DPP10: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Inactive dipeptidyl peptidase 10''' is a [[protein]] that in humans is encoded by the ''DPP10'' [[gene]].<ref name="pmid10819331">{{cite journal | vauthors = Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Res | volume = 7 | issue = 2 | pages = 143–50 |date=Sep 2000 | pmid = 10819331 | pmc =  | doi =10.1093/dnares/7.2.143  }}</ref><ref name="pmid12662155">{{cite journal | vauthors = Qi SY, Riviere PJ, Trojnar J, Junien JL, Akinsanya KO | title = Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases | journal = Biochem J | volume = 373 | issue = Pt 1 | pages = 179–89 |date=Jun 2003 | pmid = 12662155 | pmc = 1223468 | doi = 10.1042/BJ20021914 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DPP10 dipeptidyl-peptidase 10| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57628| accessdate = }}</ref> Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez" />
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Dipeptidyl-peptidase 10
| HGNCid = 20823
| Symbol = DPP10
| AltSymbols =; DPL2; DPPY; DPRP3
| OMIM = 608209
| ECnumber = 
| Homologene = 41400
| MGIid = 2442409
| GeneAtlas_image1 = PBB_GE_DPP10_gnf1h06059_at_tn.png
| GeneAtlas_image2 = PBB_GE_DPP10_gnf1h06976_at_tn.png
| Function = {{GNF_GO|id=GO:0004274 |text = dipeptidyl-peptidase IV activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 57628
    | Hs_Ensembl = ENSG00000175497
    | Hs_RefseqProtein = NP_001004360
    | Hs_RefseqmRNA = NM_001004360
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 115636271
    | Hs_GenLoc_end = 116318406
    | Hs_Uniprot = Q8N608
    | Mm_EntrezGene = 269109
    | Mm_Ensembl = ENSMUSG00000036815
    | Mm_RefseqmRNA = XM_985364
    | Mm_RefseqProtein = XP_990458
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 125159688
    | Mm_GenLoc_end = 125873098
    | Mm_Uniprot = Q6NXK7
  }}
}}
'''Dipeptidyl-peptidase 10''', also known as '''DPP10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DPP10 dipeptidyl-peptidase 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57628| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a single-pass type II membrane protein that is a member of the S9B family in clan SC of the serine proteases. This protein has no detectable protease activity, most likely due to the absence of the conserved serine residue normally present in the catalytic domain of serine proteases. However, it does bind specific voltage-gated potassium channels and alters their expression and biophysical properties.<ref name="entrez" />
{{PBB_Summary
 
| section_title =
== Clinical significance ==
| summary_text = This gene encodes a single-pass type II membrane protein that is a member of the S9B family in clan SC of the serine proteases. This protein has no detectable protease activity, most likely due to the absence of the conserved serine residue normally present in the catalytic domain of serine proteases. However, it does bind specific voltage-gated potassium channels and alters their expression and biophysical properties. Mutations in this gene have been associated with asthma. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: DPP10 dipeptidyl-peptidase 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57628| accessdate = }}</ref>
 
}}
Mutations in this gene have been associated with [[asthma]]<ref name="entrez" /> and [[autism spectrum disorders]].<ref name="pmid23375656">{{cite journal | vauthors = Girirajan S, Dennis MY, Baker C, Malig M, Coe BP, Campbell CD, Mark K, Vu TH, Alkan C, Cheng Z, Biesecker LG, Bernier R, Eichler EE | title = Refinement and discovery of new hotspots of copy-number variation associated with autism spectrum disorder | journal = Am. J. Hum. Genet. | volume = 92 | issue = 2 | pages = 221–37 |date=February 2013 | pmid = 23375656 | pmc = 3567267 | doi = 10.1016/j.ajhg.2012.12.016 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Yamada R, Ymamoto K |title=Recent findings on genes associated with inflammatory disease |journal=Mutat. Res. |volume=573 |issue= 1–2 |pages= 136–51 |year= 2005 |pmid= 15829243 |doi= 10.1016/j.mrfmmm.2004.06.061 }}
| citations =
*{{cite journal | vauthors = Chen T, Ajami K, McCaughan GW, Gorrell MD, Abbott CA | title = Dipeptidyl peptidase IV gene family. The DPIV family | journal = Adv. Exp. Med. Biol. | volume = 524 | issue = | pages = 79–86 | year = 2003 | pmid = 12675227 | doi = 10.1007/0-306-47920-6_10 }}
*{{cite journal  | author=Yamada R, Ymamoto K |title=Recent findings on genes associated with inflammatory disease. |journal=Mutat. Res. |volume=573 |issue= 1-2 |pages= 136-51 |year= 2005 |pmid= 15829243 |doi= 10.1016/j.mrfmmm.2004.06.061 }}
*{{cite journal | vauthors = Allen M, Heinzmann A, Noguchi E, Abecasis G, Broxholme J, Ponting CP, Bhattacharyya S, Tinsley J, Zhang Y, Holt R, Jones EY, Lench N, Carey A, Jones H, Dickens NJ, Dimon C, Nicholls R, Baker C, Xue L, Townsend E, Kabesch M, Weiland SK, Carr D, von Mutius E, Adcock IM, Barnes PJ, Lathrop GM, Edwards M, Moffatt MF, Cookson WO | title = Positional cloning of a novel gene influencing asthma from chromosome 2q14 | journal = Nat. Genet. | volume = 35 | issue = 3 | pages = 258–63 |date=November 2003 | pmid = 14566338 | doi = 10.1038/ng1256 }}
*{{cite journal | author=Nagase T, Kikuno R, Ishikawa K, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 2 |pages= 143-50 |year= 2000 |pmid= 10819331 |doi=  }}
*{{cite journal  | vauthors=Jerng HH, Qian Y, Pfaffinger PJ |title=Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase 10 (DPP10) |journal=Biophys. J. |volume=87 |issue= 4 |pages= 2380–96 |year= 2005 |pmid= 15454437 |doi= 10.1529/biophysj.104.042358  | pmc=1304660 }}
*{{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 }}
*{{cite journal | vauthors = Zagha E, Ozaita A, Chang SY, Nadal MS, Lin U, Saganich MJ, McCormack T, Akinsanya KO, Qi SY, Rudy B | title = DPP10 modulates Kv4-mediated A-type potassium channels | journal = J. Biol. Chem. | volume = 280 | issue = 19 | pages = 18853–61 |date=May 2005 | pmid = 15671030 | doi = 10.1074/jbc.M410613200 }}
*{{cite journal  | author=Qi SY, Riviere PJ, Trojnar J, ''et al.'' |title=Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases. |journal=Biochem. J. |volume=373 |issue= Pt 1 |pages= 179-89 |year= 2003 |pmid= 12662155 |doi= 10.1042/BJ20021914 }}
*{{cite journal  | vauthors=Ren X, Hayashi Y, Yoshimura N, Takimoto K |title=Transmembrane interaction mediates complex formation between peptidase homologues and Kv4 channels |journal=Mol. Cell. Neurosci. |volume=29 |issue= 2 |pages= 320–32 |year= 2005 |pmid= 15911355 |doi= 10.1016/j.mcn.2005.02.003 }}
*{{cite journal  | author=Chen T, Ajami K, McCaughan GW, ''et al.'' |title=Dipeptidyl peptidase IV gene family. The DPIV family. |journal=Adv. Exp. Med. Biol. |volume=524 |issue= |pages= 79-86 |year= 2003 |pmid= 12675227 |doi= }}
*{{cite journal | vauthors = Chen T, Ajami K, McCaughan GW, Gai WP, Gorrell MD, Abbott CA | title = Molecular characterization of a novel dipeptidyl peptidase like 2-short form (DPL2-s) that is highly expressed in the brain and lacks dipeptidyl peptidase activity | journal = Biochim. Biophys. Acta | volume = 1764 | issue = 1 | pages = 33–43 |date=January 2006 | pmid = 16290253 | doi = 10.1016/j.bbapap.2005.09.013 }}
*{{cite journal | author=Allen M, Heinzmann A, Noguchi E, ''et al.'' |title=Positional cloning of a novel gene influencing asthma from chromosome 2q14. |journal=Nat. Genet. |volume=35 |issue= 3 |pages= 258-63 |year= 2003 |pmid= 14566338 |doi= 10.1038/ng1256 }}
*{{cite journal  | vauthors=Takimoto K, Hayashi Y, Ren X, Yoshimura N |title=Species and tissue differences in the expression of DPPY splicing variants |journal=Biochem. Biophys. Res. Commun. |volume=348 |issue= 3 |pages= 1094–100 |year= 2006 |pmid= 16899223 |doi= 10.1016/j.bbrc.2006.07.157 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Jerng HH, Lauver AD, Pfaffinger PJ |title=DPP10 splice variants are localized in distinct neuronal populations and act to differentially regulate the inactivation properties of Kv4-based ion channels |journal=Mol. Cell. Neurosci. |volume=35 |issue= 4 |pages= 604–24 |year= 2007 |pmid= 17475505 |doi= 10.1016/j.mcn.2007.03.008 }}
*{{cite journal  | author=Jerng HH, Qian Y, Pfaffinger PJ |title=Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase 10 (DPP10). |journal=Biophys. J. |volume=87 |issue= 4 |pages= 2380-96 |year= 2005 |pmid= 15454437 |doi= 10.1529/biophysj.104.042358 }}
*{{cite journal | vauthors = Hersh CP, Raby BA, Soto-Quirós ME, Murphy AJ, Avila L, Lasky-Su J, Sylvia JS, Klanderman BJ, Lange C, Weiss ST, Celedón JC | title = Comprehensive testing of positionally cloned asthma genes in two populations | journal = Am. J. Respir. Crit. Care Med. | volume = 176 | issue = 9 | pages = 849–57 |date=November 2007 | pmid = 17702965 | pmc = 2048676 | doi = 10.1164/rccm.200704-592OC }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Zagha E, Ozaita A, Chang SY, ''et al.'' |title=DPP10 modulates Kv4-mediated A-type potassium channels. |journal=J. Biol. Chem. |volume=280 |issue= 19 |pages= 18853-61 |year= 2005 |pmid= 15671030 |doi= 10.1074/jbc.M410613200 }}
*{{cite journal  | author=Ren X, Hayashi Y, Yoshimura N, Takimoto K |title=Transmembrane interaction mediates complex formation between peptidase homologues and Kv4 channels. |journal=Mol. Cell. Neurosci. |volume=29 |issue= 2 |pages= 320-32 |year= 2005 |pmid= 15911355 |doi= 10.1016/j.mcn.2005.02.003 }}
*{{cite journal | author=Chen T, Ajami K, McCaughan GW, ''et al.'' |title=Molecular characterization of a novel dipeptidyl peptidase like 2-short form (DPL2-s) that is highly expressed in the brain and lacks dipeptidyl peptidase activity. |journal=Biochim. Biophys. Acta |volume=1764 |issue= 1 |pages= 33-43 |year= 2006 |pmid= 16290253 |doi= 10.1016/j.bbapap.2005.09.013 }}
*{{cite journal  | author=Takimoto K, Hayashi Y, Ren X, Yoshimura N |title=Species and tissue differences in the expression of DPPY splicing variants. |journal=Biochem. Biophys. Res. Commun. |volume=348 |issue= 3 |pages= 1094-100 |year= 2006 |pmid= 16899223 |doi= 10.1016/j.bbrc.2006.07.157 }}
*{{cite journal  | author=Jerng HH, Lauver AD, Pfaffinger PJ |title=DPP10 splice variants are localized in distinct neuronal populations and act to differentially regulate the inactivation properties of Kv4-based ion channels. |journal=Mol. Cell. Neurosci. |volume=35 |issue= 4 |pages= 604-24 |year= 2007 |pmid= 17475505 |doi= 10.1016/j.mcn.2007.03.008 }}
*{{cite journal | author=Hersh CP, Raby BA, Soto-Quirós ME, ''et al.'' |title=Comprehensive testing of positionally cloned asthma genes in two populations. |journal=Am. J. Respir. Crit. Care Med. |volume=176 |issue= 9 |pages= 849-57 |year= 2007 |pmid= 17702965 |doi= 10.1164/rccm.200704-592OC }}
}}
{{refend}}
{{refend}}


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Revision as of 18:41, 30 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

Inactive dipeptidyl peptidase 10 is a protein that in humans is encoded by the DPP10 gene.[1][2][3] Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[3]

Function

This gene encodes a single-pass type II membrane protein that is a member of the S9B family in clan SC of the serine proteases. This protein has no detectable protease activity, most likely due to the absence of the conserved serine residue normally present in the catalytic domain of serine proteases. However, it does bind specific voltage-gated potassium channels and alters their expression and biophysical properties.[3]

Clinical significance

Mutations in this gene have been associated with asthma[3] and autism spectrum disorders.[4]

References

  1. ↑ Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O (Sep 2000). "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (2): 143–50. doi:10.1093/dnares/7.2.143. PMID 10819331.
  2. ↑ Qi SY, Riviere PJ, Trojnar J, Junien JL, Akinsanya KO (Jun 2003). "Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases". Biochem J. 373 (Pt 1): 179–89. doi:10.1042/BJ20021914. PMC 1223468. PMID 12662155.
  3. ↑ 3.0 3.1 3.2 3.3 "Entrez Gene: DPP10 dipeptidyl-peptidase 10".
  4. ↑ Girirajan S, Dennis MY, Baker C, Malig M, Coe BP, Campbell CD, Mark K, Vu TH, Alkan C, Cheng Z, Biesecker LG, Bernier R, Eichler EE (February 2013). "Refinement and discovery of new hotspots of copy-number variation associated with autism spectrum disorder". Am. J. Hum. Genet. 92 (2): 221–37. doi:10.1016/j.ajhg.2012.12.016. PMC 3567267. PMID 23375656.

Further reading


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