Full text data of ATP6V1C2
ATP6V1C2
[Confidence: low (only semi-automatic identification from reviews)]
V-type proton ATPase subunit C 2; V-ATPase subunit C 2 (Vacuolar proton pump subunit C 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
V-type proton ATPase subunit C 2; V-ATPase subunit C 2 (Vacuolar proton pump subunit C 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8NEY4
ID VATC2_HUMAN Reviewed; 427 AA.
AC Q8NEY4; Q96EL8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2007, sequence version 2.
DT 22-JAN-2014, entry version 89.
DE RecName: Full=V-type proton ATPase subunit C 2;
DE Short=V-ATPase subunit C 2;
DE AltName: Full=Vacuolar proton pump subunit C 2;
GN Name=ATP6V1C2;
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 2), 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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP ASP-143.
RC TISSUE=Eye;
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: Subunit of the peripheral V1 complex of vacuolar ATPase.
CC Subunit C is necessary for the assembly of the catalytic sector of
CC the enzyme and is likely to have a specific function in its
CC catalytic activity. V-ATPase is responsible for acidifying a
CC 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).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NEY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NEY4-2; Sequence=VSP_024883;
CC -!- TISSUE SPECIFICITY: Kidney and placenta.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY24069.1; Type=Erroneous gene model prediction;
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; AY039759; AAK83464.1; -; mRNA.
DR EMBL; AC092687; AAY24069.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC012142; AAH12142.1; -; mRNA.
DR RefSeq; NP_001034451.1; NM_001039362.1.
DR RefSeq; NP_653184.2; NM_144583.3.
DR UniGene; Hs.580464; -.
DR ProteinModelPortal; Q8NEY4; -.
DR SMR; Q8NEY4; 7-383.
DR IntAct; Q8NEY4; 2.
DR STRING; 9606.ENSP00000272238; -.
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; Q8NEY4; -.
DR DMDM; 146325814; -.
DR PaxDb; Q8NEY4; -.
DR PRIDE; Q8NEY4; -.
DR DNASU; 245973; -.
DR Ensembl; ENST00000272238; ENSP00000272238; ENSG00000143882.
DR Ensembl; ENST00000381661; ENSP00000371077; ENSG00000143882.
DR GeneID; 245973; -.
DR KEGG; hsa:245973; -.
DR UCSC; uc002ras.3; human.
DR CTD; 245973; -.
DR GeneCards; GC02P010861; -.
DR HGNC; HGNC:18264; ATP6V1C2.
DR HPA; HPA034735; -.
DR neXtProt; NX_Q8NEY4; -.
DR PharmGKB; PA38514; -.
DR eggNOG; COG5127; -.
DR HOGENOM; HOG000207528; -.
DR HOVERGEN; HBG002470; -.
DR InParanoid; Q8NEY4; -.
DR KO; K02148; -.
DR OMA; TRFEWDM; -.
DR OrthoDB; EOG7QNVKX; -.
DR BioCyc; MetaCyc:HS07123-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP6V1C2; human.
DR GeneWiki; ATP6V1C2; -.
DR GenomeRNAi; 245973; -.
DR NextBio; 91835; -.
DR PRO; PR:Q8NEY4; -.
DR Bgee; Q8NEY4; -.
DR CleanEx; HS_ATP6V1C2; -.
DR Genevestigator; Q8NEY4; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:Ensembl.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
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; IPR004907; ATPase_V1-cplx_csu.
DR PANTHER; PTHR10137; PTHR10137; 1.
DR Pfam; PF03223; V-ATPase_C; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Hydrogen ion transport;
KW Ion transport; Polymorphism; Reference proteome; Transport.
FT CHAIN 1 427 V-type proton ATPase subunit C 2.
FT /FTId=PRO_0000285669.
FT VAR_SEQ 276 321 Missing (in isoform 2).
FT /FTId=VSP_024883.
FT VARIANT 143 143 N -> D (in dbSNP:rs1198849).
FT /FTId=VAR_032041.
SQ SEQUENCE 427 AA; 48759 MW; 7ED699EDD49CBC96 CRC64;
MSEFWLISAP GDKENLQALE RMNTVTSKSN LSYNTKFAIP DFKVGTLDSL VGLSDELGKL
DTFAESLIRR MAQSVVEVME DSKGKVQEHL LANGVDLTSF VTHFEWDMAK YPVKQPLVSV
VDTIAKQLAQ IEMDLKSRTA AYNTLKTNLE NLEKKSMGNL FTRTLSDIVS KEDFVLDSEY
LVTLLVIVPK PNYSQWQKTY ESLSDMVVPR STKLITEDKE GGLFTVTLFR KVIEDFKTKA
KENKFTVREF YYDEKEIERE REEMARLLSD KKQQYQTSCV ALKKGSSTFP DHKVKVTPLG
NPDRPAAGQT DRERESEGEG EGPLLRWLKV NFSEAFIAWI HIKALRVFVE SVLRYGLPVN
FQAVLLQPHK KSSTKRLREV LNSVFRHLDE VAATSILDAS VEIPGLQLNN QDYFPYVYFH
IDLSLLD
//
ID VATC2_HUMAN Reviewed; 427 AA.
AC Q8NEY4; Q96EL8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2007, sequence version 2.
DT 22-JAN-2014, entry version 89.
DE RecName: Full=V-type proton ATPase subunit C 2;
DE Short=V-ATPase subunit C 2;
DE AltName: Full=Vacuolar proton pump subunit C 2;
GN Name=ATP6V1C2;
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 2), 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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP ASP-143.
RC TISSUE=Eye;
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: Subunit of the peripheral V1 complex of vacuolar ATPase.
CC Subunit C is necessary for the assembly of the catalytic sector of
CC the enzyme and is likely to have a specific function in its
CC catalytic activity. V-ATPase is responsible for acidifying a
CC 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).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NEY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NEY4-2; Sequence=VSP_024883;
CC -!- TISSUE SPECIFICITY: Kidney and placenta.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY24069.1; Type=Erroneous gene model prediction;
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; AY039759; AAK83464.1; -; mRNA.
DR EMBL; AC092687; AAY24069.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC012142; AAH12142.1; -; mRNA.
DR RefSeq; NP_001034451.1; NM_001039362.1.
DR RefSeq; NP_653184.2; NM_144583.3.
DR UniGene; Hs.580464; -.
DR ProteinModelPortal; Q8NEY4; -.
DR SMR; Q8NEY4; 7-383.
DR IntAct; Q8NEY4; 2.
DR STRING; 9606.ENSP00000272238; -.
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; Q8NEY4; -.
DR DMDM; 146325814; -.
DR PaxDb; Q8NEY4; -.
DR PRIDE; Q8NEY4; -.
DR DNASU; 245973; -.
DR Ensembl; ENST00000272238; ENSP00000272238; ENSG00000143882.
DR Ensembl; ENST00000381661; ENSP00000371077; ENSG00000143882.
DR GeneID; 245973; -.
DR KEGG; hsa:245973; -.
DR UCSC; uc002ras.3; human.
DR CTD; 245973; -.
DR GeneCards; GC02P010861; -.
DR HGNC; HGNC:18264; ATP6V1C2.
DR HPA; HPA034735; -.
DR neXtProt; NX_Q8NEY4; -.
DR PharmGKB; PA38514; -.
DR eggNOG; COG5127; -.
DR HOGENOM; HOG000207528; -.
DR HOVERGEN; HBG002470; -.
DR InParanoid; Q8NEY4; -.
DR KO; K02148; -.
DR OMA; TRFEWDM; -.
DR OrthoDB; EOG7QNVKX; -.
DR BioCyc; MetaCyc:HS07123-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; ATP6V1C2; human.
DR GeneWiki; ATP6V1C2; -.
DR GenomeRNAi; 245973; -.
DR NextBio; 91835; -.
DR PRO; PR:Q8NEY4; -.
DR Bgee; Q8NEY4; -.
DR CleanEx; HS_ATP6V1C2; -.
DR Genevestigator; Q8NEY4; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:Ensembl.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
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; IPR004907; ATPase_V1-cplx_csu.
DR PANTHER; PTHR10137; PTHR10137; 1.
DR Pfam; PF03223; V-ATPase_C; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Hydrogen ion transport;
KW Ion transport; Polymorphism; Reference proteome; Transport.
FT CHAIN 1 427 V-type proton ATPase subunit C 2.
FT /FTId=PRO_0000285669.
FT VAR_SEQ 276 321 Missing (in isoform 2).
FT /FTId=VSP_024883.
FT VARIANT 143 143 N -> D (in dbSNP:rs1198849).
FT /FTId=VAR_032041.
SQ SEQUENCE 427 AA; 48759 MW; 7ED699EDD49CBC96 CRC64;
MSEFWLISAP GDKENLQALE RMNTVTSKSN LSYNTKFAIP DFKVGTLDSL VGLSDELGKL
DTFAESLIRR MAQSVVEVME DSKGKVQEHL LANGVDLTSF VTHFEWDMAK YPVKQPLVSV
VDTIAKQLAQ IEMDLKSRTA AYNTLKTNLE NLEKKSMGNL FTRTLSDIVS KEDFVLDSEY
LVTLLVIVPK PNYSQWQKTY ESLSDMVVPR STKLITEDKE GGLFTVTLFR KVIEDFKTKA
KENKFTVREF YYDEKEIERE REEMARLLSD KKQQYQTSCV ALKKGSSTFP DHKVKVTPLG
NPDRPAAGQT DRERESEGEG EGPLLRWLKV NFSEAFIAWI HIKALRVFVE SVLRYGLPVN
FQAVLLQPHK KSSTKRLREV LNSVFRHLDE VAATSILDAS VEIPGLQLNN QDYFPYVYFH
IDLSLLD
//