ATP6V0D1: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
m (Bot: HTTP→HTTPS)
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''V-type proton ATPase subunit d 1''' is an [[enzyme]] that in humans is encoded by the ''ATP6V0D1'' [[gene]].<ref name="pmid8250920">{{cite journal | vauthors = van Hille B, Vanek M, Richener H, Green JR, Bilbe G | title = Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase | journal = Biochem Biophys Res Commun | volume = 197 | issue = 1 | pages = 15–21 |date=Jan 1994 | pmid = 8250920 | pmc =  | doi =10.1006/bbrc.1993.2434 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP6V0D1 ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9114| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
 
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d1
| HGNCid = 13724
| Symbol = ATP6V0D1
| AltSymbols =; ATP6D; P39; ATP6DV; VATX; VMA6; VPATPD
| OMIM = 607028
| ECnumber = 
| Homologene = 3444
| MGIid = 1201778
| GeneAtlas_image1 = PBB_GE_ATP6V0D1_212041_at_tn.png
| Function = {{GNF_GO|id=GO:0008553 |text = hydrogen-exporting ATPase activity, phosphorylative mechanism}} {{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:0016471 |text = vacuolar proton-transporting V-type 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 = 9114
    | Hs_Ensembl = ENSG00000159720
    | Hs_RefseqProtein = NP_004682
    | Hs_RefseqmRNA = NM_004691
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 66029426
    | Hs_GenLoc_end = 66072589
    | Hs_Uniprot = P61421
    | Mm_EntrezGene = 11972
    | Mm_Ensembl = ENSMUSG00000013160
    | Mm_RefseqmRNA = NM_013477
    | Mm_RefseqProtein = NP_038505
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 108413599
    | Mm_GenLoc_end = 108455169
    | Mm_Uniprot = Q54A57
  }}
}}
'''ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d1''', also known as '''ATP6V0D1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V0D1 ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9114| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{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'', and d. Additional isoforms of many of the V1 and V0 subunit proteins are encoded by multiple genes or alternatively spliced transcript variants. This encoded protein is known as the D subunit and is found ubiquitously.<ref name="entrez">{{cite web | title = Entrez Gene: ATP6V0D1 ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9114| 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 encoded protein is known as the D subunit and is found ubiquitously.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ATP6V0D1}}
 
==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. | series=324 |journal=Biochem. J. |volume=( Pt 3) |issue=  |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=Stevens TH, Forgac M |title=Structure, function and regulation of the vacuolar (H+)-ATPase. |journal=Annu. Rev. Cell Dev. Biol. |volume=13 |issue=  1|pages= 779–808 |year= 1998 |pmid= 9442887 |doi= 10.1146/annurev.cellbio.13.1.779 }}
*{{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  | 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=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=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=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  | 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=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=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=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=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=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  | 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=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  | 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=Wang SY, Moriyama Y, Mandel M, ''et al.'' |title=Cloning of cDNA encoding a 32-kDa protein. An accessory polypeptide of the H+-ATPase from chromaffin granules. |journal=J. Biol. Chem. |volume=263 |issue= 33 |pages= 17638-42 |year= 1988 |pmid= 2903164 |doi=  }}
*{{cite journal  | vauthors=Wang SY, Moriyama Y, Mandel M |title=Cloning of cDNA encoding a 32-kDa protein. An accessory polypeptide of the H+-ATPase from chromaffin granules. |journal=J. Biol. Chem. |volume=263 |issue= 33 |pages= 17638–42 |year= 1988 |pmid= 2903164 |doi=  |display-authors=etal}}
*{{cite journal  | author=van Hille B, Vanek M, Richener H, ''et al.'' |title=Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase. |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 1 |pages= 15-21 |year= 1994 |pmid= 8250920 |doi=  }}
*{{cite journal  | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  | vauthors=Agarwal AK, White PC |title=Structure of the VPATPD gene encoding subunit D of the human vacuolar proton ATPase. |journal=Biochem. Biophys. Res. Commun. |volume=279 |issue= 2 |pages= 543–7 |year= 2001 |pmid= 11118322 |doi= 10.1006/bbrc.2000.4003 }}
*{{cite journal  | author=Agarwal AK, White PC |title=Structure of the VPATPD gene encoding subunit D of the human vacuolar proton ATPase. |journal=Biochem. Biophys. Res. Commun. |volume=279 |issue= 2 |pages= 543-7 |year= 2001 |pmid= 11118322 |doi= 10.1006/bbrc.2000.4003 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{WikiDoc Sources}}
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
 
 
{{gene-16-stub}}

Latest revision as of 18:27, 29 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

V-type proton ATPase subunit d 1 is an enzyme that in humans is encoded by the ATP6V0D1 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 encoded protein is known as the D subunit and is found ubiquitously.[2]

References

  1. ↑ van Hille B, Vanek M, Richener H, Green JR, Bilbe G (Jan 1994). "Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase". Biochem Biophys Res Commun. 197 (1): 15–21. doi:10.1006/bbrc.1993.2434. PMID 8250920.
  2. ↑ 2.0 2.1 "Entrez Gene: ATP6V0D1 ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d1".

External links

Further reading



Retrieved from "https://www.wikidoc.org/index.php?title=ATP6V0D1&oldid=1417373"