Full text data of ATP6V0D1
ATP6V0D1
(ATP6D, VPATPD)
[Confidence: high (present in two of the MS resources)]
V-type proton ATPase subunit d 1; V-ATPase subunit d 1 (32 kDa accessory protein; V-ATPase 40 kDa accessory protein; V-ATPase AC39 subunit; p39; Vacuolar proton pump subunit d 1)
V-type proton ATPase subunit d 1; V-ATPase subunit d 1 (32 kDa accessory protein; V-ATPase 40 kDa accessory protein; V-ATPase AC39 subunit; p39; Vacuolar proton pump subunit d 1)
hRBCD
IPI00034159
IPI00034159 Vacuolar ATP synthase subunit d Subunit of the integral membrane V0 complex of vacuolar ATPase, hydrogen-translocating V-type ATPase complex, proton transport soluble 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 n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00034159 Vacuolar ATP synthase subunit d Subunit of the integral membrane V0 complex of vacuolar ATPase, hydrogen-translocating V-type ATPase complex, proton transport soluble 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 n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
P61421
ID VA0D1_HUMAN Reviewed; 351 AA.
AC P61421; P12953; Q02547;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=V-type proton ATPase subunit d 1;
DE Short=V-ATPase subunit d 1;
DE AltName: Full=32 kDa accessory protein;
DE AltName: Full=V-ATPase 40 kDa accessory protein;
DE AltName: Full=V-ATPase AC39 subunit;
DE Short=p39;
DE AltName: Full=Vacuolar proton pump subunit d 1;
GN Name=ATP6V0D1; Synonyms=ATP6D, VPATPD;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Osteoclastoma;
RX PubMed=8250920; DOI=10.1006/bbrc.1993.2434;
RA van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.;
RT "Cloning and tissue distribution of subunits C, D, and E of the human
RT vacuolar H(+)-ATPase.";
RL Biochem. Biophys. Res. Commun. 197:15-21(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11118322; DOI=10.1006/bbrc.2000.4003;
RA Agarwal A.K., White P.C.;
RT "Structure of the VPATPD gene encoding subunit D of the human vacuolar
RT proton ATPase.";
RL Biochem. Biophys. Res. Commun. 279:543-547(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 264-351.
RA Bhat K.S.;
RT "Expressed sequence tags from a human cell line.";
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21844891; DOI=10.1038/cr.2011.134;
RA Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S.,
RA Lin S., Shu X., Pei D.;
RT "A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in
RT vivo.";
RL Cell Res. 22:333-345(2012).
CC -!- FUNCTION: Subunit of the integral membrane V0 complex of vacuolar
CC ATPase. Vacuolar ATPase is responsible for acidifying a variety of
CC intracellular compartments in eukaryotic cells, thus providing
CC most of the energy required for transport processes in the
CC vacuolar system. May play a role in coupling of proton transport
CC and ATP hydrolysis (By similarity). May play a role in cilium
CC biogenesis through regulation of the transport and the
CC localization of proteins to the cilium (By similarity).
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 -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein;
CC Cytoplasmic side (Probable). Note=Localizes to centrosome and the
CC base of the cilium.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA50591.1; Type=Frameshift; Positions=22, 25, 64, 66;
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; X71490; CAA50591.1; ALT_FRAME; mRNA.
DR EMBL; BC008861; AAH08861.1; -; mRNA.
DR EMBL; L05087; AAC15852.1; -; mRNA.
DR RefSeq; NP_004682.2; NM_004691.4.
DR UniGene; Hs.106876; -.
DR ProteinModelPortal; P61421; -.
DR SMR; P61421; 28-55.
DR IntAct; P61421; 2.
DR MINT; MINT-5006032; -.
DR STRING; 9606.ENSP00000290949; -.
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; P61421; -.
DR DMDM; 47606646; -.
DR PaxDb; P61421; -.
DR PeptideAtlas; P61421; -.
DR PRIDE; P61421; -.
DR DNASU; 9114; -.
DR Ensembl; ENST00000290949; ENSP00000290949; ENSG00000159720.
DR GeneID; 9114; -.
DR KEGG; hsa:9114; -.
DR UCSC; uc002ete.1; human.
DR CTD; 9114; -.
DR GeneCards; GC16M067471; -.
DR HGNC; HGNC:13724; ATP6V0D1.
DR HPA; HPA016938; -.
DR MIM; 607028; gene.
DR neXtProt; NX_P61421; -.
DR PharmGKB; PA25150; -.
DR eggNOG; COG1527; -.
DR HOGENOM; HOG000199065; -.
DR HOVERGEN; HBG018065; -.
DR InParanoid; P61421; -.
DR KO; K02146; -.
DR OrthoDB; EOG7KH9JT; -.
DR PhylomeDB; P61421; -.
DR BioCyc; MetaCyc:HS08417-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; ATP6V0D1; human.
DR GeneWiki; ATP6V0D1; -.
DR GenomeRNAi; 9114; -.
DR NextBio; 34161; -.
DR PRO; PR:P61421; -.
DR ArrayExpress; P61421; -.
DR Bgee; P61421; -.
DR CleanEx; HS_ATP6V0D1; -.
DR Genevestigator; P61421; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
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:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IDA:UniProtKB.
DR GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:Ensembl.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0042384; P:cilium assembly; ISS:UniProtKB.
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:0015992; P:proton transport; NAS:UniProtKB.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR PANTHER; PTHR11028; PTHR11028; 1.
DR Pfam; PF01992; vATP-synt_AC39; 1.
DR PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR SUPFAM; SSF103486; SSF103486; 1.
PE 1: Evidence at protein level;
KW Cilium biogenesis/degradation; Complete proteome;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1 351 V-type proton ATPase subunit d 1.
FT /FTId=PRO_0000119350.
FT MOD_RES 270 270 Phosphotyrosine (By similarity).
FT CONFLICT 27 27 V -> E (in Ref. 1; CAA50591).
FT CONFLICT 266 267 NV -> KL (in Ref. 1; CAA50591).
SQ SEQUENCE 351 AA; 40329 MW; A720F8A87511203C CRC64;
MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN
EASPLTVSVI DDRLKEKMVV EFRHMRNHAY EPLASFLDFI TYSYMIDNVI LLITGTLHQR
SIAELVPKCH PLGSFEQMEA VNIAQTPAEL YNAILVDTPL AAFFQDCISE QDLDEMNIEI
IRNTLYKAYL ESFYKFCTLL GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL
FPHCGRLYPE GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK
LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI F
//
ID VA0D1_HUMAN Reviewed; 351 AA.
AC P61421; P12953; Q02547;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=V-type proton ATPase subunit d 1;
DE Short=V-ATPase subunit d 1;
DE AltName: Full=32 kDa accessory protein;
DE AltName: Full=V-ATPase 40 kDa accessory protein;
DE AltName: Full=V-ATPase AC39 subunit;
DE Short=p39;
DE AltName: Full=Vacuolar proton pump subunit d 1;
GN Name=ATP6V0D1; Synonyms=ATP6D, VPATPD;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Osteoclastoma;
RX PubMed=8250920; DOI=10.1006/bbrc.1993.2434;
RA van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.;
RT "Cloning and tissue distribution of subunits C, D, and E of the human
RT vacuolar H(+)-ATPase.";
RL Biochem. Biophys. Res. Commun. 197:15-21(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11118322; DOI=10.1006/bbrc.2000.4003;
RA Agarwal A.K., White P.C.;
RT "Structure of the VPATPD gene encoding subunit D of the human vacuolar
RT proton ATPase.";
RL Biochem. Biophys. Res. Commun. 279:543-547(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 264-351.
RA Bhat K.S.;
RT "Expressed sequence tags from a human cell line.";
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21844891; DOI=10.1038/cr.2011.134;
RA Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S.,
RA Lin S., Shu X., Pei D.;
RT "A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in
RT vivo.";
RL Cell Res. 22:333-345(2012).
CC -!- FUNCTION: Subunit of the integral membrane V0 complex of vacuolar
CC ATPase. Vacuolar ATPase is responsible for acidifying a variety of
CC intracellular compartments in eukaryotic cells, thus providing
CC most of the energy required for transport processes in the
CC vacuolar system. May play a role in coupling of proton transport
CC and ATP hydrolysis (By similarity). May play a role in cilium
CC biogenesis through regulation of the transport and the
CC localization of proteins to the cilium (By similarity).
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 -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein;
CC Cytoplasmic side (Probable). Note=Localizes to centrosome and the
CC base of the cilium.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA50591.1; Type=Frameshift; Positions=22, 25, 64, 66;
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; X71490; CAA50591.1; ALT_FRAME; mRNA.
DR EMBL; BC008861; AAH08861.1; -; mRNA.
DR EMBL; L05087; AAC15852.1; -; mRNA.
DR RefSeq; NP_004682.2; NM_004691.4.
DR UniGene; Hs.106876; -.
DR ProteinModelPortal; P61421; -.
DR SMR; P61421; 28-55.
DR IntAct; P61421; 2.
DR MINT; MINT-5006032; -.
DR STRING; 9606.ENSP00000290949; -.
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; P61421; -.
DR DMDM; 47606646; -.
DR PaxDb; P61421; -.
DR PeptideAtlas; P61421; -.
DR PRIDE; P61421; -.
DR DNASU; 9114; -.
DR Ensembl; ENST00000290949; ENSP00000290949; ENSG00000159720.
DR GeneID; 9114; -.
DR KEGG; hsa:9114; -.
DR UCSC; uc002ete.1; human.
DR CTD; 9114; -.
DR GeneCards; GC16M067471; -.
DR HGNC; HGNC:13724; ATP6V0D1.
DR HPA; HPA016938; -.
DR MIM; 607028; gene.
DR neXtProt; NX_P61421; -.
DR PharmGKB; PA25150; -.
DR eggNOG; COG1527; -.
DR HOGENOM; HOG000199065; -.
DR HOVERGEN; HBG018065; -.
DR InParanoid; P61421; -.
DR KO; K02146; -.
DR OrthoDB; EOG7KH9JT; -.
DR PhylomeDB; P61421; -.
DR BioCyc; MetaCyc:HS08417-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_17015; Metabolism of proteins.
DR ChiTaRS; ATP6V0D1; human.
DR GeneWiki; ATP6V0D1; -.
DR GenomeRNAi; 9114; -.
DR NextBio; 34161; -.
DR PRO; PR:P61421; -.
DR ArrayExpress; P61421; -.
DR Bgee; P61421; -.
DR CleanEx; HS_ATP6V0D1; -.
DR Genevestigator; P61421; -.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
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:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IDA:UniProtKB.
DR GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IEA:Ensembl.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0042384; P:cilium assembly; ISS:UniProtKB.
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:0015992; P:proton transport; NAS:UniProtKB.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR PANTHER; PTHR11028; PTHR11028; 1.
DR Pfam; PF01992; vATP-synt_AC39; 1.
DR PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR SUPFAM; SSF103486; SSF103486; 1.
PE 1: Evidence at protein level;
KW Cilium biogenesis/degradation; Complete proteome;
KW Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1 351 V-type proton ATPase subunit d 1.
FT /FTId=PRO_0000119350.
FT MOD_RES 270 270 Phosphotyrosine (By similarity).
FT CONFLICT 27 27 V -> E (in Ref. 1; CAA50591).
FT CONFLICT 266 267 NV -> KL (in Ref. 1; CAA50591).
SQ SEQUENCE 351 AA; 40329 MW; A720F8A87511203C CRC64;
MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN
EASPLTVSVI DDRLKEKMVV EFRHMRNHAY EPLASFLDFI TYSYMIDNVI LLITGTLHQR
SIAELVPKCH PLGSFEQMEA VNIAQTPAEL YNAILVDTPL AAFFQDCISE QDLDEMNIEI
IRNTLYKAYL ESFYKFCTLL GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL
FPHCGRLYPE GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK
LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI F
//
MIM
607028
*RECORD*
*FIELD* NO
607028
*FIELD* TI
*607028 ATPase, H+ TRANSPORTING, LYSOSOMAL, 38-KD, V0 SUBUNIT D, ISOFORM 1;
ATP6V0D1
read more;;VACUOLAR PROTON PUMP, V0 SUBUNIT D, ISOFORM 1;;
V-ATPase, SUBUNIT D
*FIELD* TX
DESCRIPTION
The vacuolar-type H(+)-ATPase (V-ATPase) is responsible for the
acidification of endosomes, lysosomes, and other intracellular
organelles. It is also involved in hydrogen ion transport across the
plasma membrane into the extracellular space. The V-ATPase is a
multisubunit complex with cytosolic and transmembrane domains. The
cytosolic catalytic domain consists of 3 A subunits and 3 B subunits,
which bind and hydrolyze ATP, as well as regulatory accessory subunits
including C (603097), D, and E (108746).
CLONING
Van Hille et al. (1993) cloned subunit D from an osteoclastoma tumor
cDNA library with probes developed by PCR from the bovine cDNA sequence.
The deduced 274-amino acid protein has a calculated molecular mass of
about 32 kD and shows 99% sequence homology with bovine subunit D.
Northern blot analysis revealed ubiquitous and comparable expression of
a 1.8-kb transcript.
While characterizing a genomic clone containing the HSD11B2 gene
(614232), Agarwal and White (2000) identified the ATP6V0D1 gene. They
obtained the complete ATP6V0D1 sequence from kidney cortical collecting
duct cell cDNA and found that the deduced protein is identical to the
mouse homolog with the exception of 2 conservative amino acid
substitutions. PCR amplification revealed high expression of subunit D
in kidney and placenta.
GENE STRUCTURE
Agarwal and White (2000) determined that the ATP6V0D1 gene consists of 8
exons spanning approximately 19 kb. They found that the gene is located
immediately adjacent to the HSD11B2 gene and is oriented in the opposite
direction, with the 3-prime ends of the 2 genes only 0.5 kb apart.
Stimulation of human kidney cortical collecting duct cells or
choriocarcinoma cells indicated that their expression is regulated
independently.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the
ATP6V0D1 gene to chromosome 16 (TMAP stSG1825). Agarwal and White (2000)
identified ATP6V0D1 on a genomic clone mapped to chromosome 16q22.
GENE FUNCTION
Cruciat et al. (2010) found that the prorenin receptor (PRR; 300556)
functions in a renin-independent manner as an adaptor between Wnt
receptors and the V-ATPase complex. Moreover, PRR and V-ATPase were
required to mediate Wnt signaling during anteroposterior patterning of
Xenopus early central nervous system development. Cruciat et al. (2010)
concluded that their results revealed an unsuspected role for the
prorenin receptor, V-ATPase activity, and acidification during
Wnt/beta-catenin (116806) signaling.
MOLECULAR GENETICS
Agarwal and White (2000) screened the ATP6V0D1 gene in 17 hypertensive
subjects and found no mutations.
*FIELD* RF
1. Agarwal, A. K.; White, P. C.: Structure of the VPATPD gene encoding
subunit D of the human vacuolar proton ATPase. Biochem. Biophys.
Res. Commun. 279: 543-547, 2000.
2. Cruciat, C.-M.; Ohkawara, B.; Acebron, S. P.; Karaulanov, E.; Reinhard,
C.; Ingelfinger, D.; Boutros, M.; Niehrs, C.: Requirement of prorenin
receptor and vacuolar H(+)-ATPase-mediated acidification for Wnt signaling. Science 327:
459-463, 2010.
3. van Hille, B.; Vanek, M.; Richener, H.; Green, J. R.; Bilbe, G.
: Cloning and tissue distribution of subunits C, D, and E of the human
vacuolar H(+)-ATPase. Biochem. Biophys. Res. Commun. 97: 15-21,
1993.
*FIELD* CN
Ada Hamosh - updated: 3/3/2010
*FIELD* CD
Patricia A. Hartz: 6/10/2002
*FIELD* ED
carol: 05/23/2013
carol: 9/23/2011
alopez: 3/5/2010
terry: 3/3/2010
carol: 7/7/2006
carol: 6/11/2002
*RECORD*
*FIELD* NO
607028
*FIELD* TI
*607028 ATPase, H+ TRANSPORTING, LYSOSOMAL, 38-KD, V0 SUBUNIT D, ISOFORM 1;
ATP6V0D1
read more;;VACUOLAR PROTON PUMP, V0 SUBUNIT D, ISOFORM 1;;
V-ATPase, SUBUNIT D
*FIELD* TX
DESCRIPTION
The vacuolar-type H(+)-ATPase (V-ATPase) is responsible for the
acidification of endosomes, lysosomes, and other intracellular
organelles. It is also involved in hydrogen ion transport across the
plasma membrane into the extracellular space. The V-ATPase is a
multisubunit complex with cytosolic and transmembrane domains. The
cytosolic catalytic domain consists of 3 A subunits and 3 B subunits,
which bind and hydrolyze ATP, as well as regulatory accessory subunits
including C (603097), D, and E (108746).
CLONING
Van Hille et al. (1993) cloned subunit D from an osteoclastoma tumor
cDNA library with probes developed by PCR from the bovine cDNA sequence.
The deduced 274-amino acid protein has a calculated molecular mass of
about 32 kD and shows 99% sequence homology with bovine subunit D.
Northern blot analysis revealed ubiquitous and comparable expression of
a 1.8-kb transcript.
While characterizing a genomic clone containing the HSD11B2 gene
(614232), Agarwal and White (2000) identified the ATP6V0D1 gene. They
obtained the complete ATP6V0D1 sequence from kidney cortical collecting
duct cell cDNA and found that the deduced protein is identical to the
mouse homolog with the exception of 2 conservative amino acid
substitutions. PCR amplification revealed high expression of subunit D
in kidney and placenta.
GENE STRUCTURE
Agarwal and White (2000) determined that the ATP6V0D1 gene consists of 8
exons spanning approximately 19 kb. They found that the gene is located
immediately adjacent to the HSD11B2 gene and is oriented in the opposite
direction, with the 3-prime ends of the 2 genes only 0.5 kb apart.
Stimulation of human kidney cortical collecting duct cells or
choriocarcinoma cells indicated that their expression is regulated
independently.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the
ATP6V0D1 gene to chromosome 16 (TMAP stSG1825). Agarwal and White (2000)
identified ATP6V0D1 on a genomic clone mapped to chromosome 16q22.
GENE FUNCTION
Cruciat et al. (2010) found that the prorenin receptor (PRR; 300556)
functions in a renin-independent manner as an adaptor between Wnt
receptors and the V-ATPase complex. Moreover, PRR and V-ATPase were
required to mediate Wnt signaling during anteroposterior patterning of
Xenopus early central nervous system development. Cruciat et al. (2010)
concluded that their results revealed an unsuspected role for the
prorenin receptor, V-ATPase activity, and acidification during
Wnt/beta-catenin (116806) signaling.
MOLECULAR GENETICS
Agarwal and White (2000) screened the ATP6V0D1 gene in 17 hypertensive
subjects and found no mutations.
*FIELD* RF
1. Agarwal, A. K.; White, P. C.: Structure of the VPATPD gene encoding
subunit D of the human vacuolar proton ATPase. Biochem. Biophys.
Res. Commun. 279: 543-547, 2000.
2. Cruciat, C.-M.; Ohkawara, B.; Acebron, S. P.; Karaulanov, E.; Reinhard,
C.; Ingelfinger, D.; Boutros, M.; Niehrs, C.: Requirement of prorenin
receptor and vacuolar H(+)-ATPase-mediated acidification for Wnt signaling. Science 327:
459-463, 2010.
3. van Hille, B.; Vanek, M.; Richener, H.; Green, J. R.; Bilbe, G.
: Cloning and tissue distribution of subunits C, D, and E of the human
vacuolar H(+)-ATPase. Biochem. Biophys. Res. Commun. 97: 15-21,
1993.
*FIELD* CN
Ada Hamosh - updated: 3/3/2010
*FIELD* CD
Patricia A. Hartz: 6/10/2002
*FIELD* ED
carol: 05/23/2013
carol: 9/23/2011
alopez: 3/5/2010
terry: 3/3/2010
carol: 7/7/2006
carol: 6/11/2002