VATG2_MOUSE
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 03-AUG-2022, entry version 163.
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; 6.
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 MaxQB; Q9WTT4; -.
DR PaxDb; Q9WTT4; -.
DR PRIDE; Q9WTT4; -.
DR ProteomicsDB; 300194; -.
DR DNASU; 66237; -.
DR Ensembl; ENSMUST00000068261; ENSMUSP00000069482; ENSMUSG00000024403.
DR GeneID; 66237; -.
DR KEGG; mmu:66237; -.
DR UCSC; uc008cgy.2; mouse.
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; HPNYRIT; -.
DR OrthoDB; 1566576at2759; -.
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 71 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 170 other tissues.
DR ExpressionAtlas; Q9WTT4; baseline and differential.
DR Genevisible; Q9WTT4; MM.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
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 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 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
