DPP3

Dipeptidyl-peptidase 3 is an enzyme that in humans is encoded by the DPP3 gene.^[5][6]

DPP3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3FVY, 3T6B, 3T6J, 5E2Q, 5EHH, 5E33, 5E3C, 5E3A, 5EGY
Identifiers
Aliases	DPP3, DPPIII, dipeptidyl peptidase 3
External IDs	OMIM: 606818; MGI: 1922471; HomoloGene: 40210; GeneCards: DPP3; OMA:DPP3 - orthologs
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q13.2 Start 66,480,013 bp[1] End 66,509,657 bp[1]
Gene location (Mouse) Chr. Chromosome 19 (mouse)[2] Band 19|19 A Start 4,957,257 bp[2] End 4,978,315 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in mucosa of transverse colon oocyte rectum islet of Langerhans secondary oocyte granulocyte mucosa of pharynx mucosa of esophagus stromal cell of endometrium right adrenal gland Top expressed in yolk sac lip primitive streak epiblast esophagus neural tube lacrimal gland right kidney embryo ventricular zone More reference expression data BioGPS n/a
Gene ontology Molecular function zinc ion binding peptidase activity aminopeptidase activity protein binding hydrolase activity metallopeptidase activity dipeptidyl-peptidase activity metal ion binding Cellular component plasma membrane extracellular exosome cytoplasm nuclear speck cytosol Biological process proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10072 75221 Ensembl ENSG00000254986 ENSMUSG00000063904 UniProt Q9NY33 Q99KK7 RefSeq (mRNA) NM_130443 NM_001256670 NM_005700 NM_133803 NM_001360711 RefSeq (protein) NP_001243599 NP_005691 NP_569710 NP_598564 NP_001347640 Location (UCSC) Chr 11: 66.48 – 66.51 Mb Chr 19: 4.96 – 4.98 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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.^[7]

Dipeptidyl-peptidase 3 has been found to act as a myocardial depressant factor. Procizumab, a specific antibody for dipeptidyl-peptidase 3, was found to improve cardiac and renal function in a mouse model of heart failure. ^[8] In human studies, higher levels of circulating DPP3 protein in cardiogenic shock patients indicated a more severe disease course, with a higher risk of refractory cardiogenic shock and death.^{[9] [10]}

References

1. GRCh38: Ensembl release 89: ENSG00000254986 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000063904 – 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. Fukasawa KM, Fukasawa K, Harada M (Jun 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. doi:10.1159/000015498. PMID 10773679. S2CID 202603.
6. "DPP3 dipeptidyl peptidase 3 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2019-05-16.
7. "DPP3 dipeptidyl peptidase 3 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2019-05-16.
8. Deniau, Benjamin; Rehfeld, Linda; Santos, Karine; Dienelt, Anke; Azibani, Feriel; Sadoune, Malha; Kounde, Paul R.; Samuel, Jane L.; Tolpannen, Heli; Lassus, Johan; Harjola, Veli-Pekka; Vodovar, Nicolas; Bergmann, Andreas; Hartmann, Oliver; Mebazaa, Alexandre (February 2020). "Circulating dipeptidyl peptidase 3 is a myocardial depressant factor: dipeptidyl peptidase 3 inhibition rapidly and sustainably improves haemodynamics". European Journal of Heart Failure. 22 (2): 290–299. doi:10.1002/ejhf.1601. ISSN 1388-9842. PMID 31472040.
9. Harjola, Veli-Pekka; Lassus, Johan; Sionis, Alessandro; Køber, Lars; Tarvasmäki, Tuukka; Spinar, Jindrich; Parissis, John; Banaszewski, Marek; Silva-Cardoso, Jose; Carubelli, Valentina; Di Somma, Salvatore; Tolppanen, Heli; Zeymer, Uwe; Thiele, Holger; Nieminen, Markku S (May 2015). "Clinical picture and risk prediction of short-term mortality in cardiogenic shock". European Journal of Heart Failure. 17 (5): 501–509. doi:10.1002/ejhf.260. hdl:11573/910722. ISSN 1388-9842. PMID 25820680.
10. Takagi, Koji; Blet, Alice; Levy, Bruno; Deniau, Benjamin; Azibani, Feriel; Feliot, Elodie; Bergmann, Andreas; Santos, Karine; Hartmann, Oliver; Gayat, Etienne; Mebazaa, Alexandre; Kimmoun, Antoine (February 2020). "Circulating dipeptidyl peptidase 3 and alteration in haemodynamics in cardiogenic shock: results from the OptimaCC trial". European Journal of Heart Failure. 22 (2): 279–286. doi:10.1002/ejhf.1600. ISSN 1388-9842. PMID 31472039.

Further reading

• Kar NC, Pearson CM (1978). "Dipeptidyl peptidases in human muscle disease". Clin. Chim. Acta. 82 (1–2): 185–92. doi:10.1016/0009-8981(78)90042-6. PMID 618680.
• Grdisa M, Vitale L (1991). "Types and localization of aminopeptidases in different human blood cells". Int. J. Biochem. 23 (3): 339–45. doi:10.1016/0020-711X(91)90116-5. PMID 2044841.
• Swanson AA, Davis RM, Meinhardt NC (1985). "Proteases in human lenses and their possible significance". Curr. Eye Res. 4 (1): 43–8. doi:10.3109/02713688508999965. PMID 2858361.
• 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. doi:10.1016/0009-8981(88)90140-4. 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. doi:10.1016/0885-4505(88)90133-8. PMID 3233187.
• Abramić M, Zubanović M, Vitale L (1988). "Dipeptidyl peptidase III from human erythrocytes". Biol. Chem. Hoppe-Seyler. 369 (1): 29–38. doi:10.1515/bchm3.1988.369.1.29. PMID 3348886.
• Shimamori Y, Watanabe Y, Fujimoto Y (1987). "Purification and characterization of dipeptidyl aminopeptidase III from human placenta". Chem. Pharm. Bull. 34 (8): 3333–40. doi:10.1248/cpb.34.3333. PMID 3791505.
• Swanson AA, Davis RM, McDonald JK (1984). "Dipeptidyl peptidase III of human cataractous lenses. Partial purification". Curr. Eye Res. 3 (2): 287–91. doi:10.3109/02713688408997211. PMID 6368131.
• Jones TH, Kapralou A (1982). "A rapid assay for dipeptidyl aminopeptidase III in human erythrocytes". Anal. Biochem. 119 (2): 418–23. doi:10.1016/0003-2697(82)90607-8. 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.
• 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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• 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) (Pt 2): 275–82. doi:10.1042/bj3290275. PMC 1219041. PMID 9425109.
• 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. doi:10.1016/S0959-8049(97)00401-2. PMID 9640230.
• 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. doi:10.7164/antibiotics.51.553. PMID 9711218.
• 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.
• 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.
• 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. doi:10.1515/BC.2000.151. PMID 11209758. S2CID 22245963.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

External links

• DPP3 human gene location in the UCSC Genome Browser.
• DPP3 human gene details in the UCSC Genome Browser.