DPP10

Protein-coding gene in the species Homo sapiens
DPP10
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4WJL

Identifiers
AliasesDPP10, DPL2, DPPY, DPRP-3, DPRP3, dipeptidyl peptidase like 10
External IDsOMIM: 608209; MGI: 2442409; HomoloGene: 41400; GeneCards: DPP10; OMA:DPP10 - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for DPP10
Genomic location for DPP10
Band2q14.1Start114,442,299 bp[1]
End115,845,780 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for DPP10
Genomic location for DPP10
Band1|1 E2.3Start123,249,200 bp[2]
End124,773,776 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • Brodmann area 23

  • prefrontal cortex

  • dorsolateral prefrontal cortex

  • Brodmann area 9

  • Brodmann area 46

  • cingulate gyrus

  • anterior cingulate cortex

  • primary visual cortex

  • amygdala
Top expressed in
  • substantia nigra

  • piriform cortex

  • prefrontal cortex

  • temporal lobe

  • amygdala

  • primary motor cortex

  • cingulate gyrus

  • lateral septal nucleus

  • lobe of cerebellum

  • medial dorsal nucleus
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • potassium channel regulator activity
  • serine-type peptidase activity
  • dipeptidyl-peptidase activity
  • transmembrane transporter binding
Cellular component
  • integral component of membrane
  • plasma membrane
  • membrane
  • voltage-gated potassium channel complex
Biological process
  • protein localization to plasma membrane
  • regulation of potassium ion transmembrane transport
  • proteolysis
  • positive regulation of protein localization to plasma membrane
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

57628

269109

Ensembl

ENSG00000175497

ENSMUSG00000036815

UniProt

Q8N608

Q6NXK7

RefSeq (mRNA)
NM_001004360
NM_001178034
NM_001178036
NM_001178037
NM_020868

NM_001321905
NM_001321906
NM_001321907
NM_001321908
NM_001321909
NM_001321910
NM_001321911
NM_001321912
NM_001321913
NM_001321914
NM_001399849
NM_001399850
NM_001399851

NM_199021

RefSeq (protein)
NP_001004360
NP_001171505
NP_001171507
NP_001171508
NP_001308834

NP_001308835
NP_001308836
NP_001308837
NP_001308838
NP_001308839
NP_001308840
NP_001308841
NP_001308842
NP_001308843
NP_065919

NP_950186
NP_001393353
NP_001393354
NP_001393355

Location (UCSC)Chr 2: 114.44 – 115.85 MbChr 1: 123.25 – 124.77 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Inactive dipeptidyl peptidase 10 is a protein that in humans is encoded by the DPP10 gene.[5][6][7] Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[7]

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.[7]

Clinical significance

Mutations in this gene have been associated with asthma[7] and autism spectrum disorders.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000175497 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000036815 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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.
  7. ^ a b c d "Entrez Gene: DPP10 dipeptidyl-peptidase 10".
  8. ^ 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

  • Yamada R, Ymamoto K (2005). "Recent findings on genes associated with inflammatory disease". Mutat. Res. 573 (1–2): 136–51. doi:10.1016/j.mrfmmm.2004.06.061. PMID 15829243.
  • Chen T, Ajami K, McCaughan GW, Gorrell MD, Abbott CA (2003). "Dipeptidyl Peptidase IV Gene Family". Dipeptidyl peptidase IV gene family. The DPIV family. Adv. Exp. Med. Biol. Vol. 524. Springer. pp. 79–86. doi:10.1007/0-306-47920-6_10. ISBN 9780306479205. PMID 12675227.
  • 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 (November 2003). "Positional cloning of a novel gene influencing asthma from chromosome 2q14". Nat. Genet. 35 (3): 258–63. doi:10.1038/ng1256. PMID 14566338. S2CID 40595323.
  • Jerng HH, Qian Y, Pfaffinger PJ (2005). "Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase 10 (DPP10)". Biophys. J. 87 (4): 2380–96. doi:10.1529/biophysj.104.042358. PMC 1304660. PMID 15454437.
  • Zagha E, Ozaita A, Chang SY, Nadal MS, Lin U, Saganich MJ, McCormack T, Akinsanya KO, Qi SY, Rudy B (May 2005). "DPP10 modulates Kv4-mediated A-type potassium channels". J. Biol. Chem. 280 (19): 18853–61. doi:10.1074/jbc.M410613200. PMID 15671030.
  • Ren X, Hayashi Y, Yoshimura N, Takimoto K (2005). "Transmembrane interaction mediates complex formation between peptidase homologues and Kv4 channels". Mol. Cell. Neurosci. 29 (2): 320–32. doi:10.1016/j.mcn.2005.02.003. PMID 15911355. S2CID 34065803.
  • Chen T, Ajami K, McCaughan GW, Gai WP, Gorrell MD, Abbott CA (January 2006). "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". Biochim. Biophys. Acta. 1764 (1): 33–43. doi:10.1016/j.bbapap.2005.09.013. PMID 16290253.
  • Takimoto K, Hayashi Y, Ren X, Yoshimura N (2006). "Species and tissue differences in the expression of DPPY splicing variants". Biochem. Biophys. Res. Commun. 348 (3): 1094–100. doi:10.1016/j.bbrc.2006.07.157. PMID 16899223.
  • Jerng HH, Lauver AD, Pfaffinger PJ (2007). "DPP10 splice variants are localized in distinct neuronal populations and act to differentially regulate the inactivation properties of Kv4-based ion channels". Mol. Cell. Neurosci. 35 (4): 604–24. doi:10.1016/j.mcn.2007.03.008. PMC 3674967. PMID 17475505.
  • Hersh CP, Raby BA, Soto-Quirós ME, Murphy AJ, Avila L, Lasky-Su J, Sylvia JS, Klanderman BJ, Lange C, Weiss ST, Celedón JC (November 2007). "Comprehensive testing of positionally cloned asthma genes in two populations". Am. J. Respir. Crit. Care Med. 176 (9): 849–57. doi:10.1164/rccm.200704-592OC. PMC 2048676. PMID 17702965.


  • v
  • t
  • e