VATG1_HUMAN
ID VATG1_HUMAN Reviewed; 118 AA.
AC O75348; Q6IB33;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 192.
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;
DE AltName: Full=Vacuolar proton pump subunit M16;
GN Name=ATP6V1G1; Synonyms=ATP6G, ATP6G1, ATP6J;
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 [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [6]
RP PROTEIN SEQUENCE OF 2-16; 38-48 AND 81-89, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RA Kanor S., Bienvenut W.V., Quadroni M.;
RL Submitted (DEC-2005) to UniProtKB.
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP FUNCTION.
RX PubMed=28296633; DOI=10.7554/elife.22693;
RA Miles A.L., Burr S.P., Grice G.L., Nathan J.A.;
RT "The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115,
RT control HIF1alpha prolyl hydroxylation by regulating cellular iron
RT levels.";
RL Elife 6:E22693-E22693(2017).
RN [11]
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).
RN [12]
RP REVIEW.
RX PubMed=32001091; DOI=10.1016/j.tibs.2019.12.007;
RA Vasanthakumar T., Rubinstein J.L.;
RT "Structure and Roles of V-type ATPases.";
RL Trends Biochem. Sci. 45:295-307(2020).
RN [13] {ECO:0007744|PDB:6WLZ, ECO:0007744|PDB:6WM2, ECO:0007744|PDB:6WM3, ECO:0007744|PDB:6WM4}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS), FUNCTION, AND
RP IDENTIFICATION IN THE V-ATPASE COMPLEX.
RX PubMed=33065002; DOI=10.1016/j.molcel.2020.09.029;
RA Wang L., Wu D., Robinson C.V., Wu H., Fu T.M.;
RT "Structures of a Complete Human V-ATPase Reveal Mechanisms of Its
RT Assembly.";
RL Mol. Cell 80:501-511.e3(2020).
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 (PubMed:33065002, PubMed:32001091). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments and in
CC some cell types, is targeted to the plasma membrane, where it is
CC responsible for acidifying the extracellular environment
CC (PubMed:32001091). In aerobic conditions, involved in intracellular
CC iron homeostasis, thus triggering the activity of Fe(2+) prolyl
CC hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and
CC subsequent proteasomal degradation (PubMed:28296633).
CC {ECO:0000269|PubMed:28296633, ECO:0000269|PubMed:33065002,
CC ECO:0000303|PubMed:32001091}.
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 (PubMed:33065002). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:33065002). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:33065002).
CC {ECO:0000269|PubMed:33065002}.
CC -!- INTERACTION:
CC O75348; Q96A05: ATP6V1E2; NbExp=12; IntAct=EBI-711802, EBI-8650380;
CC O75348; Q08379: GOLGA2; NbExp=3; IntAct=EBI-711802, EBI-618309;
CC O75348; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-711802, EBI-5916454;
CC O75348; Q9H8Y8: GORASP2; NbExp=5; IntAct=EBI-711802, EBI-739467;
CC O75348; O95751: LDOC1; NbExp=4; IntAct=EBI-711802, EBI-740738;
CC O75348; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-711802, EBI-12039345;
CC O75348; P43360: MAGEA6; NbExp=3; IntAct=EBI-711802, EBI-1045155;
CC O75348; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-711802, EBI-741158;
CC O75348; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-711802, EBI-302345;
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:12384298).
CC {ECO:0000269|PubMed:12384298, ECO:0000269|PubMed:29993276}.
CC -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR EMBL; AF038954; AAC39868.1; -; mRNA.
DR EMBL; CR456971; CAG33252.1; -; mRNA.
DR EMBL; CR542237; CAG47033.1; -; mRNA.
DR EMBL; AL160275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87424.1; -; Genomic_DNA.
DR EMBL; BC008452; AAH08452.1; -; mRNA.
DR CCDS; CCDS6807.1; -.
DR RefSeq; NP_004879.1; NM_004888.3.
DR PDB; 6WLZ; EM; 2.90 A; K/L/M=1-118.
DR PDB; 6WM2; EM; 3.10 A; K/L/M=1-118.
DR PDB; 6WM3; EM; 3.40 A; K/L/M=1-118.
DR PDB; 6WM4; EM; 3.60 A; K/L/M=1-118.
DR PDBsum; 6WLZ; -.
DR PDBsum; 6WM2; -.
DR PDBsum; 6WM3; -.
DR PDBsum; 6WM4; -.
DR AlphaFoldDB; O75348; -.
DR SMR; O75348; -.
DR BioGRID; 114922; 73.
DR IntAct; O75348; 49.
DR MINT; O75348; -.
DR STRING; 9606.ENSP00000363162; -.
DR DrugBank; DB01133; Tiludronic acid.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR GlyGen; O75348; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75348; -.
DR PhosphoSitePlus; O75348; -.
DR BioMuta; ATP6V1G1; -.
DR EPD; O75348; -.
DR jPOST; O75348; -.
DR MassIVE; O75348; -.
DR PaxDb; O75348; -.
DR PeptideAtlas; O75348; -.
DR PRIDE; O75348; -.
DR ProteomicsDB; 49917; -.
DR Antibodypedia; 3900; 156 antibodies from 24 providers.
DR DNASU; 9550; -.
DR Ensembl; ENST00000374050.4; ENSP00000363162.3; ENSG00000136888.8.
DR GeneID; 9550; -.
DR KEGG; hsa:9550; -.
DR MANE-Select; ENST00000374050.4; ENSP00000363162.3; NM_004888.4; NP_004879.1.
DR UCSC; uc004bjc.4; human.
DR CTD; 9550; -.
DR DisGeNET; 9550; -.
DR GeneCards; ATP6V1G1; -.
DR HGNC; HGNC:864; ATP6V1G1.
DR HPA; ENSG00000136888; Low tissue specificity.
DR MIM; 607296; gene.
DR neXtProt; NX_O75348; -.
DR OpenTargets; ENSG00000136888; -.
DR PharmGKB; PA25163; -.
DR VEuPathDB; HostDB:ENSG00000136888; -.
DR eggNOG; KOG1772; Eukaryota.
DR GeneTree; ENSGT00940000154399; -.
DR HOGENOM; CLU_125101_1_1_1; -.
DR InParanoid; O75348; -.
DR OMA; HSKGNEQ; -.
DR OrthoDB; 1566576at2759; -.
DR PhylomeDB; O75348; -.
DR TreeFam; TF313777; -.
DR BioCyc; MetaCyc:HS06241-MON; -.
DR PathwayCommons; O75348; -.
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; O75348; -.
DR SIGNOR; O75348; -.
DR BioGRID-ORCS; 9550; 736 hits in 1090 CRISPR screens.
DR ChiTaRS; ATP6V1G1; human.
DR GeneWiki; ATP6V1G1; -.
DR GenomeRNAi; 9550; -.
DR Pharos; O75348; Tbio.
DR PRO; PR:O75348; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O75348; protein.
DR Bgee; ENSG00000136888; Expressed in adrenal tissue and 207 other tissues.
DR ExpressionAtlas; O75348; baseline and differential.
DR Genevisible; O75348; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
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:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
DR GO; GO:0036295; P:cellular response to increased oxygen levels; IMP:UniProtKB.
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 3D-structure; Acetylation; Cell membrane; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..118
FT /note="V-type proton ATPase subunit G 1"
FT /id="PRO_0000192897"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6"
FT HELIX 29..90
FT /evidence="ECO:0007829|PDB:6WLZ"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:6WLZ"
SQ SEQUENCE 118 AA; 13758 MW; A289C1B96634E34C CRC64;
MASQSQGIQQ LLQAEKRAAE KVSEARKRKN RRLKQAKEEA QAEIEQYRLQ REKEFKAKEA
AALGSRGSCS TEVEKETQEK MTILQTYFRQ NRDEVLDNLL AFVCDIRPEI HENYRING
