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.[7]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000176978 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000026958 - 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.
^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. doi:10.4049/jimmunol.163.6.3092. 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. PMC1221570. PMID 11139392.
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. PMC139241. 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. PMC1223300. 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. PMC442147. 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. PMC528928. PMID 15489334.
This article on a gene on human chromosome 9 is a stub. You can help Wikipedia by expanding it.
dpp7, dipeptidyl, peptidase, enzyme, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes3jyh, 3n0t, 4ebbidentifiersaliases, dpp2, dppii, dipeptidyl, peptidase, 7external, idsomim, 610537, 1933213, homologene, 22748, gen. Dipeptidyl peptidase 2 is an enzyme that in humans is encoded by the DPP7 gene 5 6 7 DPP7Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes3JYH 3N0T 4EBBIdentifiersAliasesDPP7 DPP2 DPPII QPP dipeptidyl peptidase 7External IDsOMIM 610537 MGI 1933213 HomoloGene 22748 GeneCards DPP7Gene location Human Chr Chromosome 9 human 1 Band9q34 3Start137 110 546 bp 1 End137 115 177 bp 1 Gene location Mouse Chr Chromosome 2 mouse 2 Band2 2 A3Start25 242 288 bp 2 End25 246 371 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inanterior pituitaryright uterine tuberight lobe of thyroid glandleft lobe of thyroid glandBrodmann area 9minor salivary glandcingulate gyrusbody of stomachright coronary arteryskin of abdomenTop expressed inyolk saccalvariaproximal tubulekidneyirisislet of Langerhanscorneal stromablastocystmorulaciliary bodyMore reference expression dataBioGPSn aGene ontologyMolecular functionpeptidase activity hydrolase activity aminopeptidase activity serine type peptidase activity dipeptidyl peptidase activityCellular componentcytosol Golgi apparatus lysosome cytoplasmic vesicle vesicle intracellular membrane bounded organelle extracellular exosome extracellular region azurophil granule lumenBiological processneutrophil degranulation proteolysisSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez2995283768EnsemblENSG00000176978ENSMUSG00000026958UniProtQ9UHL4Q9ET22RefSeq mRNA NM 013379NM 031843RefSeq protein NP 037511NP 114031Location UCSC Chr 9 137 11 137 12 MbChr 2 25 24 25 25 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseThe 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 7 References edit a b c GRCh38 Ensembl release 89 ENSG00000176978 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000026958 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 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 doi 10 4049 jimmunol 163 6 3092 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 a b Entrez Gene DPP7 dipeptidyl peptidase 7 Further reading editFornas 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 nbsp This article on a gene on human chromosome 9 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title DPP7 amp oldid 1199393783, wikipedia, wiki, book, books, library,
