DPP3

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
Gene location (Human)
Chr.	Chromosome 11 (human)[1]
End	66,509,657 bp[1]
Gene location (Mouse)
Chr.	Chromosome 19 (mouse)[2]
End	4,928,287 bp[2]
Gene ontology
Molecular function	• zinc ion binding; • peptidase activity; • aminopeptidase activity; • GO:0001948 protein binding; • hydrolase activity; • metallopeptidase activity; • dipeptidyl-peptidase activity; • metal ion binding;
Cellular component	• cell membrane; • extracellular exosome; • cytoplasm; • nuclear speck; • cytosol;
Biological process	• proteolysis;
	Sources:Amigo / QuickGO
Orthologs
	10072
	75221
	ENSG00000254986
	ENSMUSG00000063904
	Q9NY33
	Q99KK7
	NM_130443; NM_001256670; NM_005700
	NM_133803; NM_001360711
	NP_001243599; NP_005691; NP_569710
	NP_598564; NP_001347640
	Wikidata
View/Edit Human	View/Edit Mouse

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

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]

References

GRCh38: Ensembl release 89: ENSG00000254986 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000063904 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
"DPP3 dipeptidyl peptidase 3 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2019-05-16.
"DPP3 dipeptidyl peptidase 3 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2019-05-16.

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. 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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000254986 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid10773679-5] 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.

DPP3

References

Further reading

External links