ID   VATG1_MOUSE             Reviewed;         118 AA.
AC   Q9CR51;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=V-type proton ATPase subunit G 1;
DE            Short=V-ATPase subunit G 1;
DE   AltName: Full=V-ATPase 13 kDa subunit 1;
DE   AltName: Full=Vacuolar proton pump subunit G 1;
GN   Name=Atp6v1g1; Synonyms=Atp6g1;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, and Tongue;
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   [2]
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   [3]
RP   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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   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   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=29993276; DOI=10.1152/ajprenal.00539.2017;
RA   Frische S., Chambrey R., Trepiccione F., Zamani R., Marcussen N.,
RA   Alexander R.T., Skjoedt K., Svenningsen P., Dimke H.;
RT   "H+-ATPase B1 subunit localizes to thick ascending limb and distal
RT   convoluted tubule of rodent and human kidney.";
RL   Am. J. Physiol. 315:F429-F444(2018).
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 (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). In aerobic
CC       conditions, involved in intracellular iron homeostasis, thus triggering
CC       the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to
CC       HIF1A hydroxylation and subsequent proteasomal degradation (By
CC       similarity). {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 (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). {ECO:0000250|UniProtKB:O75348}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:29993276}.
CC   -!- TISSUE SPECIFICITY: Kidney; localizes to early distal nephron,
CC       encompassing thick ascending limbs and distal convoluted tubules (at
CC       protein level)(PubMed:29993276). Ubiquitous (PubMed:12527205).
CC       {ECO:0000269|PubMed:12527205, ECO:0000269|PubMed:29993276}.
CC   -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR   EMBL; AK010131; BAB26720.1; -; mRNA.
DR   EMBL; AK003563; BAB22859.1; -; mRNA.
DR   EMBL; AK007596; BAB25127.1; -; mRNA.
DR   EMBL; BC003429; AAH03429.1; -; mRNA.
DR   CCDS; CCDS18260.1; -.
DR   RefSeq; NP_077135.1; NM_024173.2.
DR   AlphaFoldDB; Q9CR51; -.
DR   SMR; Q9CR51; -.
DR   BioGRID; 211359; 9.
DR   IntAct; Q9CR51; 1.
DR   MINT; Q9CR51; -.
DR   STRING; 10090.ENSMUSP00000048770; -.
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; Q9CR51; -.
DR   PhosphoSitePlus; Q9CR51; -.
DR   SwissPalm; Q9CR51; -.
DR   EPD; Q9CR51; -.
DR   jPOST; Q9CR51; -.
DR   MaxQB; Q9CR51; -.
DR   PaxDb; Q9CR51; -.
DR   PRIDE; Q9CR51; -.
DR   ProteomicsDB; 300193; -.
DR   Antibodypedia; 3900; 156 antibodies from 24 providers.
DR   DNASU; 66290; -.
DR   Ensembl; ENSMUST00000035301; ENSMUSP00000048770; ENSMUSG00000039105.
DR   GeneID; 66290; -.
DR   KEGG; mmu:66290; -.
DR   UCSC; uc008tgq.2; mouse.
DR   CTD; 9550; -.
DR   MGI; MGI:1913540; Atp6v1g1.
DR   VEuPathDB; HostDB:ENSMUSG00000039105; -.
DR   eggNOG; KOG1772; Eukaryota.
DR   GeneTree; ENSGT00940000154399; -.
DR   HOGENOM; CLU_125101_1_1_1; -.
DR   InParanoid; Q9CR51; -.
DR   OMA; HSKGNEQ; -.
DR   OrthoDB; 1566576at2759; -.
DR   PhylomeDB; Q9CR51; -.
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; 66290; 25 hits in 72 CRISPR screens.
DR   ChiTaRS; Atp6v1g1; mouse.
DR   PRO; PR:Q9CR51; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9CR51; protein.
DR   Bgee; ENSMUSG00000039105; Expressed in granulocyte and 124 other tissues.
DR   ExpressionAtlas; Q9CR51; baseline and differential.
DR   Genevisible; Q9CR51; MM.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:MGI.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI.
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:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
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   Acetylation; Cell membrane; Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O75348"
FT   CHAIN           2..118
FT                   /note="V-type proton ATPase subunit G 1"
FT                   /id="PRO_0000192898"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O75348"
SQ   SEQUENCE   118 AA;  13724 MW;  1FC54025CFCFD951 CRC64;
     MASQSQGIQQ LLQAEKRAAE KVSEARKRKN RRLKQAKEEA QAEIEQYRLQ REKEFKAKEA
     AALGSHGSCS SEVEKETREK MTVLQNYFEQ NRDEVLDNLL AFVCDIRPEI HENYRING