Full text data of ATP6V0C
ATP6V0C
(ATP6C, ATP6L, ATPL)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
V-type proton ATPase 16 kDa proteolipid subunit; V-ATPase 16 kDa proteolipid subunit (Vacuolar proton pump 16 kDa proteolipid subunit)
V-type proton ATPase 16 kDa proteolipid subunit; V-ATPase 16 kDa proteolipid subunit (Vacuolar proton pump 16 kDa proteolipid subunit)
hRBCD
IPI00018855
IPI00018855 Vacuolar ATP synthase 16 kDa proteolipid subunit Vacuolar ATP synthase 16 kDa proteolipid subunit membrane n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00018855 Vacuolar ATP synthase 16 kDa proteolipid subunit Vacuolar ATP synthase 16 kDa proteolipid subunit membrane n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
P27449
ID VATL_HUMAN Reviewed; 155 AA.
AC P27449; Q6FH26;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1992, sequence version 1.
DT 22-JAN-2014, entry version 141.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit;
DE Short=V-ATPase 16 kDa proteolipid subunit;
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit;
GN Name=ATP6V0C; Synonyms=ATP6C, ATP6L, ATPL;
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].
RX PubMed=1709739; DOI=10.1073/pnas.88.10.4289;
RA Gillespie G.A.J., Somlo S., Germino G.G., Weinstat-Saslow D.,
RA Reeders S.T.;
RT "CpG island in the region of an autosomal dominant polycystic kidney
RT disease locus defines the 5' end of a gene encoding a putative proton
RT channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4289-4293(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Muscle, and Skin;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-155.
RX PubMed=1532310; DOI=10.1016/0006-291X(92)90562-Y;
RA Hasebe M., Hanada H., Moriyama Y., Maeda M., Futai M.;
RT "Vacuolar type H(+)-ATPase genes: presence of four genes including
RT pseudogenes for the 16-kDa proteolipid subunit in the human genome.";
RL Biochem. Biophys. Res. Commun. 183:856-863(1992).
RN [6]
RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I.
RX PubMed=7636472;
RA Koralnik I.J., Mulloy J.C., Andresson T., Fullen J., Franchini G.;
RT "Mapping of the intermolecular association of human T cell
RT leukaemia/lymphotropic virus type I p12I and the vacuolar H+-ATPase 16
RT kDa subunit protein.";
RL J. Gen. Virol. 76:1909-1916(1995).
RN [7]
RP INTERACTION WITH LASS2.
RX PubMed=11543633; DOI=10.1006/geno.2001.6614;
RA Pan H., Qin W.-X., Huo K.-K., Wan D.-F., Yu Y., Xu Z.-G., Hu Q.-D.,
RA Gu K.T., Zhou X.-M., Jiang H.-Q., Zhang P.-P., Huang Y., Li Y.-Y.,
RA Gu J.-R.;
RT "Cloning, mapping, and characterization of a human homologue of the
RT yeast longevity assurance gene LAG1.";
RL Genomics 77:58-64(2001).
RN [8]
RP INTERACTION WITH RNF182, AND UBIQUITINATION.
RX PubMed=18298843; DOI=10.1186/1750-1326-3-4;
RA Liu Q.Y., Lei J.X., Sikorska M., Liu R.;
RT "A novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in
RT the brains of Alzheimer's patients and targets ATP6V0C for
RT degradation.";
RL Mol. Neurodegener. 3:4-4(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Proton-conducting pore forming subunit of the membrane
CC integral V0 complex of vacuolar ATPase. V-ATPase is responsible
CC for acidifying a variety of intracellular compartments in
CC eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (main components: subunits A, B,
CC C, D, E, and F) attached to an integral membrane V0 proton pore
CC complex (main component: the proteolipid protein; which is present
CC as a hexamer that forms the proton-conducting pore). Interacts
CC with LASS2. Interacts with HTLV-1 accessory protein p12I.
CC Interacts with RNF182; this interaction leads to ubiquitination
CC and degradation via the proteasome pathway.
CC -!- INTERACTION:
CC Q96G23:CERS2; NbExp=3; IntAct=EBI-721179, EBI-1057080;
CC P0CK45:E5 (xeno); NbExp=2; IntAct=EBI-721179, EBI-7015490;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane
CC protein.
CC -!- PTM: Ubiquitinated by RNF182, leading to its degradation via the
CC ubiquitin-proteasome pathway.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid 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; M62762; AAA60039.1; -; mRNA.
DR EMBL; CR541930; CAG46728.1; -; mRNA.
DR EMBL; CR541951; CAG46749.1; -; mRNA.
DR EMBL; BT007155; AAP35819.1; -; mRNA.
DR EMBL; BC004537; AAH04537.1; -; mRNA.
DR EMBL; BC007389; AAH07389.1; -; mRNA.
DR EMBL; BC007759; AAH07759.1; -; mRNA.
DR EMBL; BC009290; AAH09290.1; -; mRNA.
DR PIR; A39367; A39367.
DR RefSeq; NP_001185498.1; NM_001198569.1.
DR RefSeq; NP_001685.1; NM_001694.3.
DR UniGene; Hs.389107; -.
DR ProteinModelPortal; P27449; -.
DR SMR; P27449; 14-153.
DR IntAct; P27449; 6.
DR MINT; MINT-1414327; -.
DR STRING; 9606.ENSP00000329757; -.
DR PhosphoSite; P27449; -.
DR DMDM; 137479; -.
DR PaxDb; P27449; -.
DR PRIDE; P27449; -.
DR DNASU; 527; -.
DR Ensembl; ENST00000330398; ENSP00000329757; ENSG00000185883.
DR GeneID; 527; -.
DR KEGG; hsa:527; -.
DR UCSC; uc002cqn.3; human.
DR CTD; 527; -.
DR GeneCards; GC16P002563; -.
DR HGNC; HGNC:855; ATP6V0C.
DR MIM; 108745; gene.
DR neXtProt; NX_P27449; -.
DR PharmGKB; PA25149; -.
DR eggNOG; COG0636; -.
DR HOGENOM; HOG000056520; -.
DR HOVERGEN; HBG002712; -.
DR InParanoid; P27449; -.
DR KO; K02155; -.
DR OMA; GVMKPDL; -.
DR OrthoDB; EOG7FV3RW; -.
DR PhylomeDB; P27449; -.
DR BioCyc; MetaCyc:MONOMER66-34368; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GeneWiki; ATP6V0C; -.
DR GenomeRNAi; 527; -.
DR NextBio; 2187; -.
DR PRO; PR:P27449; -.
DR ArrayExpress; P27449; -.
DR Bgee; P27449; -.
DR CleanEx; HS_ATP6V0C; -.
DR Genevestigator; P27449; -.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; TAS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; TAS:ProtInc.
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:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR InterPro; IPR002379; ATPase_proteolipid_c_like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Host-virus interaction; Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Vacuole.
FT CHAIN 1 155 V-type proton ATPase 16 kDa proteolipid
FT subunit.
FT /FTId=PRO_0000071743.
FT TOPO_DOM 1 10 Lumenal (Potential).
FT TRANSMEM 11 33 Helical; (Potential).
FT TOPO_DOM 34 55 Cytoplasmic (Potential).
FT TRANSMEM 56 76 Helical; (Potential).
FT TOPO_DOM 77 92 Lumenal (Potential).
FT TRANSMEM 93 114 Helical; (Potential).
FT TOPO_DOM 115 131 Cytoplasmic (Potential).
FT TRANSMEM 132 152 Helical; (Potential).
FT TOPO_DOM 153 155 Lumenal (Potential).
FT SITE 139 139 Essential for proton translocation (By
FT similarity).
SQ SEQUENCE 155 AA; 15736 MW; 91141854A0492A5B CRC64;
MSESKSGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE QIMKSIIPVV
MAGIIAIYGL VVAVLIANSL NDDISLYKSF LQLGAGLSVG LSGLAAGFAI GIVGDAGVRG
TAQQPRLFVG MILILIFAEV LGLYGLIVAL ILSTK
//
ID VATL_HUMAN Reviewed; 155 AA.
AC P27449; Q6FH26;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1992, sequence version 1.
DT 22-JAN-2014, entry version 141.
DE RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit;
DE Short=V-ATPase 16 kDa proteolipid subunit;
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit;
GN Name=ATP6V0C; Synonyms=ATP6C, ATP6L, ATPL;
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].
RX PubMed=1709739; DOI=10.1073/pnas.88.10.4289;
RA Gillespie G.A.J., Somlo S., Germino G.G., Weinstat-Saslow D.,
RA Reeders S.T.;
RT "CpG island in the region of an autosomal dominant polycystic kidney
RT disease locus defines the 5' end of a gene encoding a putative proton
RT channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4289-4293(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Muscle, and Skin;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-155.
RX PubMed=1532310; DOI=10.1016/0006-291X(92)90562-Y;
RA Hasebe M., Hanada H., Moriyama Y., Maeda M., Futai M.;
RT "Vacuolar type H(+)-ATPase genes: presence of four genes including
RT pseudogenes for the 16-kDa proteolipid subunit in the human genome.";
RL Biochem. Biophys. Res. Commun. 183:856-863(1992).
RN [6]
RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I.
RX PubMed=7636472;
RA Koralnik I.J., Mulloy J.C., Andresson T., Fullen J., Franchini G.;
RT "Mapping of the intermolecular association of human T cell
RT leukaemia/lymphotropic virus type I p12I and the vacuolar H+-ATPase 16
RT kDa subunit protein.";
RL J. Gen. Virol. 76:1909-1916(1995).
RN [7]
RP INTERACTION WITH LASS2.
RX PubMed=11543633; DOI=10.1006/geno.2001.6614;
RA Pan H., Qin W.-X., Huo K.-K., Wan D.-F., Yu Y., Xu Z.-G., Hu Q.-D.,
RA Gu K.T., Zhou X.-M., Jiang H.-Q., Zhang P.-P., Huang Y., Li Y.-Y.,
RA Gu J.-R.;
RT "Cloning, mapping, and characterization of a human homologue of the
RT yeast longevity assurance gene LAG1.";
RL Genomics 77:58-64(2001).
RN [8]
RP INTERACTION WITH RNF182, AND UBIQUITINATION.
RX PubMed=18298843; DOI=10.1186/1750-1326-3-4;
RA Liu Q.Y., Lei J.X., Sikorska M., Liu R.;
RT "A novel brain-enriched E3 ubiquitin ligase RNF182 is up regulated in
RT the brains of Alzheimer's patients and targets ATP6V0C for
RT degradation.";
RL Mol. Neurodegener. 3:4-4(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Proton-conducting pore forming subunit of the membrane
CC integral V0 complex of vacuolar ATPase. V-ATPase is responsible
CC for acidifying a variety of intracellular compartments in
CC eukaryotic cells.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a
CC peripheral catalytic V1 complex (main components: subunits A, B,
CC C, D, E, and F) attached to an integral membrane V0 proton pore
CC complex (main component: the proteolipid protein; which is present
CC as a hexamer that forms the proton-conducting pore). Interacts
CC with LASS2. Interacts with HTLV-1 accessory protein p12I.
CC Interacts with RNF182; this interaction leads to ubiquitination
CC and degradation via the proteasome pathway.
CC -!- INTERACTION:
CC Q96G23:CERS2; NbExp=3; IntAct=EBI-721179, EBI-1057080;
CC P0CK45:E5 (xeno); NbExp=2; IntAct=EBI-721179, EBI-7015490;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane
CC protein.
CC -!- PTM: Ubiquitinated by RNF182, leading to its degradation via the
CC ubiquitin-proteasome pathway.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid 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; M62762; AAA60039.1; -; mRNA.
DR EMBL; CR541930; CAG46728.1; -; mRNA.
DR EMBL; CR541951; CAG46749.1; -; mRNA.
DR EMBL; BT007155; AAP35819.1; -; mRNA.
DR EMBL; BC004537; AAH04537.1; -; mRNA.
DR EMBL; BC007389; AAH07389.1; -; mRNA.
DR EMBL; BC007759; AAH07759.1; -; mRNA.
DR EMBL; BC009290; AAH09290.1; -; mRNA.
DR PIR; A39367; A39367.
DR RefSeq; NP_001185498.1; NM_001198569.1.
DR RefSeq; NP_001685.1; NM_001694.3.
DR UniGene; Hs.389107; -.
DR ProteinModelPortal; P27449; -.
DR SMR; P27449; 14-153.
DR IntAct; P27449; 6.
DR MINT; MINT-1414327; -.
DR STRING; 9606.ENSP00000329757; -.
DR PhosphoSite; P27449; -.
DR DMDM; 137479; -.
DR PaxDb; P27449; -.
DR PRIDE; P27449; -.
DR DNASU; 527; -.
DR Ensembl; ENST00000330398; ENSP00000329757; ENSG00000185883.
DR GeneID; 527; -.
DR KEGG; hsa:527; -.
DR UCSC; uc002cqn.3; human.
DR CTD; 527; -.
DR GeneCards; GC16P002563; -.
DR HGNC; HGNC:855; ATP6V0C.
DR MIM; 108745; gene.
DR neXtProt; NX_P27449; -.
DR PharmGKB; PA25149; -.
DR eggNOG; COG0636; -.
DR HOGENOM; HOG000056520; -.
DR HOVERGEN; HBG002712; -.
DR InParanoid; P27449; -.
DR KO; K02155; -.
DR OMA; GVMKPDL; -.
DR OrthoDB; EOG7FV3RW; -.
DR PhylomeDB; P27449; -.
DR BioCyc; MetaCyc:MONOMER66-34368; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR GeneWiki; ATP6V0C; -.
DR GenomeRNAi; 527; -.
DR NextBio; 2187; -.
DR PRO; PR:P27449; -.
DR ArrayExpress; P27449; -.
DR Bgee; P27449; -.
DR CleanEx; HS_ATP6V0C; -.
DR Genevestigator; P27449; -.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; TAS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; TAS:ProtInc.
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:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0090382; P:phagosome maturation; TAS:Reactome.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR InterPro; IPR002379; ATPase_proteolipid_c_like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Host-virus interaction; Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Vacuole.
FT CHAIN 1 155 V-type proton ATPase 16 kDa proteolipid
FT subunit.
FT /FTId=PRO_0000071743.
FT TOPO_DOM 1 10 Lumenal (Potential).
FT TRANSMEM 11 33 Helical; (Potential).
FT TOPO_DOM 34 55 Cytoplasmic (Potential).
FT TRANSMEM 56 76 Helical; (Potential).
FT TOPO_DOM 77 92 Lumenal (Potential).
FT TRANSMEM 93 114 Helical; (Potential).
FT TOPO_DOM 115 131 Cytoplasmic (Potential).
FT TRANSMEM 132 152 Helical; (Potential).
FT TOPO_DOM 153 155 Lumenal (Potential).
FT SITE 139 139 Essential for proton translocation (By
FT similarity).
SQ SEQUENCE 155 AA; 15736 MW; 91141854A0492A5B CRC64;
MSESKSGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE QIMKSIIPVV
MAGIIAIYGL VVAVLIANSL NDDISLYKSF LQLGAGLSVG LSGLAAGFAI GIVGDAGVRG
TAQQPRLFVG MILILIFAEV LGLYGLIVAL ILSTK
//
MIM
108745
*RECORD*
*FIELD* NO
108745
*FIELD* TI
*108745 ATPase, H+ TRANSPORTING, LYSOSOMAL, 16-KD, V0 SUBUNIT C; ATP6V0C
;;ATPase, H+ TRANSPORTING, LYSOSOMAL; ATP6L;;
read moreVACUOLAR PROTON PUMP, SUBUNIT C; VPPC
*FIELD* TX
CLONING
In an attempt to isolate candidate genes for autosomal dominant
polycystic kidney disease (PKD1; 173900), Gillespie et al. (1991)
identified a number of CpG-rich islands from the PKD1 critical region on
16p13.3. Genomic fragments adjacent to 1 of these islands were used to
isolate cDNAs from both HeLa cells and cultured cystic epithelium that
encode a 155-amino acid peptide having 4 putative transmembrane domains.
The corresponding transcript was found in all tissues tested but was
most abundant in brain and kidney. The deduced amino acid sequence had
93% similarity to the 16-kD proteolipid component that is believed to be
part of the proton channel of the vacuolar H(+)-ATPase. A mutated proton
channel might be implicated in the pathogenesis of cystic disease.
However, sequencing of cDNAs corresponding to both alleles of an
affected person revealed no differences in the deduced amino acid
sequence. Moreover, transcript size and abundance were not altered in
cystic kidney.
GENE FUNCTION
Using a bacterial 2-hybrid assay, Sun et al. (2004) showed that the rat
bile acid transporter Asbt (SLC10A2; 601295) interacted with mouse Vppc.
The interaction was confirmed by in vitro pull-down assays and mammalian
2-hybrid analysis. Immunofluorescence confocal microscopy demonstrated
that Asbt and Vppc colocalized in transfected COS-7 and MDCK canine
kidney cells. Pharmacologic blockade of the vacuolar proton pump
abrogated the apical localization of Asbt and colocalization of Asbt and
Vppc, and it significantly decreased cellular uptake of the bile acid
taurocholate. Sun et al. (2004) concluded that VPPC contributes to the
apical membrane localization of ASBT.
MAPPING
By genomic sequence analysis, Gillespie et al. (1991) mapped the ATP6V0C
gene to chromosome 16p13.3. Simckes et al. (2002) mapped the mouse
Atp6v0c gene to chromosome 17, where it is closely linked to the TSC2
gene (191092).
*FIELD* RF
1. Gillespie, G. A. J.; Somlo, S.; Germino, G. G.; Weinstat-Saslow,
D.; Reeders, S. T.: CpG island in the region of an autosomal dominant
polycystic kidney disease locus defines the 5-prime end of a gene
encoding a putative proton channel. Proc. Nat. Acad. Sci. 88: 4289-4293,
1991.
2. Simckes, A. M.; Swanson, S. K.; White, R. A.: Chromosomal localization
of three vacuolar-H(+)-ATPase 16 kDa subunit (ATP6V0C) genes in the
murine genome. Cytogenet. Genome Res. 97: 111-115, 2002.
3. Sun, A.-Q.; Balasubramaniyan, N.; Liu, C.-J.; Shahid, M.; Suchy,
F. J.: Association of the 16-kDa subunit c of vacuolar proton pump
with the ileal Na(+)-dependent bile acid transporter: protein-protein
interaction and intracellular trafficking. J. Biol. Chem. 279: 16295-16300,
2004.
*FIELD* CN
Patricia A. Hartz - updated: 3/12/2010
Patricia A. Hartz - updated: 2/10/2003
*FIELD* CD
Victor A. McKusick: 12/22/1993
*FIELD* ED
carol: 07/26/2013
mgross: 3/15/2010
terry: 3/12/2010
alopez: 3/8/2010
terry: 3/5/2010
mgross: 2/10/2003
terry: 2/10/2003
carol: 12/26/2000
psherman: 10/9/1998
psherman: 10/8/1998
carol: 12/22/1993
*RECORD*
*FIELD* NO
108745
*FIELD* TI
*108745 ATPase, H+ TRANSPORTING, LYSOSOMAL, 16-KD, V0 SUBUNIT C; ATP6V0C
;;ATPase, H+ TRANSPORTING, LYSOSOMAL; ATP6L;;
read moreVACUOLAR PROTON PUMP, SUBUNIT C; VPPC
*FIELD* TX
CLONING
In an attempt to isolate candidate genes for autosomal dominant
polycystic kidney disease (PKD1; 173900), Gillespie et al. (1991)
identified a number of CpG-rich islands from the PKD1 critical region on
16p13.3. Genomic fragments adjacent to 1 of these islands were used to
isolate cDNAs from both HeLa cells and cultured cystic epithelium that
encode a 155-amino acid peptide having 4 putative transmembrane domains.
The corresponding transcript was found in all tissues tested but was
most abundant in brain and kidney. The deduced amino acid sequence had
93% similarity to the 16-kD proteolipid component that is believed to be
part of the proton channel of the vacuolar H(+)-ATPase. A mutated proton
channel might be implicated in the pathogenesis of cystic disease.
However, sequencing of cDNAs corresponding to both alleles of an
affected person revealed no differences in the deduced amino acid
sequence. Moreover, transcript size and abundance were not altered in
cystic kidney.
GENE FUNCTION
Using a bacterial 2-hybrid assay, Sun et al. (2004) showed that the rat
bile acid transporter Asbt (SLC10A2; 601295) interacted with mouse Vppc.
The interaction was confirmed by in vitro pull-down assays and mammalian
2-hybrid analysis. Immunofluorescence confocal microscopy demonstrated
that Asbt and Vppc colocalized in transfected COS-7 and MDCK canine
kidney cells. Pharmacologic blockade of the vacuolar proton pump
abrogated the apical localization of Asbt and colocalization of Asbt and
Vppc, and it significantly decreased cellular uptake of the bile acid
taurocholate. Sun et al. (2004) concluded that VPPC contributes to the
apical membrane localization of ASBT.
MAPPING
By genomic sequence analysis, Gillespie et al. (1991) mapped the ATP6V0C
gene to chromosome 16p13.3. Simckes et al. (2002) mapped the mouse
Atp6v0c gene to chromosome 17, where it is closely linked to the TSC2
gene (191092).
*FIELD* RF
1. Gillespie, G. A. J.; Somlo, S.; Germino, G. G.; Weinstat-Saslow,
D.; Reeders, S. T.: CpG island in the region of an autosomal dominant
polycystic kidney disease locus defines the 5-prime end of a gene
encoding a putative proton channel. Proc. Nat. Acad. Sci. 88: 4289-4293,
1991.
2. Simckes, A. M.; Swanson, S. K.; White, R. A.: Chromosomal localization
of three vacuolar-H(+)-ATPase 16 kDa subunit (ATP6V0C) genes in the
murine genome. Cytogenet. Genome Res. 97: 111-115, 2002.
3. Sun, A.-Q.; Balasubramaniyan, N.; Liu, C.-J.; Shahid, M.; Suchy,
F. J.: Association of the 16-kDa subunit c of vacuolar proton pump
with the ileal Na(+)-dependent bile acid transporter: protein-protein
interaction and intracellular trafficking. J. Biol. Chem. 279: 16295-16300,
2004.
*FIELD* CN
Patricia A. Hartz - updated: 3/12/2010
Patricia A. Hartz - updated: 2/10/2003
*FIELD* CD
Victor A. McKusick: 12/22/1993
*FIELD* ED
carol: 07/26/2013
mgross: 3/15/2010
terry: 3/12/2010
alopez: 3/8/2010
terry: 3/5/2010
mgross: 2/10/2003
terry: 2/10/2003
carol: 12/26/2000
psherman: 10/9/1998
psherman: 10/8/1998
carol: 12/22/1993