DPP7

Dipeptidyl-peptidase 7
Rendering based on PDB 3JYH.
Available structures PDB 3JYH, 3N0T
Identifiers
Symbols	DPP7; DPP2; DPPII; QPP
External IDs	OMIM: 610537 MGI: 1933213 HomoloGene: 22748 GeneCards: DPP7 Gene
EC number	3.4.14.2
Gene Ontology Molecular function • aminopeptidase activity • protein binding • peptidase activity • serine-type peptidase activity • dipeptidyl-peptidase activity Cellular component • extracellular region • lysosome • cytosol • cytoplasmic membrane-bounded vesicle Biological process • proteolysis Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	29952	83768
Ensembl	ENSG00000176978	ENSMUSG00000026958
UniProt	Q9UHL4	Q8R082
RefSeq (mRNA)	XM_001130451	NM_031843.2
RefSeq (protein)	XP_001130451	NP_114031.2
Location (UCSC)	Chr 9: 140 – 140.01 Mb	Chr 2: 25.21 – 25.21 Mb
PubMed search	[1]	[2]

Dipeptidyl-peptidase 2 is an enzyme that in humans is encoded by the DPP7 gene.^[1][2][3]

The protein encoded by this gene is a post-proline cleaving aminopeptidase expressed in quiescent lymphocytes. The resting lymphocytes are maintained through suppression of apoptosis, a state which is disrupted by inhibition of this novel serine protease. The enzyme has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH.^[3]

References

1. ^ Chiravuri M, Schmitz T, Yardley K, Underwood R, Dayal Y, Huber BT (Oct 1999). "A novel apoptotic pathway in quiescent lymphocytes identified by inhibition of a post-proline cleaving aminodipeptidase: a candidate target protease, quiescent cell proline dipeptidase". J Immunol 163 (6): 3092–9. PMID 10477574. 
2. ^ Fukasawa KM, Fukasawa K, Higaki K, Shiina N, Ohno M, Ito S, Otogoto J, Ota N (Jan 2001). "Cloning and functional expression of rat kidney dipeptidyl peptidase II". Biochem J 353 (Pt 2): 283–90. doi:10.1042/0264-6021:3530283. PMC 1221570. PMID 11139392. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1221570. 
3. ^ ^{a b} "Entrez Gene: DPP7 dipeptidyl-peptidase 7". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=29952. 

Further reading

• Fornas E, Mayordomo F, Renau-Piqueras J, Alborch E (1992). "Effect of cholesterol and its autooxidation derivatives on endocytosis and dipeptidyl peptidases of aortic endothelial cells". Histol. Histopathol. 7 (2): 163–8. PMID 1515698. 
• Roberts VJ, Gorenstein C (1990). "The effect of antimitotic agents on the intraneuronal distribution of lysosomes". Brain Res. 521 (1–2): 62–72. doi:10.1016/0006-8993(90)91525-L. PMID 2207678. 
• Andersen KJ, McDonald JK (1989). "Lysosomal heterogeneity of dipeptidyl peptidase II active on collagen-related peptides". Ren. Physiol. Biochem. 12 (1): 32–40. PMID 2727382. 
• Demuth HU, Schlenzig D, Schierhorn A et al. (1993). "Design of (omega-N-(O-acyl)hydroxy amid) aminodicarboxylic acid pyrrolidides as potent inhibitors of proline-specific peptidases". FEBS Lett. 320 (1): 23–7. doi:10.1016/0014-5793(93)81649-K. PMID 8096464. 
• Underwood R, Chiravuri M, Lee H et al. (1999). "Sequence, purification, and cloning of an intracellular serine protease, quiescent cell proline dipeptidase". J. Biol. Chem. 274 (48): 34053–8. doi:10.1074/jbc.274.48.34053. PMID 10567372. 
• Chiravuri M, Agarraberes F, Mathieu SL et al. (2000). "Vesicular localization and characterization of a novel post-proline-cleaving aminodipeptidase, quiescent cell proline dipeptidase". J. Immunol. 165 (10): 5695–702. PMID 11067927. 
• Araki H, Li Y, Yamamoto Y et al. (2001). "Purification, molecular cloning, and immunohistochemical localization of dipeptidyl peptidase II from the rat kidney and its identity with quiescent cell proline dipeptidase". J. Biochem. 129 (2): 279–88. PMID 11173530. 
• Zhan H, Yamamoto Y, Shumiya S et al. (2002). "Peptidases play an important role in cataractogenesis: an immunohistochemical study on lenses derived from Shumiya cataract rats". Histochem. J. 33 (9–10): 511–21. doi:10.1023/A:1014943522613. PMID 12005022. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Leiting B, Pryor KD, Wu JK et al. (2003). "Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII". Biochem. J. 371 (Pt 2): 525–32. doi:10.1042/BJ20021643. PMC 1223300. PMID 12529175. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223300. 
• Lehner B, Sanderson CM (2004). "A Protein Interaction Framework for Human mRNA Degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442147. 
• 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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.