DPP7

DPP7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3JYH, 3N0T, 4EBB
Identifiers
Aliases	DPP7, DPP2, DPPII, QPP, dipeptidyl peptidase 7
External IDs	OMIM: 610537 MGI: 1933213 HomoloGene: 22748 GeneCards: DPP7
Gene location (Human) Chr. Chromosome 9 (human) Band 9q34.3 Start 137,110,546 bp End 137,115,177 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 A3 Start 25,242,288 bp End 25,246,371 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in anterior pituitary right uterine tube right lobe of thyroid gland left lobe of thyroid gland Brodmann area 9 minor salivary glands cingulate gyrus body of stomach right coronary artery skin of abdomen Top expressed in yolk sac calvaria proximal tubule kidney iris islet of Langerhans corneal stroma blastocyst morula ciliary body More reference expression data BioGPS n/a
Gene ontology Molecular function peptidase activity hydrolase activity aminopeptidase activity serine-type peptidase activity dipeptidyl-peptidase activity Cellular component cytosol Golgi apparatus lysosome cytoplasmic vesicle vesicle intracellular membrane-bounded organelle extracellular exosome extracellular region azurophil granule lumen Biological process neutrophil degranulation proteolysis Sources:Amigo / QuickGO
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: 137.11 – 137.12 Mb Chr 2: 25.24 – 25.25 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Dipeptidyl-peptidase 2 is an enzyme that in humans is encoded by the DPP7 gene.

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 prolyl carboxypeptidase and is active at both acidic and neutral pH.

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. S2CID 10381435.
• 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, Grosche G, Chapotchartier M, Gripon J (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. S2CID 24505098.
• Underwood R, Chiravuri M, Lee H, Schmitz T, Kabcenell AK, Yardley K, Huber BT (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, Lee H, Huber BT (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, Haneda M, Nishi K, Kikkawa R, Ohkubo I (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, Kunimatsu M, Nishi K, Ohkubo I, Kani K (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. S2CID 29588226.
• Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (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.
• Leiting B, Pryor KD, Wu JK, Marsilio F, Patel RA, Craik CS, Ellman JA, Cummings RT, Thornberry NA (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, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R (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.