:0000255"
FT /id="PRO_5015098718"
FT PROPEP 18..?
FT /evidence="ECO:0000250|UniProtKB:Q9R1Q9"
FT /id="PRO_0000454044"
FT TOPO_DOM 18..333
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 282..326
FT /evidence="ECO:0000250|UniProtKB:Q15904"
SQ SEQUENCE 379 AA; 41124 MW; CCEC805AC0452C8A CRC64;
MLWKSLIALC VIGAAVAEQT PVFLWGANSV AKPSLKTVSQ VEFAEQLAAL LEDHMVVAFE
ENGLSSKDFL CSNSQAQSCY AQLQGVSPKT YYTSVENPSE ALRSVAAKRE HNSIDASGKL
TTPAKCAVGT ALFVTFEDAA ESREASLESH DAAIAAISKQ FECKVAYLYL AAPSTAPVVQ
RRTRRDTAAT TGGIMWKSTN QFQIFYTALL YNGNPITVTD LKLTNSSSTK LSVVMDTSVA
DKPITFDVVY NGGYFSLSNL VYDNNNFRSS GVNAPTTFSY SCGNLTLESA AVNNMYNTLS
FKSLQLQAPF DGTYKEDFPF GDSWDCVGFV TPGILMGLFV VALLLVIMFV GVCWMMDINT
MDRFDDPKGK TITINAAAE
