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Database: UniProt
Entry: Q9JHF5_MOUSE
LinkDB: Q9JHF5_MOUSE
Original site: Q9JHF5_MOUSE 
ID   Q9JHF5_MOUSE            Unreviewed;       834 AA.
AC   Q9JHF5;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   22-NOV-2017, entry version 103.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=Tcirg1 {ECO:0000313|EMBL:EDL32965.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000001801, ECO:0000313|MGI:MGI:1350931};
GN   Synonyms=Oc116 {ECO:0000313|EMBL:AAF37193.1};
GN   ORFNames=mCG_3894 {ECO:0000313|EMBL:EDL32965.1};
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 {ECO:0000313|EMBL:BAA93006.1};
RN   [1] {ECO:0000313|EMBL:AAF37193.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/Sv {ECO:0000313|EMBL:AAF37193.1};
RX   PubMed=10709991; DOI=10.1016/S8756-3282(99)00278-1;
RA   Scimeca J.C., Franchi A., Trojani C., Parrinello H., Grosgeorge J.,
RA   Robert C., Jaillon O., Poirier C., Gaudray P., Carle G.F.;
RT   "The gene encoding the mouse homologue of the human osteoclast-
RT   specific 116-kDa V-ATPase subunit bears a deletion in osteosclerotic
RT   (oc/oc) mutants.";
RL   Bone 26:207-213(2000).
RN   [2] {ECO:0000313|EMBL:BAA93006.1}
RP   NUCLEOTIDE SEQUENCE.
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   [3] {ECO:0000313|EMBL:EDL32965.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDL32965.1};
RX   PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4] {ECO:0000313|EMBL:EDL32965.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDL32965.1};
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] {ECO:0000213|PubMed:19144319}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6] {ECO:0000313|Ensembl:ENSMUSP00000001801, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000001801,
RC   ECO:0000313|Proteomes:UP000000589};
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   [7] {ECO:0000213|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [8] {ECO:0000313|Ensembl:ENSMUSP00000001801}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000001801};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-
CC       ATPase), a multimeric enzyme that catalyzes the translocation of
CC       protons across the membranes. Required for assembly and activity
CC       of the V-ATPase. {ECO:0000256|RuleBase:RU361189}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|RuleBase:RU361189}.
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DR   EMBL; AC133523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF188702; AAF37193.1; -; Genomic_DNA.
DR   EMBL; AB022322; BAA93006.1; -; mRNA.
DR   EMBL; CH466612; EDL32965.1; -; Genomic_DNA.
DR   EMBL; CH466612; EDL32968.1; -; Genomic_DNA.
DR   RefSeq; NP_001129563.1; NM_001136091.2.
DR   RefSeq; NP_001161256.1; NM_001167784.1.
DR   RefSeq; NP_058617.3; NM_016921.3.
DR   UniGene; Mm.271689; -.
DR   MINT; MINT-4129645; -.
DR   STRING; 10090.ENSMUSP00000001801; -.
DR   Ensembl; ENSMUST00000001801; ENSMUSP00000001801; ENSMUSG00000001750.
DR   Ensembl; ENSMUST00000126070; ENSMUSP00000120531; ENSMUSG00000001750.
DR   Ensembl; ENSMUST00000145791; ENSMUSP00000122474; ENSMUSG00000001750.
DR   GeneID; 27060; -.
DR   KEGG; mmu:27060; -.
DR   UCSC; uc008fxk.2; mouse.
DR   CTD; 10312; -.
DR   MGI; MGI:1350931; Tcirg1.
DR   eggNOG; KOG2189; Eukaryota.
DR   eggNOG; COG1269; LUCA.
DR   GeneTree; ENSGT00390000004941; -.
DR   HOVERGEN; HBG014606; -.
DR   KO; K02154; -.
DR   OMA; WRACRGF; -.
DR   OrthoDB; EOG091G031W; -.
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   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000001750; -.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA: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; IBA:GO_Central.
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:0016236; P:macroautophagy; IMP:MGI.
DR   GO; GO:0007039; P:protein catabolic process in the vacuole; 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   Complete proteome {ECO:0000313|Proteomes:UP000000589};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|RuleBase:RU361189};
KW   Proteomics identification {ECO:0000213|MaxQB:Q9JHF5,
KW   ECO:0000213|PeptideAtlas:Q9JHF5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transmembrane {ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    399    423       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    444    462       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    505    524       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    536    555       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    575    594       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    601    620       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    632    657       Helical. {ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM    770    795       Helical. {ECO:0000256|RuleBase:RU361189}.
SQ   SEQUENCE   834 AA;  93460 MW;  E95ECD70C26367C0 CRC64;
     MGSMFRSEEV ALVQLLLPTG SAYNCVSQLG ELGLVEFRDL NESVSAFQRR FVVDVRRCEE
     LEKTFTFLRE EVQRAGLTLA PPEGTLPAPP PRDLLRIQEE TDRLAQELRD VRGNQQALRA
     QLHQLRLHSA VLGQSHSPPV AADHTEGPFS ETTPLLPGTR GPHSDLKVNF VAGAVEPYKA
     AALERLLWRA CRGFLIASFR ETEGQLEDPV TGEPATWMTF VISYWGEQIG QKIRKITDCF
     HCHVFPYLEQ EEARFRTLQQ LQQQSQELQE VLGETDRFLS QVLGRVQQLL PPWQVQIHKM
     KAVYLTLNQC SVNTTHKCLI AEVWCAARDL PTVQQALQSG SSEEGVSAVA HRIPCQDMPP
     TLIRTNRFTS SFQGIVDAYG VGRYREVNPA PYTIITFPFL FAVMFGDVGH GLLMFLFALA
     MVLTENRPAV KAAQNEIWQT FFGGRYLLLL MGLFSVYTGF IYNECFSRAT TIFPSGWSVA
     AMANQSGWSD EYLSQHSMLT LNPNITGVFL GPYPFGIDPI WSLATNHLSF LNSFKMKMSV
     ILGVTHMAFG VFLSIFNHVH FGQAHRLLLE TLPELIFLLG LFGYLVFLIV YKWVNVSAAS
     ASSAPSILIH FINMFLFSQN PTNHLLFHGQ EVVQYVLVVL ALATVPILLL GTPLYLLRQH
     RHRRNTQRRP AGQQDEDTDK LLASPDASTL ENSWSPDEEK AGSPGDEETE FVPSEIFMHQ
     AIHTIEFCLG CISNTASYLR LWALSLAHAQ LSEVLWAMVM RIGLGMGREI GVAAVVLVPV
     FAAFAVLTVA ILLVMEGLSA FLHALRLHWV EFQNKFYSGT GYKLSPFTFT VDSD
//
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