VPP1_MOUSE
ID VPP1_MOUSE Reviewed; 839 AA.
AC Q9Z1G4; A2A5A1; Q9JHJ4; Q9JL13; Q9JL14;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a 1;
DE Short=V-ATPase 116 kDa subunit a 1;
DE AltName: Full=Clathrin-coated vesicle/synaptic vesicle proton pump 116 kDa subunit;
DE AltName: Full=Vacuolar adenosine triphosphatase subunit Ac116;
DE AltName: Full=Vacuolar proton pump subunit 1;
DE AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1;
GN Name=Atp6v0a1; Synonyms=Atp6n1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1-II).
RA Howell M.L., Dean G.E.;
RT "cDNA sequences for mouse vacuolar ATPase subunits.";
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Liver;
RX PubMed=10702241; DOI=10.1074/jbc.275.10.6824;
RA Nishi T., Forgac M.;
RT "Molecular cloning and expression of three isoforms of the 100-kDa a
RT subunit of the mouse vacuolar proton-translocating ATPase.";
RL J. Biol. Chem. 275:6824-6830(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A1-III).
RX PubMed=10722719; DOI=10.1074/jbc.275.12.8760;
RA Toyomura T., Oka T., Yamaguchi C., Wada Y., Futai M.;
RT "Three subunit a isoforms of mouse vacuolar H+-ATPase. Preferential
RT expression of the a3 isoform during osteoclast differentiation.";
RL J. Biol. Chem. 275:8760-8765(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP PROTEIN SEQUENCE OF 39-49; 75-103; 121-129; 175-184; 206-239; 272-286;
RP 347-361; 377-394; 537-544; 675-685 AND 816-833, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-371, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH SPAAR.
RX PubMed=28024296; DOI=10.1038/nature21034;
RA Matsumoto A., Pasut A., Matsumoto M., Yamashita R., Fung J., Monteleone E.,
RA Saghatelian A., Nakayama K.I., Clohessy J.G., Pandolfi P.P.;
RT "mTORC1 and muscle regeneration are regulated by the LINC00961-encoded SPAR
RT polypeptide.";
RL Nature 541:228-232(2017).
CC -!- FUNCTION: Subunit of the V0 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). Required for
CC assembly and activity of the vacuolar ATPase (By similarity).
CC {ECO:0000250|UniProtKB:P32563, ECO:0000250|UniProtKB:Q29466,
CC ECO:0000250|UniProtKB:Q93050}.
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 ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC similarity). Interacts with SPAAR (PubMed:28024296).
CC {ECO:0000250|UniProtKB:Q93050, ECO:0000269|PubMed:28024296}.
CC -!- INTERACTION:
CC Q9Z1G4; P49769: Psen1; NbExp=2; IntAct=EBI-771149, EBI-990067;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000250|UniProtKB:P25286}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000250|UniProtKB:P25286}; Multi-pass membrane protein
CC {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:Q93050}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A1-II;
CC IsoId=Q9Z1G4-1; Sequence=Displayed;
CC Name=A1-I;
CC IsoId=Q9Z1G4-2; Sequence=VSP_000342, VSP_000343;
CC Name=A1-III;
CC IsoId=Q9Z1G4-3; Sequence=VSP_000342;
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; U13836; AAC83083.1; -; mRNA.
DR EMBL; AF218249; AAF59918.1; -; mRNA.
DR EMBL; AF218250; AAF59919.1; -; mRNA.
DR EMBL; AF218251; AAF59920.1; -; mRNA.
DR EMBL; AB022321; BAA93005.1; -; mRNA.
DR EMBL; AL591425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466677; EDL03866.1; -; Genomic_DNA.
DR CCDS; CCDS25443.1; -. [Q9Z1G4-2]
DR CCDS; CCDS56808.1; -. [Q9Z1G4-1]
DR CCDS; CCDS56809.1; -. [Q9Z1G4-3]
DR RefSeq; NP_001229979.1; NM_001243050.1. [Q9Z1G4-3]
DR RefSeq; NP_001229980.1; NM_001243051.1. [Q9Z1G4-1]
DR RefSeq; NP_058616.1; NM_016920.3. [Q9Z1G4-2]
DR AlphaFoldDB; Q9Z1G4; -.
DR SMR; Q9Z1G4; -.
DR BioGRID; 198267; 12.
DR IntAct; Q9Z1G4; 5.
DR MINT; Q9Z1G4; -.
DR STRING; 10090.ENSMUSP00000044838; -.
DR TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; Q9Z1G4; -.
DR PhosphoSitePlus; Q9Z1G4; -.
DR SwissPalm; Q9Z1G4; -.
DR EPD; Q9Z1G4; -.
DR jPOST; Q9Z1G4; -.
DR MaxQB; Q9Z1G4; -.
DR PaxDb; Q9Z1G4; -.
DR PeptideAtlas; Q9Z1G4; -.
DR PRIDE; Q9Z1G4; -.
DR ProteomicsDB; 300178; -. [Q9Z1G4-1]
DR ProteomicsDB; 300179; -. [Q9Z1G4-2]
DR ProteomicsDB; 300180; -. [Q9Z1G4-3]
DR Antibodypedia; 16938; 110 antibodies from 21 providers.
DR DNASU; 11975; -.
DR Ensembl; ENSMUST00000044721; ENSMUSP00000044838; ENSMUSG00000019302. [Q9Z1G4-2]
DR Ensembl; ENSMUST00000092663; ENSMUSP00000090333; ENSMUSG00000019302. [Q9Z1G4-3]
DR Ensembl; ENSMUST00000103110; ENSMUSP00000099399; ENSMUSG00000019302. [Q9Z1G4-1]
DR GeneID; 11975; -.
DR KEGG; mmu:11975; -.
DR UCSC; uc007lmt.2; mouse. [Q9Z1G4-3]
DR UCSC; uc007lmu.2; mouse. [Q9Z1G4-2]
DR UCSC; uc007lmx.2; mouse. [Q9Z1G4-1]
DR CTD; 535; -.
DR MGI; MGI:103286; Atp6v0a1.
DR VEuPathDB; HostDB:ENSMUSG00000019302; -.
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_1_1; -.
DR InParanoid; Q9Z1G4; -.
DR OMA; FSYDRAR; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; Q9Z1G4; -.
DR TreeFam; TF300346; -.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-77387; Insulin receptor recycling.
DR Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR Reactome; R-MMU-983712; Ion channel transport.
DR BioGRID-ORCS; 11975; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Atp6v0a1; mouse.
DR PRO; PR:Q9Z1G4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9Z1G4; protein.
DR Bgee; ENSMUSG00000019302; Expressed in superior frontal gyrus and 251 other tissues.
DR ExpressionAtlas; Q9Z1G4; baseline and differential.
DR Genevisible; Q9Z1G4; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043229; C:intracellular organelle; IDA:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0016241; P:regulation of macroautophagy; ISO:MGI.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..839
FT /note="V-type proton ATPase 116 kDa subunit a 1"
FT /id="PRO_0000119212"
FT TOPO_DOM 1..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..416
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..542
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 543..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..646
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 727..751
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..772
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 812..839
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q93050"
FT MOD_RES 371
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT VAR_SEQ 142..148
FT /note="Missing (in isoform A1-I and isoform A1-III)"
FT /evidence="ECO:0000303|PubMed:10722719"
FT /id="VSP_000342"
FT VAR_SEQ 712
FT /note="E -> EPTEDEV (in isoform A1-I)"
FT /evidence="ECO:0000305"
FT /id="VSP_000343"
FT VARIANT 194
FT /note="L -> F"
FT CONFLICT 36
FT /note="Q -> N (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..92
FT /note="VPFPR -> APLPW (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="N -> D (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="F -> S (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="K -> T (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="L -> P (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="S -> F (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="G -> R (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="F -> L (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="G -> W (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="H -> L (in Ref. 1; AAC83083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 839 AA; 96467 MW; E102667721450C06 CRC64;
MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
MDRKLRFVEK EIRKANIPIM DTGENPEVPF PRDMIDLEAN FEKIENELKE INTNQEALKR
NFLELTELKF ILRKTQQFFD EAELHHQQMA DPDLLEESSS LLEPNEMGRG APLRLGFVAG
VINRERIPTF ERMLWRVCRG NVFLRQAEIE NPLEDPVTGD YVHKSVFIIF FQGDQLKNRV
KKICEGFRAS LYPCPETPQE RKEMASGVNT RIDDLQMVLN QTEDHRQRVL QAAAKNIRVW
FIKVRKMKAI YHTLNLCNID VTQKCLIAEV WCPVTDLDSI QFALRRGTEH SGSTVPSILN
RMQTNQTPPT YNKTNKFTHG FQNIVDAYGI GTYREINPAP YTVITFPFLF AVMFGDFGHG
ILMTLFAVWM VLRESRILSQ KHENEMFSMV FSGRYIILLM GLFSIYTGLI YNDCFSKSLN
IFGSSWSVRP MFTQGNWTEE TLLGSSVLQL NPAIPGVFGG PYPFGIDPIW NIATNKLTFL
NSFKMKMSVI LGIIHMLFGV SLSLFNHIYF KKPLNIYFGF IPEIIFMSSL FGYLVILIFY
KWTAYDAHSS RNAPSLLIHF INMFLFSYPE SGNAMLYSGQ KGIQCFLIVV AMLCVPWMLL
FKPLILRHQY LRKKHLGTLN FGGIRVGNGP TEEDAEIIQH DQLSTHSEDA EEFDFGDTMV
HQAIHTIEYC LGCISNTASY LRLWALSLAH AQLSEVLWTM VIHIGLHVRS LAGGLGLFFI
FAAFATLTVA ILLIMEGLSA FLHALRLHWV EFQNKFYTGT GFKFLPFSFE HIREGKFDE
