DPP7
| Dipeptidyl-peptidase 7 | |||||||||||||
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 Rendering based on PDB 3JYH. | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | DPP7 ; DPP2; DPPII; QPP | ||||||||||||
| External IDs | OMIM: 610537 MGI: 1933213 HomoloGene: 22748 IUPHAR: 1605 ChEMBL: 3976 GeneCards: DPP7 Gene | ||||||||||||
| EC number | 3.4.14.2 | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 29952 | 83768 | |||||||||||
| Ensembl | ENSG00000176978 | ENSMUSG00000026958 | |||||||||||
| UniProt | Q9UHL4 | Q9ET22 | |||||||||||
| RefSeq (mRNA) | NM_013379 | NM_031843 | |||||||||||
| RefSeq (protein) | NP_037511 | NP_114031 | |||||||||||
| Location (UCSC) | Chr 9: 140 – 140.01 Mb | Chr 2: 25.35 – 25.36 Mb | |||||||||||
| PubMed search | |||||||||||||
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
- ↑ 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.
- ↑ 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.
- ↑ 3.0 3.1 "Entrez Gene: DPP7 dipeptidyl-peptidase 7".
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. doi:10.1159/000173177. 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. doi:10.4049/jimmunol.165.10.5695. 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. doi:10.1093/oxfordjournals.jbchem.a002855. 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.
- 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.
- 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.
- 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.