Chymotrypsin-C

CTRC
Identifiers
Aliases	CTRC, CLCR, ELA4, chymotrypsin C
External IDs	OMIM: 601405; MGI: 1923951; GeneCards: CTRC
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4H4F
Enzyme activity
Gene location (Human)
Chr.	Chromosome 1 (human)
End	15,449,242 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	141,573,670 bp
RNA expression pattern
	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
	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
Databases	NCBI: entry; OMA: entry
	11330
	76701
	ENSG00000162438
	ENSMUSG00000062478
	Q99895
	Q3SYP2
	NM_007272
	NM_001033875
	NP_009203
	NP_001029047
	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. This enzyme is primarily produced in the pancreas by acinar cells, where it is involved in regulating the activation of digestive enzymes like trypsins and carboxypeptidases.

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. In other words, it is involved in breaking peptide bonds in proteins. It catalyzes the preferential cleavage of peptide bonds from the following amino acids:

Leu┼, Tyr┼, Phe┼, Met┼, Trp┼, Gln┼, Asn┼

This is enzyme activity is similar to chymotrypsin A/B (EC 3.4.21.1), but with some differences such as a preference for breaking leucine over phenylalanine bonds.

A protein with similar enzyme activity can also be formed from pig chymotrypsinogen C and cattle subunit II of procarboxypeptidase A.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000162438 – Ensembl, May 2017
1 2 3 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.
1 2 "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.
↑ "Q99895 · CTRC_HUMAN". uniprot.org. UniProt consortium. Retrieved 2026-08-01.
↑ EC 3.4.21.2
↑ Peanasky RJ, Gratecos D, Baratti J, Rovery M (May 1969). "Mode of activation of N-terminal sequence of subunit II in bovine procarboxypeptidase A and of porcine chymotrypsinogen C". Biochimica et Biophysica Acta (BBA) - Protein Structure. 181 (1): 82–92. doi:10.1016/0005-2795(69)90229-3. PMID 5792601.
↑ Folk, J.E. (1970). "Chymotrypsin C (Porcine pancreas)". Proteolytic Enzymes. Methods in Enzymology. Vol. 19. pp. 109–112. doi:10.1016/0076-6879(70)19008-2. ISBN 9780121818814.
↑ Wilcox PE (1970). "Chymotrypsinogens—chymotrypsins". Proteolytic Enzymes. Methods in Enzymology. Vol. 19. pp. 64–108. doi:10.1016/0076-6879(70)19007-0. ISBN 9780121818814.

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.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000162438 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[entrez-5] 1 2 "Entrez Gene: chymotrypsin C (caldecrin)".

[pmid8635596-6] 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.

[7] "Q99895 · CTRC_HUMAN". uniprot.org. UniProt consortium. Retrieved 2026-08-01.

[8] EC 3.4.21.2

[9] Peanasky RJ, Gratecos D, Baratti J, Rovery M (May 1969). "Mode of activation of N-terminal sequence of subunit II in bovine procarboxypeptidase A and of porcine chymotrypsinogen C". Biochimica et Biophysica Acta (BBA) - Protein Structure. 181 (1): 82–92. doi:10.1016/0005-2795(69)90229-3. PMID 5792601.

[10] Folk, J.E. (1970). "Chymotrypsin C (Porcine pancreas)". Proteolytic Enzymes. Methods in Enzymology. Vol. 19. pp. 109–112. doi:10.1016/0076-6879(70)19008-2. ISBN 9780121818814.

[11] Wilcox PE (1970). "Chymotrypsinogens—chymotrypsins". Proteolytic Enzymes. Methods in Enzymology. Vol. 19. pp. 64–108. doi:10.1016/0076-6879(70)19007-0. ISBN 9780121818814.

v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue-type plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Chymotrypsin-C

Function

See also

References

Further reading