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   27-MAR-2024, entry version 166.
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; 4.
DR   IntAct; Q96LB4; 2.
DR   STRING; 9606.ENSP00000417171; -.
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; 9606-ENSP00000281087; -.
DR   PeptideAtlas; Q96LB4; -.
DR   ProteomicsDB; 77189; -. [Q96LB4-1]
DR   ProteomicsDB; 77190; -. [Q96LB4-3]
DR   ProteomicsDB; 77191; -. [Q96LB4-4]
DR   Antibodypedia; 34484; 115 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   AGR; HGNC:18265; -.
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; SYHRNME; -.
DR   OrthoDB; 33708at2759; -.
DR   PhylomeDB; Q96LB4; -.
DR   TreeFam; TF313777; -.
DR   BioCyc; MetaCyc:HS07734-MONOMER; -.
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 1148 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 male germ line stem cell (sensu Vertebrata) in testis and 28 other cell types or tissues.
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   Gene3D; 1.20.5.2950; -; 1.
DR   InterPro; IPR005124; V-ATPase_G.
DR   NCBIfam; TIGR01147; V_ATP_synt_G; 1.
DR   PANTHER; PTHR12713:SF5; V-TYPE PROTON ATPASE SUBUNIT G 3; 1.
DR   PANTHER; PTHR12713; VACUOLAR ATP SYNTHASE SUBUNIT G; 1.
DR   Pfam; PF03179; V-ATPase_G; 1.
DR   Genevisible; Q96LB4; HS.
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
//