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Database: UniProt
Entry: VPP1_MOUSE
LinkDB: VPP1_MOUSE
Original site: 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   07-JUN-2017, entry version 151.
DE   RecName: Full=V-type proton ATPase 116 kDa subunit a isoform 1;
DE            Short=V-ATPase 116 kDa isoform a1;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RP   MASS 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
RP   BY 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
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Spleen, and
RC   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
RT   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.,
RA   Monteleone E., Saghatelian A., Nakayama K.I., Clohessy J.G.,
RA   Pandolfi P.P.;
RT   "mTORC1 and muscle regeneration are regulated by the LINC00961-encoded
RT   SPAR polypeptide.";
RL   Nature 541:228-232(2017).
CC   -!- FUNCTION: Required for assembly and activity of the vacuolar
CC       ATPase. Potential role in differential targeting and regulation of
CC       the enzyme for a specific organelle (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: The V-ATPase is a heteromultimeric enzyme composed of at
CC       least thirteen different subunits. It has a membrane peripheral V1
CC       sector for ATP hydrolysis and an integral V0 for proton
CC       translocation. The V1 sector comprises subunits A-H, whereas V0
CC       includes subunits a, d, c, c', and c''. Interacts with SPAAR
CC       (PubMed:28024296). {ECO:0000269|PubMed:28024296}.
CC   -!- INTERACTION:
CC       P49769:Psen1; NbExp=2; IntAct=EBI-771149, EBI-990067;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass
CC       membrane protein. Melanosome {ECO:0000250}. Note=Coated vesicle.
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}.
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; CAM19437.1; -; 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   UniGene; Mm.340818; -.
DR   UniGene; Mm.475829; -.
DR   ProteinModelPortal; Q9Z1G4; -.
DR   BioGrid; 198267; 5.
DR   IntAct; Q9Z1G4; 6.
DR   MINT; MINT-1866025; -.
DR   STRING; 10090.ENSMUSP00000099399; -.
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   PaxDb; Q9Z1G4; -.
DR   PeptideAtlas; Q9Z1G4; -.
DR   PRIDE; Q9Z1G4; -.
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   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   GeneTree; ENSGT00390000004941; -.
DR   HOGENOM; HOG000037059; -.
DR   HOVERGEN; HBG014606; -.
DR   InParanoid; Q9Z1G4; -.
DR   KO; K02154; -.
DR   OMA; WTAYDAH; -.
DR   OrthoDB; EOG091G01BI; -.
DR   TreeFam; TF300346; -.
DR   Reactome; R-MMU-1222556; ROS, 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   ChiTaRS; Atp6v0a1; mouse.
DR   PRO; PR:Q9Z1G4; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000019302; -.
DR   CleanEx; MM_ATP6V0A1; -.
DR   ExpressionAtlas; Q9Z1G4; baseline and differential.
DR   Genevisible; Q9Z1G4; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; 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; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
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   GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; 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; Complete proteome; Cytoplasmic vesicle;
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW   Membrane; Phosphoprotein; Polymorphism; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    839       V-type proton ATPase 116 kDa subunit a
FT                                isoform 1.
FT                                /FTId=PRO_0000119212.
FT   TOPO_DOM      1    395       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    396    414       Helical. {ECO:0000255}.
FT   TOPO_DOM    415    416       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    417    433       Helical. {ECO:0000255}.
FT   TOPO_DOM    434    448       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    449    478       Helical. {ECO:0000255}.
FT   TOPO_DOM    479    542       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    543    562       Helical. {ECO:0000255}.
FT   TOPO_DOM    563    580       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    581    601       Helical. {ECO:0000255}.
FT   TOPO_DOM    602    646       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    647    666       Helical. {ECO:0000255}.
FT   TOPO_DOM    667    726       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    727    751       Helical. {ECO:0000255}.
FT   TOPO_DOM    752    772       Vacuolar. {ECO:0000255}.
FT   TRANSMEM    773    811       Helical. {ECO:0000255}.
FT   TOPO_DOM    812    839       Cytoplasmic. {ECO:0000255}.
FT   MOD_RES     257    257       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     367    367       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q93050}.
FT   MOD_RES     371    371       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:18034455}.
FT   VAR_SEQ     142    148       Missing (in isoform A1-I and isoform A1-
FT                                III). {ECO:0000303|PubMed:10722719}.
FT                                /FTId=VSP_000342.
FT   VAR_SEQ     712    712       E -> EPTEDEV (in isoform A1-I).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_000343.
FT   VARIANT     194    194       L -> F.
FT   CONFLICT     36     36       Q -> N (in Ref. 1; AAC83083).
FT                                {ECO:0000305}.
FT   CONFLICT     88     92       VPFPR -> APLPW (in Ref. 1; AAC83083).
FT                                {ECO:0000305}.
FT   CONFLICT    112    112       N -> D (in Ref. 1; AAC83083).
FT                                {ECO:0000305}.
FT   CONFLICT    190    190       F -> S (in Ref. 1; AAC83083).
FT                                {ECO:0000305}.
FT   CONFLICT    262    262       K -> T (in Ref. 1; AAC83083).
FT                                {ECO:0000305}.
FT   CONFLICT    337    337       L -> P (in Ref. 1; AAC83083).
FT                                {ECO:0000305}.
FT   CONFLICT    357    357       S -> F (in Ref. 1; AAC83083).
FT                                {ECO:0000305}.
FT   CONFLICT    415    415       G -> R (in Ref. 1; AAC83083).
FT                                {ECO:0000305}.
FT   CONFLICT    518    518       F -> L (in Ref. 1; AAC83083).
FT                                {ECO:0000305}.
FT   CONFLICT    683    683       G -> W (in Ref. 1; AAC83083).
FT                                {ECO:0000305}.
FT   CONFLICT    803    803       H -> L (in Ref. 1; AAC83083).
FT                                {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
//
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