DPP3

Dipeptidyl-peptidase 3
Identifiers
Symbols	DPP3 ; DPPIII; FLJ11387; FLJ22331
External IDs	Template:OMIM5 Template:MGI HomoloGene: 40210
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
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/a	n/a
PubMed search	n/a	n/a

Dipeptidyl-peptidase 3, also known as DPP3, is a human gene.

This gene encodes a protein that is a member of the S9B family in clan SC of the serine proteases. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH) and has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. Increased activity of this protein is associated with endometrial and ovarian cancers. Alternate transcriptional splice variants have been characterized.

Further reading

• Kar NC, Pearson CM (1978). "Dipeptidyl peptidases in human muscle disease". Clin. Chim. Acta. 82 (1–2): 185–92. PMID 618680.
• Grdisa M, Vitale L (1991). "Types and localization of aminopeptidases in different human blood cells". Int. J. Biochem. 23 (3): 339–45. PMID 2044841.
• Swanson AA, Davis RM, Meinhardt NC (1985). "Proteases in human lenses and their possible significance". Curr. Eye Res. 4 (1): 43–8. PMID 2858361.CS1 maint: Multiple names: authors list (link)
• Vanha-Perttula T (1989). "Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: origin and biochemical properties". Clin. Chim. Acta. 177 (2): 179–95. PMID 2906822.
• Shimamori Y, Watanabe Y, Fujimoto Y (1989). "Human placental dipeptidyl aminopeptidase III: hydrolysis of enkephalins and its stimulation by cobaltous ion". Biochem. Med. Metab. Biol. 40 (3): 305–10. PMID 3233187.CS1 maint: Multiple names: authors list (link)
• Abramić M, Zubanović M, Vitale L (1988). "Dipeptidyl peptidase III from human erythrocytes". Biol. Chem. Hoppe-Seyler. 369 (1): 29–38. PMID 3348886.CS1 maint: Multiple names: authors list (link)
• Shimamori Y, Watanabe Y, Fujimoto Y (1987). "Purification and characterization of dipeptidyl aminopeptidase III from human placenta". Chem. Pharm. Bull. 34 (8): 3333–40. PMID 3791505.CS1 maint: Multiple names: authors list (link)
• Swanson AA, Davis RM, McDonald JK (1984). "Dipeptidyl peptidase III of human cataractous lenses. Partial purification". Curr. Eye Res. 3 (2): 287–91. PMID 6368131.CS1 maint: Multiple names: authors list (link)
• Jones TH, Kapralou A (1982). "A rapid assay for dipeptidyl aminopeptidase III in human erythrocytes". Anal. Biochem. 119 (2): 418–23. PMID 7041700.
• Vitale L, Zubanović M, Abramić M (1982). "Properties and distribution of aminopeptidase and dipeptidyl aminopeptidase III of human erythrocytes". Acta Biol. Med. Ger. 40 (10–11): 1489–95. PMID 7044004.CS1 maint: Multiple names: authors list (link)
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fukasawa K, Fukasawa KM, Kanai M; et al. (1998). "Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression". Biochem. J. 329 ( Pt 2): 275–82. PMID 9425109.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Simaga S, Babić D, Osmak M; et al. (1998). "Dipeptidyl peptidase III in malignant and non-malignant gynaecological tissue". Eur. J. Cancer. 34 (3): 399–405. PMID 9640230.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Akiyama T, Harada S, Kojima F; et al. (1998). "Fluostatins A and B, new inhibitors of dipeptidyl peptidase III, produced by Streptomyces sp. TA-3391. I. Taxonomy of producing strain, production, isolation, physico-chemical properties and biological properties". J. Antibiot. 51 (6): 553–9. PMID 9711218.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fukasawa K, Fukasawa KM, Iwamoto H; et al. (1999). "The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme". Biochemistry. 38 (26): 8299–303. doi:10.1021/bi9904959. PMID 10387075.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fukasawa KM, Fukasawa K, Harada M (2000). "Assignment of the dipeptidyl peptidase III gene (DPP3) to human chromosome 11 band q12-->q13.1 by in situ hybridization". Cytogenet. Cell Genet. 88 (1–2): 99–100. PMID 10773679.CS1 maint: Multiple names: authors list (link)
• Hashimoto J, Yamamoto Y, Kurosawa H; et al. (2000). "Identification of dipeptidyl peptidase III in human neutrophils". Biochem. Biophys. Res. Commun. 273 (2): 393–7. doi:10.1006/bbrc.2000.2827. PMID 10873616.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Abramić M, Schleuder D, Dolovcak L; et al. (2001). "Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences". Biol. Chem. 381 (12): 1233–43. PMID 11209758.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)