VATG3_HUMAN
ID VATG3_HUMAN Reviewed; 118 AA.
AC Q96LB4; Q495K2; Q495K4; Q5T9L6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=V-type proton ATPase subunit G 3;
DE Short=V-ATPase subunit G 3;
DE AltName: Full=V-ATPase 13 kDa subunit 3;
DE AltName: Full=Vacuolar proton pump subunit G 3;
GN Name=ATP6V1G3; Synonyms=ATP6G3;
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 [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND TISSUE
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
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).
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 Q96LB4-4; P32243-2: OTX2; NbExp=3; IntAct=EBI-12941272, EBI-9087860;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96LB4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96LB4-2; Sequence=Not described;
CC Name=3;
CC IsoId=Q96LB4-3; Sequence=VSP_036423;
CC Name=4;
CC IsoId=Q96LB4-4; Sequence=VSP_036426;
CC -!- TISSUE SPECIFICITY: Kidney. {ECO:0000269|PubMed:12384298}.
CC -!- SIMILARITY: Belongs to the V-ATPase G subunit family. {ECO:0000305}.
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DR EMBL; AY039760; AAK83465.1; -; mRNA.
DR EMBL; AL157402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101129; AAI01130.1; -; mRNA.
DR EMBL; BC101130; AAI01131.1; -; mRNA.
DR EMBL; BC101131; AAI01132.2; -; mRNA.
DR CCDS; CCDS1395.1; -. [Q96LB4-1]
DR CCDS; CCDS1396.1; -. [Q96LB4-3]
DR CCDS; CCDS81414.1; -. [Q96LB4-4]
DR RefSeq; NP_001307147.1; NM_001320218.1. [Q96LB4-4]
DR RefSeq; NP_573569.1; NM_133262.2. [Q96LB4-1]
DR RefSeq; NP_579872.1; NM_133326.1. [Q96LB4-3]
DR RefSeq; XP_006711226.1; XM_006711163.3.
DR RefSeq; XP_011507488.1; XM_011509186.2.
DR RefSeq; XP_011507489.1; XM_011509187.2.
DR AlphaFoldDB; Q96LB4; -.
DR SMR; Q96LB4; -.
DR BioGRID; 126042; 3.
DR IntAct; Q96LB4; 2.
DR STRING; 9606.ENSP00000281087; -.
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 iPTMnet; Q96LB4; -.
DR PhosphoSitePlus; Q96LB4; -.
DR BioMuta; ATP6V1G3; -.
DR DMDM; 20140697; -.
DR jPOST; Q96LB4; -.
DR MassIVE; Q96LB4; -.
DR PaxDb; Q96LB4; -.
DR PeptideAtlas; Q96LB4; -.
DR PRIDE; Q96LB4; -.
DR ProteomicsDB; 77189; -. [Q96LB4-1]
DR ProteomicsDB; 77190; -. [Q96LB4-3]
DR ProteomicsDB; 77191; -. [Q96LB4-4]
DR Antibodypedia; 34484; 105 antibodies from 26 providers.
DR DNASU; 127124; -.
DR Ensembl; ENST00000281087.6; ENSP00000281087.2; ENSG00000151418.12. [Q96LB4-1]
DR Ensembl; ENST00000309309.11; ENSP00000309574.7; ENSG00000151418.12. [Q96LB4-3]
DR Ensembl; ENST00000367381.2; ENSP00000356351.2; ENSG00000263014.5. [Q96LB4-1]
DR Ensembl; ENST00000367382.6; ENSP00000356352.2; ENSG00000151418.12. [Q96LB4-1]
DR Ensembl; ENST00000489986.1; ENSP00000417171.1; ENSG00000151418.12. [Q96LB4-4]
DR Ensembl; ENST00000571439.5; ENSP00000461616.1; ENSG00000263014.5. [Q96LB4-3]
DR Ensembl; ENST00000573121.5; ENSP00000461329.1; ENSG00000263014.5. [Q96LB4-1]
DR Ensembl; ENST00000575971.5; ENSP00000461228.1; ENSG00000263014.5. [Q96LB4-4]
DR GeneID; 127124; -.
DR KEGG; hsa:127124; -.
DR MANE-Select; ENST00000367382.6; ENSP00000356352.2; NM_001376861.1; NP_001363790.1.
DR UCSC; uc001guo.3; human. [Q96LB4-1]
DR CTD; 127124; -.
DR DisGeNET; 127124; -.
DR GeneCards; ATP6V1G3; -.
DR HGNC; HGNC:18265; ATP6V1G3.
DR HPA; ENSG00000151418; Tissue enriched (kidney).
DR MIM; 618071; gene.
DR neXtProt; NX_Q96LB4; -.
DR OpenTargets; ENSG00000151418; -.
DR PharmGKB; PA38515; -.
DR VEuPathDB; HostDB:ENSG00000151418; -.
DR eggNOG; KOG1772; Eukaryota.
DR GeneTree; ENSGT00940000160882; -.
DR HOGENOM; CLU_125101_1_1_1; -.
DR InParanoid; Q96LB4; -.
DR OMA; DQYRMQK; -.
DR OrthoDB; 1566576at2759; -.
DR PhylomeDB; Q96LB4; -.
DR TreeFam; TF313777; -.
DR BioCyc; MetaCyc:HS07734-MON; -.
DR PathwayCommons; Q96LB4; -.
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; Q96LB4; -.
DR BioGRID-ORCS; 127124; 15 hits in 1070 CRISPR screens.
DR GeneWiki; ATP6V1G3; -.
DR GenomeRNAi; 127124; -.
DR Pharos; Q96LB4; Tbio.
DR PRO; PR:Q96LB4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96LB4; protein.
DR Bgee; ENSG00000151418; Expressed in adult mammalian kidney and 29 other tissues.
DR Genevisible; Q96LB4; HS.
DR GO; GO:0005829; C:cytosol; IDA: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:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:Ensembl.
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; Coiled coil; Hydrogen ion transport; Ion transport;
KW Reference proteome; Transport.
FT CHAIN 1..118
FT /note="V-type proton ATPase subunit G 3"
FT /id="PRO_0000192904"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..54
FT /evidence="ECO:0000255"
FT COMPBIAS 13..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 28..118
FT /note="RKGKRLKQAKEEAMVEIDQYRMQRDKEFRLKQSKIMGSQNNLSDEIEEQTLG
FT KIQELNGHYNKYMESVMNQLLSMVCDMKPEIHVNYRATN -> ILHLLFLKRRDWDCFW
FT KRKAIEASQGGSNGRN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036423"
FT VAR_SEQ 28
FT /note="R -> KTGTASG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036426"
FT VARIANT 54
FT /note="E -> Q (in dbSNP:rs16843254)"
FT /id="VAR_048343"
SQ SEQUENCE 118 AA; 13917 MW; 651F8F5497164754 CRC64;
MTSQSQGIHQ LLQAEKRAKD KLEEAKKRKG KRLKQAKEEA MVEIDQYRMQ RDKEFRLKQS
KIMGSQNNLS DEIEEQTLGK IQELNGHYNK YMESVMNQLL SMVCDMKPEI HVNYRATN
