DPP10

Dipeptidyl-peptidase 10 (non-functional)
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4WJL​
Identifiers
Symbols	DPP10 ; DPL2; DPPY; DPRP-3; DPRP3
External IDs	OMIM: 608209 MGI: 2442409 HomoloGene: 41400 GeneCards: DPP10 Gene
Gene ontology Molecular function • serine-type peptidase activity • dipeptidyl-peptidase activity • potassium channel regulator activity Cellular component • plasma membrane • membrane • integral component of membrane Biological process • proteolysis • protein localization to plasma membrane • positive regulation of establishment of protein localization to plasma membrane • regulation of potassium ion transmembrane transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	57628	269109
Ensembl	ENSG00000175497	ENSMUSG00000036815
UniProt	Q8N608	Q6NXK7
RefSeq (mRNA)	NM_001004360	NM_199021
RefSeq (protein)	NP_001004360	NP_950186
Location (UCSC)	Chr 2: 114.44 – 115.85 Mb	Chr 1: 123.32 – 124.05 Mb
PubMed search

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. "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

• 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. The DPIV family". Adv. Exp. Med. Biol. 524: 79–86. doi:10.1007/0-306-47920-6_10. 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.
• 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.
• 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. 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.