Chymotrypsin-C

CTRC
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4H4F
Identifiers
Aliases	CTRC , CLCR, ELA4, chymotrypsin C
External IDs	OMIM: 601405; MGI: 1923951; HomoloGene: 21422; GeneCards: CTRC; OMA:CTRC - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1p36.21 Start 15,438,442 bp [1] End 15,449,242 bp [1]
Gene location (Mouse) Chr. Chromosome 4 (mouse) [2] Band 4|4 D3 Start 141,565,550 bp [2] End 141,573,670 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas islet of Langerhans pancreatic epithelial cell beta cell pancreatic ductal cell right coronary artery ectocervix Descending thoracic aorta granulocyte right lobe of liver Top expressed in pyloric antrum pancreas islet of Langerhans embryo embryo morula duodenum blastocyst mesenteric lymph nodes spleen More reference expression data BioGPS n/a
Gene ontology Molecular function peptidase activity serine-type peptidase activity serine-type endopeptidase activity protein binding hydrolase activity Cellular component extracellular region Biological process cobalamin metabolic process proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 11330 76701 Ensembl ENSG00000162438 ENSMUSG00000062478 UniProt Q99895 Q3SYP2 RefSeq (mRNA) NM_007272 NM_001033875 RefSeq (protein) NP_009203 NP_001029047 Location (UCSC) Chr 1: 15.44 – 15.45 Mb Chr 4: 141.57 – 141.57 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Chymotrypsin C, also known as caldecrin or elastase 4, is an enzyme that in humans is encoded by the CTRC gene. ^{[5] [6]}

Function

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]

References

1. GRCh38: Ensembl release 89: ENSG00000162438 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000062478 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: chymotrypsin C (caldecrin)".
6. 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

• 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. 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-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 . 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.