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{{Infobox_gene}}
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'''V-type proton ATPase subunit D''' is an [[enzyme]] that in humans is encoded by the ''ATP6V1D'' [[gene]].<ref name="pmid9442887">{{cite journal | vauthors = Stevens TH, Forgac M | title = Structure, function and regulation of the vacuolar (H+)-ATPase | journal = Annu Rev Cell Dev Biol | volume = 13 | issue =  | pages = 779–808 |date=Feb 1998 | pmid = 9442887 | pmc =  | doi = 10.1146/annurev.cellbio.13.1.779 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1D ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51382| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D
| HGNCid = 13527
| Symbol = ATP6V1D
| AltSymbols =; ATP6M; VATD; VMA8
| OMIM = 609398
| ECnumber = 
| Homologene = 5783
| MGIid = 1921084
| Function = {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046933 |text = hydrogen ion transporting ATP synthase activity, rotational mechanism}} {{GNF_GO|id=GO:0046961 |text = hydrogen ion transporting ATPase activity, rotational mechanism}}
| Component = {{GNF_GO|id=GO:0016469 |text = proton-transporting two-sector ATPase complex}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0015986 |text = ATP synthesis coupled proton transport}} {{GNF_GO|id=GO:0015992 |text = proton transport}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 51382
    | Hs_Ensembl = ENSG00000100554
    | Hs_RefseqProtein = NP_057078
    | Hs_RefseqmRNA = NM_015994
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 66830841
    | Hs_GenLoc_end = 66896261
    | Hs_Uniprot = Q9Y5K8
    | Mm_EntrezGene = 73834
    | Mm_Ensembl = ENSMUSG00000021114
    | Mm_RefseqmRNA = NM_023721
    | Mm_RefseqProtein = NP_076210
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 79761822
    | Mm_GenLoc_end = 79780478
    | Mm_Uniprot = Q3U684
  }}
}}
'''ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D''', also known as '''ATP6V1D''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1D ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51382| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c&quot;, and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene encodes the V1 domain D subunit protein.<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V1D ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51382| accessdate = }}</ref>
| summary_text = This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene encodes the V1 domain D subunit protein.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ATP6V1D}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Finbow ME, Harrison MA |title=The vacuolar H+-ATPase: a universal proton pump of eukaryotes. |journal=Biochem. J. |volume=324 ( Pt 3) |issue=  |pages= 697-712 |year= 1997 |pmid= 9210392 |doi=  }}
*{{cite journal  | vauthors=Finbow ME, Harrison MA |title=The vacuolar H+-ATPase: a universal proton pump of eukaryotes |journal=Biochem. J. |volume=324 |issue=  3|pages= 697–712 |year= 1997 |pmid= 9210392 |doi=  10.1042/bj3240697| pmc=1218484 }}
*{{cite journal  | author=Stevens TH, Forgac M |title=Structure, function and regulation of the vacuolar (H+)-ATPase. |journal=Annu. Rev. Cell Dev. Biol. |volume=13 |issue=  |pages= 779-808 |year= 1998 |pmid= 9442887 |doi= 10.1146/annurev.cellbio.13.1.779 }}
*{{cite journal  | vauthors=Nelson N, Harvey WR |title=Vacuolar and plasma membrane proton-adenosinetriphosphatases |journal=Physiol. Rev. |volume=79 |issue= 2 |pages= 361–85 |year= 1999 |pmid= 10221984 |doi=  }}
*{{cite journal  | author=Nelson N, Harvey WR |title=Vacuolar and plasma membrane proton-adenosinetriphosphatases. |journal=Physiol. Rev. |volume=79 |issue= 2 |pages= 361-85 |year= 1999 |pmid= 10221984 |doi=  }}
*{{cite journal  | author=Forgac M |title=Structure and properties of the vacuolar (H+)-ATPases |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 12951–4 |year= 1999 |pmid= 10224039 |doi=10.1074/jbc.274.19.12951 }}
*{{cite journal  | author=Forgac M |title=Structure and properties of the vacuolar (H+)-ATPases. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 12951-4 |year= 1999 |pmid= 10224039 |doi=  }}
*{{cite journal  | author=Kane PM |title=Introduction: V-ATPases 1992-1998 |journal=J. Bioenerg. Biomembr. |volume=31 |issue= 1 |pages= 3–5 |year= 1999 |pmid= 10340843 |doi=10.1023/A:1001884227654 }}
*{{cite journal  | author=Kane PM |title=Introduction: V-ATPases 1992-1998. |journal=J. Bioenerg. Biomembr. |volume=31 |issue= 1 |pages= 3-5 |year= 1999 |pmid= 10340843 |doi=  }}
*{{cite journal  | vauthors=Wieczorek H, Brown D, Grinstein S |title=Animal plasma membrane energization by proton-motive V-ATPases |journal=BioEssays |volume=21 |issue= 8 |pages= 637–48 |year= 1999 |pmid= 10440860 |doi= 10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W |display-authors=etal}}
*{{cite journal  | author=Wieczorek H, Brown D, Grinstein S, ''et al.'' |title=Animal plasma membrane energization by proton-motive V-ATPases. |journal=Bioessays |volume=21 |issue= 8 |pages= 637-48 |year= 1999 |pmid= 10440860 |doi= 10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W }}
*{{cite journal  | vauthors=Nishi T, Forgac M |title=The vacuolar (H+)-ATPases--nature's most versatile proton pumps |journal=Nat. Rev. Mol. Cell Biol. |volume=3 |issue= 2 |pages= 94–103 |year= 2002 |pmid= 11836511 |doi= 10.1038/nrm729 }}
*{{cite journal  | author=Nishi T, Forgac M |title=The vacuolar (H+)-ATPases--nature's most versatile proton pumps. |journal=Nat. Rev. Mol. Cell Biol. |volume=3 |issue= 2 |pages= 94-103 |year= 2002 |pmid= 11836511 |doi= 10.1038/nrm729 }}
*{{cite journal  | vauthors=Kawasaki-Nishi S, Nishi T, Forgac M |title=Proton translocation driven by ATP hydrolysis in V-ATPases |journal=FEBS Lett. |volume=545 |issue= 1 |pages= 76–85 |year= 2003 |pmid= 12788495 |doi=10.1016/S0014-5793(03)00396-X }}
*{{cite journal  | author=Kawasaki-Nishi S, Nishi T, Forgac M |title=Proton translocation driven by ATP hydrolysis in V-ATPases. |journal=FEBS Lett. |volume=545 |issue= 1 |pages= 76-85 |year= 2003 |pmid= 12788495 |doi=  }}
*{{cite journal  | author=Morel N |title=Neurotransmitter release: the dark side of the vacuolar-H+ATPase |journal=Biol. Cell |volume=95 |issue= 7 |pages= 453–7 |year= 2004 |pmid= 14597263 |doi=10.1016/S0248-4900(03)00075-3 }}
*{{cite journal  | author=Morel N |title=Neurotransmitter release: the dark side of the vacuolar-H+ATPase. |journal=Biol. Cell |volume=95 |issue= 7 |pages= 453-7 |year= 2004 |pmid= 14597263 |doi=  }}
*{{cite journal  | vauthors=Hu RM, Han ZG, Song HD |title=Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 17 |pages= 9543–8 |year= 2000 |pmid= 10931946 |doi= 10.1073/pnas.160270997 | pmc=16901 |display-authors=etal}}
*{{cite journal  | author=Hu RM, Han ZG, Song HD, ''et al.'' |title=Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 17 |pages= 9543-8 |year= 2000 |pmid= 10931946 |doi= 10.1073/pnas.160270997 }}
*{{cite journal  | vauthors=Kennell JA, Richards NW, Schaner PE, Gumucio DL |title=cDNA cloning, chromosomal localization and evolutionary analysis of mouse vacuolar ATPase subunit D, Atp6m |journal=Cytogenet. Cell Genet. |volume=92 |issue= 3–4 |pages= 337–41 |year= 2001 |pmid= 11435709 |doi=10.1159/000056924 }}
*{{cite journal  | author=Kennell JA, Richards NW, Schaner PE, Gumucio DL |title=cDNA cloning, chromosomal localization and evolutionary analysis of mouse vacuolar ATPase subunit D, Atp6m. |journal=Cytogenet. Cell Genet. |volume=92 |issue= 3-4 |pages= 337-41 |year= 2001 |pmid= 11435709 |doi=  }}
*{{cite journal  | vauthors=Yang CS, Weiner H |title=Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol |journal=Arch. Biochem. Biophys. |volume=400 |issue= 1 |pages= 105–10 |year= 2002 |pmid= 11913976 |doi= 10.1006/abbi.2002.2778 }}
*{{cite journal  | author=Yang CS, Weiner H |title=Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol. |journal=Arch. Biochem. Biophys. |volume=400 |issue= 1 |pages= 105-10 |year= 2002 |pmid= 11913976 |doi= 10.1006/abbi.2002.2778 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:27, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

V-type proton ATPase subunit D is an enzyme that in humans is encoded by the ATP6V1D gene.[1][2]

This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This gene encodes the V1 domain D subunit protein.[2]

References

  1. ↑ Stevens TH, Forgac M (Feb 1998). "Structure, function and regulation of the vacuolar (H+)-ATPase". Annu Rev Cell Dev Biol. 13: 779–808. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
  2. ↑ 2.0 2.1 "Entrez Gene: ATP6V1D ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D".

External links

Further reading



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