Chymotrypsin C is a member of the peptidase S1 family. The encoded protein is a serum calcium-decreasing factor that has chymotrypsin-like protease activity.[5]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000162438 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000062478 – 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.
^Tomomura A, Akiyama M, Itoh H, Yoshino I, Tomomura M, Nishii Y, Noikura T, Saheki T (May 1996). "Molecular cloning and expression of human caldecrin". FEBS Lett. 386 (1): 26–8. doi:10.1016/0014-5793(96)00377-8. PMID 8635596.
Further readingedit
Freeman TC, Davies R, Calam J (1990). "Interactions of pancreatic secretory trypsin inhibitor in small intestinal juice: its hydrolysis and protection by intraluminal factors". Clin. Chim. Acta. 195 (1–2): 27–39. doi:10.1016/0009-8981(90)90191-T. PMID 2093478.
Masson E, Chen JM, Scotet V, et al. (2008). "Association of rare chymotrypsinogen C (CTRC) gene variations in patients with idiopathic chronic pancreatitis". Hum. Genet. 123 (1): 83–91. doi:10.1007/s00439-007-0459-3. PMID 18172691. S2CID 20466442.
Rosendahl J, Witt H, Szmola R, et al. (2008). "Chymotrypsin C (CTRC) alterations that diminish activity or secretion are associated with chronic pancreatitis". Nat. Genet. 40 (1): 78–82. doi:10.1038/ng.2007.44. PMC2650829. PMID 18059268.
Kitahara K, Kawa S, Katsuyama Y, et al. (2008). "Microsatellite scan identifies new candidate genes for susceptibility to alcoholic chronic pancreatitis in Japanese patients". Dis. Markers. 25 (3): 175–80. doi:10.1155/2008/426764. PMC3827802. PMID 19096130.
Stavridi ES, O'Malley K, Lukacs CM, et al. (1996). "Structural change in alpha-chymotrypsin induced by complexation with alpha 1-antichymotrypsin as seen by enhanced sensitivity to proteolysis". Biochemistry. 35 (33): 10608–15. doi:10.1021/bi9605806. PMID 8718849.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
Chang MC, Chang YT, Wei SC, et al. (2009). "Association of novel chymotrypsin C gene variations and haplotypes in patients with chronic pancreatitis in Chinese in Taiwan". Pancreatology. 9 (3): 287–92. doi:10.1159/000199437. PMID 19407484. S2CID 25853177.
Yoshino-Yasuda I, Kobayashi K, Akiyama M, et al. (1998). "Caldecrin is a novel-type serine protease expressed in pancreas, but its homologue, elastase IV, is an artifact during cloning derived from caldecrin gene". J. Biochem. 123 (3): 546–54. doi:10.1093/oxfordjournals.jbchem.a021971. PMID 9538241.
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. PMC528928. PMID 15489334.
Harris WR, Malencik DA, Johnson CM, et al. (1990). "Purification and characterization of catalytic fragments of phosphorylase kinase gamma subunit missing a calmodulin-binding domain". J. Biol. Chem. 265 (20): 11740–5. doi:10.1016/S0021-9258(19)38460-1. PMID 2365696.
Derikx MH, Szmola R, te Morsche RH, et al. (2009). "Tropical calcific pancreatitis and its association with CTRC and SPINK1 (p.N34S) variants". Eur J Gastroenterol Hepatol. 21 (8): 889–94. doi:10.1097/MEG.0b013e32832183cf. PMID 19404200. S2CID 22812634.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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.
Szmola R; Sahin-Tóth M (2007). "Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: Identity with Rinderknecht's enzyme Y". Proc. Natl. Acad. Sci. U.S.A. 104 (27): 11227–32. Bibcode:2007PNAS..10411227S. doi:10.1073/pnas.0703714104. PMC2040881. PMID 17592142.
Brecher AS, Yang MP (1998). "Acetaldehyde inhibits chymotrypsin and serum anti-chymotrypsin activity". J. Investig. Med. 46 (4): 146–52. PMID 9635374.
This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.
chymotrypsin, chymotrypsin, also, known, caldecrin, elastase, enzyme, that, humans, encoded, ctrc, gene, ctrcavailable, structurespdbortholog, search, pdbe, rcsblist, codes4h4fidentifiersaliasesctrc, clcr, ela4, chymotrypsin, cexternal, idsomim, 601405, 192395. Chymotrypsin C also known as caldecrin or elastase 4 is an enzyme that in humans is encoded by the CTRC gene 5 6 CTRCAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes4H4FIdentifiersAliasesCTRC CLCR ELA4 chymotrypsin CExternal IDsOMIM 601405 MGI 1923951 HomoloGene 21422 GeneCards CTRCGene location Human Chr Chromosome 1 human 1 Band1p36 21Start15 438 442 bp 1 End15 449 242 bp 1 Gene location Mouse Chr Chromosome 4 mouse 2 Band4 4 D3Start141 565 550 bp 2 End141 573 670 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inbody of pancreasislet of Langerhanspancreatic epithelial cellpancreatic ductal cellright coronary arteryright lobe of liverfunduscanal of the cervixleft uterine tubespleenTop expressed inpyloric antrumpancreasislet of Langerhansmoruladuodenumspleenthymuslarge intestinecolonleft colonMore reference expression dataBioGPSn aGene ontologyMolecular functionpeptidase activity serine type peptidase activity serine type endopeptidase activity protein binding hydrolase activityCellular componentextracellular regionBiological processcobalamin metabolic process proteolysisSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez1133076701EnsemblENSG00000162438ENSMUSG00000062478UniProtQ99895Q3SYP2RefSeq mRNA NM 007272NM 001033875RefSeq protein NP 009203NP 001029047Location UCSC Chr 1 15 44 15 45 MbChr 4 141 57 141 57 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseFunction editChymotrypsin C is a member of the peptidase S1 family The encoded protein is a serum calcium decreasing factor that has chymotrypsin like protease activity 5 References edit a b c GRCh38 Ensembl release 89 ENSG00000162438 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000062478 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 a b Entrez Gene chymotrypsin C caldecrin Tomomura A Akiyama M Itoh H Yoshino I Tomomura M Nishii Y Noikura T Saheki T May 1996 Molecular cloning and expression of human caldecrin FEBS Lett 386 1 26 8 doi 10 1016 0014 5793 96 00377 8 PMID 8635596 Further reading editFreeman TC Davies R Calam J 1990 Interactions of pancreatic secretory trypsin inhibitor in small intestinal juice its hydrolysis and protection by intraluminal factors Clin Chim Acta 195 1 2 27 39 doi 10 1016 0009 8981 90 90191 T PMID 2093478 Masson E Chen JM Scotet V et al 2008 Association of rare chymotrypsinogen C CTRC gene variations in patients with idiopathic chronic pancreatitis Hum Genet 123 1 83 91 doi 10 1007 s00439 007 0459 3 PMID 18172691 S2CID 20466442 Rosendahl J Witt H Szmola R et al 2008 Chymotrypsin C CTRC alterations that diminish activity or secretion are associated with chronic pancreatitis Nat Genet 40 1 78 82 doi 10 1038 ng 2007 44 PMC 2650829 PMID 18059268 Kitahara K Kawa S Katsuyama Y et al 2008 Microsatellite scan identifies new candidate genes for susceptibility to alcoholic chronic pancreatitis in Japanese patients Dis Markers 25 3 175 80 doi 10 1155 2008 426764 PMC 3827802 PMID 19096130 Stavridi ES O Malley K Lukacs CM et al 1996 Structural change in alpha chymotrypsin induced by complexation with alpha 1 antichymotrypsin as seen by enhanced sensitivity to proteolysis Biochemistry 35 33 10608 15 doi 10 1021 bi9605806 PMID 8718849 Gregory SG Barlow KF McLay KE et al 2006 The DNA sequence and biological annotation of human chromosome 1 Nature 441 7091 315 21 Bibcode 2006Natur 441 315G doi 10 1038 nature04727 PMID 16710414 Chang MC Chang YT Wei SC et al 2009 Association of novel chymotrypsin C gene variations and haplotypes in patients with chronic pancreatitis in Chinese in Taiwan Pancreatology 9 3 287 92 doi 10 1159 000199437 PMID 19407484 S2CID 25853177 Yoshino Yasuda I Kobayashi K Akiyama M et al 1998 Caldecrin is a novel type serine protease expressed in pancreas but its homologue elastase IV is an artifact during cloning derived from caldecrin gene J Biochem 123 3 546 54 doi 10 1093 oxfordjournals jbchem a021971 PMID 9538241 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 Harris WR Malencik DA Johnson CM et al 1990 Purification and characterization of catalytic fragments of phosphorylase kinase gamma subunit missing a calmodulin binding domain J Biol Chem 265 20 11740 5 doi 10 1016 S0021 9258 19 38460 1 PMID 2365696 Derikx MH Szmola R te Morsche RH et al 2009 Tropical calcific pancreatitis and its association with CTRC and SPINK1 p N34S variants Eur J Gastroenterol Hepatol 21 8 889 94 doi 10 1097 MEG 0b013e32832183cf PMID 19404200 S2CID 22812634 Strausberg RL Feingold EA Grouse LH et al 2002 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 Szmola R Sahin Toth M 2007 Chymotrypsin C caldecrin promotes degradation of human cationic trypsin Identity with Rinderknecht s enzyme Y Proc Natl Acad Sci U S A 104 27 11227 32 Bibcode 2007PNAS 10411227S doi 10 1073 pnas 0703714104 PMC 2040881 PMID 17592142 Brecher AS Yang MP 1998 Acetaldehyde inhibits chymotrypsin and serum anti chymotrypsin activity J Investig Med 46 4 146 52 PMID 9635374 nbsp This article on a gene on human chromosome 1 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Chymotrypsin C amp oldid 1081535676, wikipedia, wiki, book, books, library,
