VATG2_HUMAN
ID VATG2_HUMAN Reviewed; 118 AA.
AC O95670; B5MEF0; Q2L6F8; Q5HYU8; Q5RJ63;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 188.
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=ATP6G, ATP6G2, NG38;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10202016;
RA Neville M.J., Campbell R.D.;
RT "A new member of the Ig superfamily and a V-ATPase G subunit are among the
RT predicted products of novel genes close to the TNF locus in the human
RT MHC.";
RL J. Immunol. 162:4745-4754(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RA Iida A., Kondo K., Mishima C., Nakamura Y.;
RT "Genomic structure of human ATP6G gene.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shichi D., Naruse T., Nakashima M., Kikkawa E., Ota M., Katsuyama Y.,
RA Kimura A., Matsumori A., Inoko H.;
RT "Polymorphism of ATP6G.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
RT "Genome diversity in HLA: a new strategy for detection of genetic
RT polymorphisms in expressed genes within the HLA class III and class I
RT regions.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Leiomyosarcoma;
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-75 (ISOFORM 3).
RA Hillier L., Clark N., Dubuque T., Elliston K., Hawkins M., Holman M.,
RA Hultman M., Kucaba T., Le M., Lennon G., Marra M., Parsons J., Rifkin L.,
RA Rohlfing T., Soares M., Tan F., Trevaskis E., Waterston R., Williamson A.,
RA Wohldmann P., Wilson R.;
RT "The WashU-Merck EST project.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=12384298; DOI=10.1016/s0378-1119(02)00884-3;
RA Smith A.N., Borthwick K.J., Karet F.E.;
RT "Molecular cloning and characterization of novel tissue-specific isoforms
RT of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation
RT in autosomal recessive distal renal tubular acidosis.";
RL Gene 297:169-177(2002).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
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 -!- INTERACTION:
CC O95670; Q96A05: ATP6V1E2; NbExp=6; IntAct=EBI-348290, EBI-8650380;
CC O95670; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-348290, EBI-14096082;
CC -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000269|PubMed:17081065}.
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:0000269|PubMed:17081065}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95670-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95670-2; Sequence=VSP_045909;
CC Name=3;
CC IsoId=O95670-3; Sequence=VSP_047411;
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:12384298}.
CC -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR EMBL; Y14768; CAA75073.1; -; Genomic_DNA.
DR EMBL; AB063177; BAC00863.1; -; Genomic_DNA.
DR EMBL; AB102692; BAD74058.1; -; Genomic_DNA.
DR EMBL; AB097672; BAD74057.1; -; Genomic_DNA.
DR EMBL; BA000025; BAB63399.1; -; Genomic_DNA.
DR EMBL; AB088115; BAC54952.1; -; Genomic_DNA.
DR EMBL; AL662801; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX001040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR942185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03414.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03416.1; -; Genomic_DNA.
DR EMBL; AB202112; BAE78636.1; -; Genomic_DNA.
DR EMBL; AB103621; BAF31286.1; -; Genomic_DNA.
DR EMBL; BC047791; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC119726; AAI19727.1; -; mRNA.
DR EMBL; BC119727; AAI19728.1; -; mRNA.
DR EMBL; AA401769; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS4698.1; -. [O95670-1]
DR CCDS; CCDS4699.1; -. [O95670-3]
DR CCDS; CCDS56413.1; -. [O95670-2]
DR RefSeq; NP_001191007.1; NM_001204078.1. [O95670-2]
DR RefSeq; NP_569730.1; NM_130463.3. [O95670-1]
DR RefSeq; NP_612139.1; NM_138282.2. [O95670-3]
DR AlphaFoldDB; O95670; -.
DR SMR; O95670; -.
DR BioGRID; 107017; 36.
DR IntAct; O95670; 9.
DR STRING; 9606.ENSP00000302194; -.
DR DrugBank; DB01133; Tiludronic acid.
DR iPTMnet; O95670; -.
DR PhosphoSitePlus; O95670; -.
DR BioMuta; ATP6V1G2; -.
DR EPD; O95670; -.
DR jPOST; O95670; -.
DR MassIVE; O95670; -.
DR PaxDb; O95670; -.
DR PeptideAtlas; O95670; -.
DR PRIDE; O95670; -.
DR ProteomicsDB; 50983; -. [O95670-1]
DR ProteomicsDB; 6232; -.
DR ProteomicsDB; 62960; -.
DR Antibodypedia; 48928; 104 antibodies from 26 providers.
DR DNASU; 534; -.
DR Ensembl; ENST00000303892.10; ENSP00000302194.5; ENSG00000213760.11. [O95670-1]
DR Ensembl; ENST00000376151.4; ENSP00000365321.4; ENSG00000213760.11. [O95670-2]
DR Ensembl; ENST00000383503.4; ENSP00000372995.4; ENSG00000206445.4. [O95670-1]
DR Ensembl; ENST00000421596.2; ENSP00000406575.2; ENSG00000234668.3. [O95670-2]
DR Ensembl; ENST00000434217.2; ENSP00000406668.2; ENSG00000226850.2. [O95670-2]
DR Ensembl; ENST00000441959.2; ENSP00000395436.2; ENSG00000227587.2. [O95670-1]
DR Ensembl; ENST00000443657.2; ENSP00000416031.2; ENSG00000227587.2. [O95670-2]
DR Ensembl; ENST00000444088.2; ENSP00000406389.2; ENSG00000234920.3. [O95670-1]
DR Ensembl; ENST00000447174.2; ENSP00000403158.2; ENSG00000230900.5. [O95670-2]
DR Ensembl; ENST00000448779.2; ENSP00000409104.2; ENSG00000234920.3. [O95670-2]
DR Ensembl; ENST00000449748.2; ENSP00000406372.2; ENSG00000226850.2. [O95670-1]
DR Ensembl; ENST00000452453.2; ENSP00000402430.2; ENSG00000206445.4. [O95670-2]
DR Ensembl; ENST00000454370.2; ENSP00000413222.2; ENSG00000234668.3. [O95670-1]
DR Ensembl; ENST00000454889.2; ENSP00000408670.2; ENSG00000230900.5. [O95670-1]
DR Ensembl; ENST00000483251.1; ENSP00000419698.1; ENSG00000213760.11. [O95670-3]
DR GeneID; 534; -.
DR KEGG; hsa:534; -.
DR MANE-Select; ENST00000303892.10; ENSP00000302194.5; NM_130463.4; NP_569730.1.
DR UCSC; uc003ntz.4; human. [O95670-1]
DR CTD; 534; -.
DR DisGeNET; 534; -.
DR GeneCards; ATP6V1G2; -.
DR HGNC; HGNC:862; ATP6V1G2.
DR HPA; ENSG00000213760; Group enriched (brain, choroid plexus).
DR MIM; 606853; gene.
DR neXtProt; NX_O95670; -.
DR OpenTargets; ENSG00000213760; -.
DR PharmGKB; PA25164; -.
DR VEuPathDB; HostDB:ENSG00000213760; -.
DR eggNOG; KOG1772; Eukaryota.
DR GeneTree; ENSGT00940000161280; -.
DR HOGENOM; CLU_125101_1_1_1; -.
DR InParanoid; O95670; -.
DR OMA; HPNYRIT; -.
DR PhylomeDB; O95670; -.
DR TreeFam; TF313777; -.
DR BioCyc; MetaCyc:HS10685-MON; -.
DR PathwayCommons; O95670; -.
DR Reactome; R-HSA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-HSA-77387; Insulin receptor recycling.
DR Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
DR Reactome; R-HSA-9639288; Amino acids regulate mTORC1.
DR Reactome; R-HSA-983712; Ion channel transport.
DR SignaLink; O95670; -.
DR BioGRID-ORCS; 534; 14 hits in 1068 CRISPR screens.
DR GeneWiki; ATP6V1G2; -.
DR GenomeRNAi; 534; -.
DR Pharos; O95670; Tbio.
DR PRO; PR:O95670; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O95670; protein.
DR Bgee; ENSG00000213760; Expressed in cerebellar cortex and 98 other tissues.
DR ExpressionAtlas; O95670; baseline and differential.
DR Genevisible; O95670; HS.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:Ensembl.
DR GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
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 Alternative splicing; Cytoplasmic vesicle; Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transport.
FT CHAIN 1..118
FT /note="V-type proton ATPase subunit G 2"
FT /id="PRO_0000192900"
FT REGION 25..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.10"
FT /id="VSP_047411"
FT VAR_SEQ 35..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045909"
FT CONFLICT 52
FT /note="E -> D (in Ref. 10; AA401769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 118 AA; 13604 MW; 5D46EEE0C8D7657D CRC64;
MASQSQGIQQ LLQAEKRAAE KVADARKRKA RRLKQAKEEA QMEVEQYRRE REHEFQSKQQ
AAMGSQGNLS AEVEQATRRQ VQGMQSSQQR NRERVLAQLL GMVCDVRPQV HPNYRISA
