DPP9

From Wikipedia, the free encyclopedia

Dipeptidyl-peptidase 9

Identifiers

DPP9; DKFZp762F117; DPRP2; FLJ16073

External IDs

OMIM: 608258 MGI: 2443967 HomoloGene: 16385

Gene ontology
Molecular Function:	• aminopeptidase activity • serine-type endopeptidase activity • dipeptidyl-peptidase IV activity
Cellular Component:	• membrane
Biological Process:	• proteolysis

Orthologs

Human

Mouse

Refseq

NM_139159 (mRNA)
NP_631898 (protein)

NM_172624 (mRNA)
NP_766212 (protein)

Location

Chr 19: 4.63 - 4.67 Mb

Chr 17: 55.82 - 55.85 Mb

Pubmed search

[1]

[2]

Dipeptidyl-peptidase 9, also known as DPP9, is a human gene.^[1]

This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. The protein has been shown to have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Although the activity of this protein is similar to that of dipeptidyl peptidase 4 (DPP4), it does not appear to be membrane bound. In general, dipeptidyl peptidases appear to be involved in the regulation of the activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. Several transcript variants of this gene have been described but not fully characterized.^[1]

[edit] References

^ ^a ^b Entrez Gene: DPP9 dipeptidyl-peptidase 9.

[edit] Further reading

Olsen C, Wagtmann N (2003). "Identification and characterization of human DPP9, a novel homologue of dipeptidyl peptidase IV.". Gene 299 (1-2): 185–93. PMID 12459266.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Ajami K, Abbott CA, Obradovic M, et al. (2003). "Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family.". Biochemistry 42 (3): 694–701. doi:10.1021/bi026846s. PMID 12534281.
Qi SY, Riviere PJ, Trojnar J, et al. (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. PMID 12662155.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Ajami K, Abbott CA, McCaughan GW, Gorrell MD (2004). "Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity.". Biochim. Biophys. Acta 1679 (1): 18–28. doi:10.1016/j.bbaexp.2004.03.010. PMID 15245913.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Ogasawara W, Tanaka C, Suzuki M, et al. (2005). "Isoforms of dipeptidyl aminopeptidase IV from Pseudomonas sp. WO24: role of the signal sequence and overexpression in Escherichia coli.". Protein Expr. Purif. 41 (2): 241–51. doi:10.1016/j.pep.2004.10.027. PMID 15866709.
Bjelke JR, Christensen J, Nielsen PF, et al. (2006). "Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV.". Biochem. J. 396 (2): 391–9. doi:10.1042/BJ20060079. PMID 16475979.
Yu DM, Wang XM, Ajami K, et al. (2006). "DP8 and DP9 have extra-enzymatic roles in cell adhesion, migration and apoptosis.". Adv. Exp. Med. Biol. 575: 63–72. PMID 16700509.
Yu DM, Wang XM, McCaughan GW, Gorrell MD (2006). "Extraenzymatic functions of the dipeptidyl peptidase IV-related proteins DP8 and DP9 in cell adhesion, migration and apoptosis.". FEBS J. 273 (11): 2447–60. doi:10.1111/j.1742-4658.2006.05253.x. PMID 16704418.