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   27-MAR-2024, entry version 201.
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   PDB; 7U4T; EM; 3.60 A; K/L/M=1-118.
DR   PDB; 7UNF; EM; 4.08 A; e/f/g=1-118.
DR   PDBsum; 6WLZ; -.
DR   PDBsum; 6WM2; -.
DR   PDBsum; 6WM3; -.
DR   PDBsum; 6WM4; -.
DR   PDBsum; 7U4T; -.
DR   PDBsum; 7UNF; -.
DR   AlphaFoldDB; O75348; -.
DR   EMDB; EMD-21845; -.
DR   EMDB; EMD-21847; -.
DR   EMDB; EMD-21848; -.
DR   EMDB; EMD-21849; -.
DR   EMDB; EMD-26334; -.
DR   EMDB; EMD-26623; -.
DR   SMR; O75348; -.
DR   BioGRID; 114922; 91.
DR   IntAct; O75348; 50.
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; 9606-ENSP00000363162; -.
DR   PeptideAtlas; O75348; -.
DR   ProteomicsDB; 49917; -.
DR   Pumba; O75348; -.
DR   Antibodypedia; 3900; 165 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   AGR; HGNC:864; -.
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; ARKYRQD; -.
DR   OrthoDB; 33708at2759; -.
DR   PhylomeDB; O75348; -.
DR   TreeFam; TF313777; -.
DR   BioCyc; MetaCyc:HS06241-MONOMER; -.
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; 770 hits in 1177 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 209 other cell types or tissues.
DR   ExpressionAtlas; O75348; baseline and differential.
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:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:1902495; C:transmembrane transporter complex; IEA:Ensembl.
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:0036295; P:cellular response to increased oxygen levels; IMP:UniProtKB.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
DR   GO; GO:0097401; P:synaptic vesicle lumen acidification; IEA:Ensembl.
DR   Gene3D; 1.20.5.2950; -; 1.
DR   InterPro; IPR005124; V-ATPase_G.
DR   NCBIfam; TIGR01147; V_ATP_synt_G; 1.
DR   PANTHER; PTHR12713:SF12; V-TYPE PROTON ATPASE SUBUNIT G 1; 1.
DR   PANTHER; PTHR12713; VACUOLAR ATP SYNTHASE SUBUNIT G; 1.
DR   Pfam; PF03179; V-ATPase_G; 1.
DR   Genevisible; O75348; HS.
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
//