ID   VATG2_MOUSE             Reviewed;         118 AA.
AC   Q9WTT4;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=V-type proton ATPase subunit G 2;
DE            Short=V-ATPase subunit G 2;
DE   AltName: Full=V-ATPase 13 kDa subunit 2;
DE   AltName: Full=Vacuolar proton pump subunit G 2;
GN   Name=Atp6v1g2; Synonyms=Atp6g2, Ng38;
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 GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA   Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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].
RC   TISSUE=Eye;
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=Brain;
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   -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000250|UniProtKB:O95670}.
CC       Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC       {ECO:0000250|UniProtKB:Q0VCV6}; Peripheral membrane protein
CC       {ECO:0000305}. Note=Highly enriched in late-stage melanosomes.
CC       {ECO:0000250|UniProtKB:O95670}.
CC   -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR   EMBL; AC007080; AAD30176.1; -; Genomic_DNA.
DR   EMBL; AK011945; BAB27931.1; -; mRNA.
DR   EMBL; BC020190; AAH20190.1; -; mRNA.
DR   EMBL; BC062380; AAH62380.1; -; mRNA.
DR   CCDS; CCDS37597.1; -.
DR   RefSeq; NP_001334280.1; NM_001347351.1.
DR   RefSeq; NP_075668.1; NM_023179.3.
DR   AlphaFoldDB; Q9WTT4; -.
DR   SMR; Q9WTT4; -.
DR   BioGRID; 211318; 8.
DR   IntAct; Q9WTT4; 2.
DR   MINT; Q9WTT4; -.
DR   STRING; 10090.ENSMUSP00000069482; -.
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; Q9WTT4; -.
DR   PhosphoSitePlus; Q9WTT4; -.
DR   SwissPalm; Q9WTT4; -.
DR   MaxQB; Q9WTT4; -.
DR   PaxDb; 10090-ENSMUSP00000069482; -.
DR   ProteomicsDB; 300194; -.
DR   DNASU; 66237; -.
DR   Ensembl; ENSMUST00000068261.9; ENSMUSP00000069482.9; ENSMUSG00000024403.17.
DR   GeneID; 66237; -.
DR   KEGG; mmu:66237; -.
DR   UCSC; uc008cgy.2; mouse.
DR   AGR; MGI:1913487; -.
DR   CTD; 534; -.
DR   MGI; MGI:1913487; Atp6v1g2.
DR   VEuPathDB; HostDB:ENSMUSG00000024403; -.
DR   eggNOG; KOG1772; Eukaryota.
DR   GeneTree; ENSGT00940000161280; -.
DR   HOGENOM; CLU_125101_1_1_1; -.
DR   InParanoid; Q9WTT4; -.
DR   OMA; ELHNNYR; -.
DR   OrthoDB; 33708at2759; -.
DR   PhylomeDB; Q9WTT4; -.
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; 66237; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Atp6v1g2; mouse.
DR   PRO; PR:Q9WTT4; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9WTT4; Protein.
DR   Bgee; ENSMUSG00000024403; Expressed in subiculum and 172 other cell types or tissues.
DR   ExpressionAtlas; Q9WTT4; baseline and differential.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IDA:MGI.
DR   GO; GO:0097401; P:synaptic vesicle lumen acidification; IDA:SynGO.
DR   Gene3D; 1.20.5.2950; -; 1.
DR   InterPro; IPR005124; V-ATPase_G.
DR   NCBIfam; TIGR01147; V_ATP_synt_G; 1.
DR   PANTHER; PTHR12713:SF13; V-TYPE PROTON ATPASE SUBUNIT G 2; 1.
DR   PANTHER; PTHR12713; VACUOLAR ATP SYNTHASE SUBUNIT G; 1.
DR   Pfam; PF03179; V-ATPase_G; 1.
DR   Genevisible; Q9WTT4; MM.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Transport.
FT   CHAIN           1..118
FT                   /note="V-type proton ATPase subunit G 2"
FT                   /id="PRO_0000192902"
FT   REGION          23..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   118 AA;  13651 MW;  32479E10DFF11078 CRC64;
     MASQTQGIQQ LLQAEKRAAE KVADARKRKA RRLKQAKEEA QMEVEQYRRE REQEFQSKQQ
     AAMGSQGNLS AEVEQATRRQ VQGMQSSQQR NRERVLAQLL GMVCEVRPQV HPNYRVTV
//