ID   VATG3_MOUSE             Reviewed;         118 AA.
AC   Q8BMC1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=V-type proton ATPase subunit G 3;
DE            Short=V-ATPase subunit G 3;
DE   AltName: Full=V-ATPase 13 kDa subunit 3;
DE   AltName: Full=Vacuolar proton pump subunit G 3;
GN   Name=Atp6v1g3; Synonyms=Atp6g3;
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], AND TISSUE SPECIFICITY.
RX   PubMed=12527205; DOI=10.1016/s0378-1119(02)01099-5;
RA   Sun-Wada G.-H., Yoshimizu T., Imai-Senga Y., Wada Y., Futai M.;
RT   "Diversity of mouse proton-translocating ATPase: presence of multiple
RT   isoforms of the C, d and G subunits.";
RL   Gene 302:147-153(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
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).
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. V-ATPase is responsible for acidifying and maintaining the pH
CC       of intracellular compartments and in some cell types, is targeted to
CC       the plasma membrane, where it is responsible for acidifying the
CC       extracellular environment. {ECO:0000250|UniProtKB:O75348}.
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. The V1 complex consists of three catalytic AB heterodimers
CC       that form a heterohexamer, three peripheral stalks each consisting of
CC       EG heterodimers, one central rotor including subunits D and F, and the
CC       regulatory subunits C and H. The proton translocation complex V0
CC       consists of the proton transport subunit a, a ring of proteolipid
CC       subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC       subunits ATP6AP1/Ac45 and ATP6AP2/PRR. {ECO:0000250|UniProtKB:O75348}.
CC   -!- TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:12527205}.
CC   -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR   EMBL; AB088359; BAC57952.1; -; mRNA.
DR   EMBL; AK032887; BAC28072.1; -; mRNA.
DR   EMBL; BC107267; AAI07268.1; -; mRNA.
DR   EMBL; BC107268; AAI07269.1; -; mRNA.
DR   CCDS; CCDS15331.1; -.
DR   RefSeq; NP_796371.1; NM_177397.3.
DR   AlphaFoldDB; Q8BMC1; -.
DR   SMR; Q8BMC1; -.
DR   BioGRID; 237226; 1.
DR   STRING; 10090.ENSMUSP00000027643; -.
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; Q8BMC1; -.
DR   PhosphoSitePlus; Q8BMC1; -.
DR   jPOST; Q8BMC1; -.
DR   MaxQB; Q8BMC1; -.
DR   PaxDb; Q8BMC1; -.
DR   PeptideAtlas; Q8BMC1; -.
DR   PRIDE; Q8BMC1; -.
DR   ProteomicsDB; 275173; -.
DR   Antibodypedia; 34484; 105 antibodies from 26 providers.
DR   DNASU; 338375; -.
DR   Ensembl; ENSMUST00000027643; ENSMUSP00000027643; ENSMUSG00000026394.
DR   GeneID; 338375; -.
DR   KEGG; mmu:338375; -.
DR   UCSC; uc007cvm.1; mouse.
DR   CTD; 127124; -.
DR   MGI; MGI:2450548; Atp6v1g3.
DR   VEuPathDB; HostDB:ENSMUSG00000026394; -.
DR   eggNOG; KOG1772; Eukaryota.
DR   GeneTree; ENSGT00940000160882; -.
DR   HOGENOM; CLU_125101_1_1_1; -.
DR   InParanoid; Q8BMC1; -.
DR   OMA; DQYRMQK; -.
DR   OrthoDB; 1566576at2759; -.
DR   PhylomeDB; Q8BMC1; -.
DR   TreeFam; TF313777; -.
DR   Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-MMU-77387; Insulin receptor recycling.
DR   Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-MMU-983712; Ion channel transport.
DR   BioGRID-ORCS; 338375; 0 hits in 72 CRISPR screens.
DR   PRO; PR:Q8BMC1; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8BMC1; protein.
DR   Bgee; ENSMUSG00000026394; Expressed in right kidney and 9 other tissues.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IC:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IDA:MGI.
DR   GO; GO:1902600; P:proton transmembrane transport; IC:MGI.
DR   InterPro; IPR005124; V-ATPase_G.
DR   PANTHER; PTHR12713; PTHR12713; 1.
DR   Pfam; PF03179; V-ATPase_G; 1.
DR   TIGRFAMs; TIGR01147; V_ATP_synt_G; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..118
FT                   /note="V-type proton ATPase subunit G 3"
FT                   /id="PRO_0000285921"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          5..53
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        14..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   118 AA;  13749 MW;  1D3EF03A5CEB61EE CRC64;
     MTSQSQGIQQ LLQAEKRAKD KLDEAKKRKG KRLRQAKEEA VAETDQYRMQ MEKDFRLKQA
     KIMGSQSHLS DEIEEQTLEK IKELNGSYNK CMESVIKQLL SMVCDMKPEV HVNYRATN