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V-type proton ATPase subunit G 1 (V-ATPase subunit G 1) (V-ATPase 13 kDa subunit 1) (Vacuolar proton pump subunit G 1) (Vacuolar proton pump subunit M16)

 VATG1_HUMAN             Reviewed;         118 AA.
O75348; Q6IB33;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
18-JUL-2018, entry version 167.
RecName: Full=V-type proton ATPase subunit G 1;
Short=V-ATPase subunit G 1;
AltName: Full=V-ATPase 13 kDa subunit 1;
AltName: Full=Vacuolar proton pump subunit G 1;
AltName: Full=Vacuolar proton pump subunit M16;
Name=ATP6V1G1; Synonyms=ATP6G, ATP6G1, ATP6J;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
Wang Y.-X., Chen S.-J., Chen Z.;
"Identification of genes expressed in human CD34(+) hematopoietic
stem/progenitor cells by expressed sequence tags and efficient full-
length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-16; 38-48 AND 81-89, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Melanoma;
Kanor S., Bienvenut W.V., Quadroni M.;
Submitted (DEC-2005) to UniProtKB.
[7]
TISSUE SPECIFICITY.
PubMed=12384298; DOI=10.1016/S0378-1119(02)00884-3;
Smith A.N., Borthwick K.J., Karet F.E.;
"Molecular cloning and characterization of novel tissue-specific
isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and
their evaluation in autosomal recessive distal renal tubular
acidosis.";
Gene 297:169-177(2002).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[10]
FUNCTION.
PubMed=28296633; DOI=10.7554/eLife.22693;
Miles A.L., Burr S.P., Grice G.L., Nathan J.A.;
"The vacuolar-ATPase complex and assembly factors, TMEM199 and
CCDC115, control HIF1alpha prolyl hydroxylation by regulating cellular
iron levels.";
Elife 6:E22693-E22693(2017).
-!- FUNCTION: Catalytic subunit of the peripheral V1 complex of
vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying
a variety of intracellular compartments in eukaryotic cells. In
aerobic conditions, involved in intracellular iron homeostasis,
thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD)
enzymes, and leading to HIF1A hydroxylation and subsequent
proteasomal degradation (PubMed:28296633).
{ECO:0000269|PubMed:28296633}.
-!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
peripheral catalytic V1 complex (components A to H) attached to an
integral membrane V0 proton pore complex (components: a, c, c',
c'' and d).
-!- INTERACTION:
Q96A05:ATP6V1E2; NbExp=10; IntAct=EBI-711802, EBI-8650380;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-711802, EBI-618309;
O95751:LDOC1; NbExp=3; IntAct=EBI-711802, EBI-740738;
P43360:MAGEA6; NbExp=3; IntAct=EBI-711802, EBI-1045155;
P0C6X7:rep (xeno); NbExp=5; IntAct=EBI-711802, EBI-7843867;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12384298}.
-!- SIMILARITY: Belongs to the V-ATPase G subunit family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF038954; AAC39868.1; -; mRNA.
EMBL; CR456971; CAG33252.1; -; mRNA.
EMBL; CR542237; CAG47033.1; -; mRNA.
EMBL; AL160275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87424.1; -; Genomic_DNA.
EMBL; BC008452; AAH08452.1; -; mRNA.
CCDS; CCDS6807.1; -.
RefSeq; NP_004879.1; NM_004888.3.
UniGene; Hs.388654; -.
ProteinModelPortal; O75348; -.
SMR; O75348; -.
BioGrid; 114922; 27.
IntAct; O75348; 41.
MINT; O75348; -.
STRING; 9606.ENSP00000363162; -.
TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
iPTMnet; O75348; -.
PhosphoSitePlus; O75348; -.
BioMuta; ATP6V1G1; -.
EPD; O75348; -.
PaxDb; O75348; -.
PeptideAtlas; O75348; -.
PRIDE; O75348; -.
ProteomicsDB; 49917; -.
DNASU; 9550; -.
Ensembl; ENST00000374050; ENSP00000363162; ENSG00000136888.
GeneID; 9550; -.
KEGG; hsa:9550; -.
UCSC; uc004bjc.4; human.
CTD; 9550; -.
DisGeNET; 9550; -.
EuPathDB; HostDB:ENSG00000136888.6; -.
GeneCards; ATP6V1G1; -.
HGNC; HGNC:864; ATP6V1G1.
HPA; CAB004615; -.
HPA; HPA042898; -.
MIM; 607296; gene.
neXtProt; NX_O75348; -.
OpenTargets; ENSG00000136888; -.
PharmGKB; PA25163; -.
eggNOG; KOG1772; Eukaryota.
eggNOG; ENOG4111XX0; LUCA.
GeneTree; ENSGT00390000011172; -.
HOGENOM; HOG000186416; -.
HOVERGEN; HBG057827; -.
InParanoid; O75348; -.
KO; K02152; -.
OMA; EFHANYR; -.
OrthoDB; EOG091G0XIZ; -.
PhylomeDB; O75348; -.
TreeFam; TF313777; -.
BioCyc; MetaCyc:HS06241-MONOMER; -.
Reactome; R-HSA-1222556; ROS, RNS production in phagocytes.
Reactome; R-HSA-77387; Insulin receptor recycling.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
Reactome; R-HSA-983712; Ion channel transport.
ChiTaRS; ATP6V1G1; human.
GeneWiki; ATP6V1G1; -.
GenomeRNAi; 9550; -.
PRO; PR:O75348; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000136888; -.
CleanEx; HS_ATP6V1G1; -.
ExpressionAtlas; O75348; baseline and differential.
Genevisible; O75348; HS.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IEA:Ensembl.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0008553; F:proton-exporting ATPase activity, phosphorylative mechanism; IEA:Ensembl.
GO; GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
GO; GO:0036295; P:cellular response to increased oxygen levels; IMP:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0033572; P:transferrin transport; TAS:Reactome.
InterPro; IPR005124; V-ATPase_G.
PANTHER; PTHR12713; PTHR12713; 1.
Pfam; PF03179; V-ATPase_G; 1.
TIGRFAMs; TIGR01147; V_ATP_synt_G; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Direct protein sequencing;
Hydrogen ion transport; Ion transport; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.6}.
CHAIN 2 118 V-type proton ATPase subunit G 1.
/FTId=PRO_0000192897.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.6}.
SEQUENCE 118 AA; 13758 MW; A289C1B96634E34C CRC64;
MASQSQGIQQ LLQAEKRAAE KVSEARKRKN RRLKQAKEEA QAEIEQYRLQ REKEFKAKEA
AALGSRGSCS TEVEKETQEK MTILQTYFRQ NRDEVLDNLL AFVCDIRPEI HENYRING


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