Full text data of ATP6V1G3
ATP6V1G3
(ATP6G3)
[Confidence: low (only semi-automatic identification from reviews)]
V-type proton ATPase subunit G 3; V-ATPase subunit G 3 (V-ATPase 13 kDa subunit 3; Vacuolar proton pump subunit G 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
V-type proton ATPase subunit G 3; V-ATPase subunit G 3 (V-ATPase 13 kDa subunit 3; Vacuolar proton pump subunit G 3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96LB4
ID VATG3_HUMAN Reviewed; 118 AA.
AC Q96LB4; Q495K2; Q495K4; Q5T9L6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 97.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND
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
RT isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and
RT their evaluation in autosomal recessive distal renal tubular
RT 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of
CC vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying
CC a variety of intracellular compartments in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (components A to H) attached to an
CC integral membrane V0 proton pore complex (components: a, c, c',
CC c'' and d) (By similarity).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Kidney.
CC -!- SIMILARITY: Belongs to the V-ATPase G subunit family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY039760; AAK83465.1; -; mRNA.
DR EMBL; AL157402; CAI15638.1; -; Genomic_DNA.
DR EMBL; BC101129; AAI01130.1; -; mRNA.
DR EMBL; BC101130; AAI01131.1; -; mRNA.
DR EMBL; BC101131; AAI01132.2; -; mRNA.
DR RefSeq; NP_573569.1; NM_133262.2.
DR RefSeq; NP_579872.1; NM_133326.1.
DR RefSeq; XP_005244949.1; XM_005244892.1.
DR RefSeq; XP_005276806.1; XM_005276749.1.
DR UniGene; Hs.127743; -.
DR ProteinModelPortal; Q96LB4; -.
DR SMR; Q96LB4; 3-81.
DR STRING; 9606.ENSP00000281087; -.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSite; Q96LB4; -.
DR DMDM; 20140697; -.
DR PaxDb; Q96LB4; -.
DR PRIDE; Q96LB4; -.
DR Ensembl; ENST00000281087; ENSP00000281087; ENSG00000151418.
DR Ensembl; ENST00000309309; ENSP00000309574; ENSG00000151418.
DR Ensembl; ENST00000367381; ENSP00000356351; ENSG00000151418.
DR Ensembl; ENST00000367382; ENSP00000356352; ENSG00000151418.
DR Ensembl; ENST00000489986; ENSP00000417171; ENSG00000151418.
DR Ensembl; ENST00000571439; ENSP00000461616; ENSG00000263014.
DR Ensembl; ENST00000573121; ENSP00000461329; ENSG00000263014.
DR Ensembl; ENST00000575971; ENSP00000461228; ENSG00000263014.
DR GeneID; 127124; -.
DR KEGG; hsa:127124; -.
DR UCSC; uc001gup.3; human.
DR CTD; 127124; -.
DR GeneCards; GC01M198492; -.
DR HGNC; HGNC:18265; ATP6V1G3.
DR HPA; HPA028701; -.
DR neXtProt; NX_Q96LB4; -.
DR PharmGKB; PA38515; -.
DR eggNOG; NOG235870; -.
DR HOGENOM; HOG000186416; -.
DR HOVERGEN; HBG057827; -.
DR KO; K02152; -.
DR OMA; HVNYRAT; -.
DR OrthoDB; EOG7MWH0X; -.
DR PhylomeDB; Q96LB4; -.
DR BioCyc; MetaCyc:HS07734-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GeneWiki; ATP6V1G3; -.
DR GenomeRNAi; 127124; -.
DR NextBio; 82029; -.
DR PRO; PR:Q96LB4; -.
DR Bgee; Q96LB4; -.
DR CleanEx; HS_ATP6V1G3; -.
DR Genevestigator; Q96LB4; -.
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; IEA:InterPro.
DR GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR InterPro; IPR005124; V-ATPase_G.
DR PANTHER; PTHR12713; PTHR12713; 1.
DR TIGRFAMs; TIGR01147; V_ATP_synt_G; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW Hydrogen ion transport; Ion transport; Polymorphism;
KW Reference proteome; Transport.
FT CHAIN 1 118 V-type proton ATPase subunit G 3.
FT /FTId=PRO_0000192904.
FT COILED 5 54 Potential.
FT VAR_SEQ 28 118 RKGKRLKQAKEEAMVEIDQYRMQRDKEFRLKQSKIMGSQNN
FT LSDEIEEQTLGKIQELNGHYNKYMESVMNQLLSMVCDMKPE
FT IHVNYRATN -> ILHLLFLKRRDWDCFWKRKAIEASQGGS
FT NGRN (in isoform 3).
FT /FTId=VSP_036423.
FT VAR_SEQ 28 28 R -> KTGTASG (in isoform 4).
FT /FTId=VSP_036426.
FT VARIANT 54 54 E -> Q (in dbSNP:rs16843254).
FT /FTId=VAR_048343.
SQ SEQUENCE 118 AA; 13917 MW; 651F8F5497164754 CRC64;
MTSQSQGIHQ LLQAEKRAKD KLEEAKKRKG KRLKQAKEEA MVEIDQYRMQ RDKEFRLKQS
KIMGSQNNLS DEIEEQTLGK IQELNGHYNK YMESVMNQLL SMVCDMKPEI HVNYRATN
//
ID VATG3_HUMAN Reviewed; 118 AA.
AC Q96LB4; Q495K2; Q495K4; Q5T9L6;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 97.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND
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
RT isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and
RT their evaluation in autosomal recessive distal renal tubular
RT 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of
CC vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying
CC a variety of intracellular compartments in eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (components A to H) attached to an
CC integral membrane V0 proton pore complex (components: a, c, c',
CC c'' and d) (By similarity).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Kidney.
CC -!- SIMILARITY: Belongs to the V-ATPase G subunit family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY039760; AAK83465.1; -; mRNA.
DR EMBL; AL157402; CAI15638.1; -; Genomic_DNA.
DR EMBL; BC101129; AAI01130.1; -; mRNA.
DR EMBL; BC101130; AAI01131.1; -; mRNA.
DR EMBL; BC101131; AAI01132.2; -; mRNA.
DR RefSeq; NP_573569.1; NM_133262.2.
DR RefSeq; NP_579872.1; NM_133326.1.
DR RefSeq; XP_005244949.1; XM_005244892.1.
DR RefSeq; XP_005276806.1; XM_005276749.1.
DR UniGene; Hs.127743; -.
DR ProteinModelPortal; Q96LB4; -.
DR SMR; Q96LB4; 3-81.
DR STRING; 9606.ENSP00000281087; -.
DR TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PhosphoSite; Q96LB4; -.
DR DMDM; 20140697; -.
DR PaxDb; Q96LB4; -.
DR PRIDE; Q96LB4; -.
DR Ensembl; ENST00000281087; ENSP00000281087; ENSG00000151418.
DR Ensembl; ENST00000309309; ENSP00000309574; ENSG00000151418.
DR Ensembl; ENST00000367381; ENSP00000356351; ENSG00000151418.
DR Ensembl; ENST00000367382; ENSP00000356352; ENSG00000151418.
DR Ensembl; ENST00000489986; ENSP00000417171; ENSG00000151418.
DR Ensembl; ENST00000571439; ENSP00000461616; ENSG00000263014.
DR Ensembl; ENST00000573121; ENSP00000461329; ENSG00000263014.
DR Ensembl; ENST00000575971; ENSP00000461228; ENSG00000263014.
DR GeneID; 127124; -.
DR KEGG; hsa:127124; -.
DR UCSC; uc001gup.3; human.
DR CTD; 127124; -.
DR GeneCards; GC01M198492; -.
DR HGNC; HGNC:18265; ATP6V1G3.
DR HPA; HPA028701; -.
DR neXtProt; NX_Q96LB4; -.
DR PharmGKB; PA38515; -.
DR eggNOG; NOG235870; -.
DR HOGENOM; HOG000186416; -.
DR HOVERGEN; HBG057827; -.
DR KO; K02152; -.
DR OMA; HVNYRAT; -.
DR OrthoDB; EOG7MWH0X; -.
DR PhylomeDB; Q96LB4; -.
DR BioCyc; MetaCyc:HS07734-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GeneWiki; ATP6V1G3; -.
DR GenomeRNAi; 127124; -.
DR NextBio; 82029; -.
DR PRO; PR:Q96LB4; -.
DR Bgee; Q96LB4; -.
DR CleanEx; HS_ATP6V1G3; -.
DR Genevestigator; Q96LB4; -.
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; IEA:InterPro.
DR GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0051701; P:interaction with host; TAS:Reactome.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR InterPro; IPR005124; V-ATPase_G.
DR PANTHER; PTHR12713; PTHR12713; 1.
DR TIGRFAMs; TIGR01147; V_ATP_synt_G; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Complete proteome;
KW Hydrogen ion transport; Ion transport; Polymorphism;
KW Reference proteome; Transport.
FT CHAIN 1 118 V-type proton ATPase subunit G 3.
FT /FTId=PRO_0000192904.
FT COILED 5 54 Potential.
FT VAR_SEQ 28 118 RKGKRLKQAKEEAMVEIDQYRMQRDKEFRLKQSKIMGSQNN
FT LSDEIEEQTLGKIQELNGHYNKYMESVMNQLLSMVCDMKPE
FT IHVNYRATN -> ILHLLFLKRRDWDCFWKRKAIEASQGGS
FT NGRN (in isoform 3).
FT /FTId=VSP_036423.
FT VAR_SEQ 28 28 R -> KTGTASG (in isoform 4).
FT /FTId=VSP_036426.
FT VARIANT 54 54 E -> Q (in dbSNP:rs16843254).
FT /FTId=VAR_048343.
SQ SEQUENCE 118 AA; 13917 MW; 651F8F5497164754 CRC64;
MTSQSQGIHQ LLQAEKRAKD KLEEAKKRKG KRLKQAKEEA MVEIDQYRMQ RDKEFRLKQS
KIMGSQNNLS DEIEEQTLGK IQELNGHYNK YMESVMNQLL SMVCDMKPEI HVNYRATN
//