Reviewed,
UniProtKB/Swiss-Prot Q99895 (CTRC_HUMAN)
Last modified
June 16, 2009.
Version 81.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Chymotrypsin-C EC=3.4.21.2 Alternative name(s): Caldecrin | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 268 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Has chymotrypsin-type protease activity and hypocalcemic activity. |
| Catalytic activity | Preferential cleavage: Leu-|-Xaa, Tyr-|-Xaa, Phe-|-Xaa, Met-|-Xaa, Trp-|-Xaa, Gln-|-Xaa, Asn-|-Xaa. |
| Tissue specificity | Pancreas. |
| Involvement in disease | Variations in CTRC influence susceptibility to chronic pancreatitis [MIM:167800]. Chronic pancreatitis is a persistent inflammatory disorder characterized by permanent destruction of the pancreatic parenchyma. |
| Sequence similarities | Belongs to the peptidase S1 family. Elastase subfamily. Contains 1 peptidase S1 domain. |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Polymorphism |
| Domain | Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Gene Ontology (GO) | |
| Biological process | proteolysis Ref.1 Traceable author statement. Source: ProtInc |
| Molecular function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 16 | 16 | Potential | ||||||||
| Propeptide | 17 – 29 | 13 | Activation peptide | PRO_0000027713 | |||||||
| Chain | 30 – 268 | 239 | Chymotrypsin-C | PRO_0000027714 | |||||||
Regions | |||||||||||
| Domain | 30 – 267 | 238 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 74 | 1 | Charge relay system By similarity | ||||||||
| Active site | 121 | 1 | Charge relay system By similarity | ||||||||
| Active site | 216 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 25 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 52 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 226 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 17 ↔ 141 | By similarity | |||||||||
| Disulfide bond | 59 ↔ 75 | By similarity | |||||||||
| Disulfide bond | 155 ↔ 222 | By similarity | |||||||||
| Disulfide bond | 186 ↔ 202 | By similarity | |||||||||
| Disulfide bond | 212 ↔ 243 | By similarity | |||||||||
Natural variations | |||||||||||
| Natural variant | 35 | 1 | D → H Ref.6 | VAR_043516 | |||||||
| Natural variant | 35 | 1 | D → N Ref.6 | VAR_043517 | |||||||
| Natural variant | 37 | 1 | R → Q Normal secretion and activity. Ref.6 | VAR_043518 | |||||||
| Natural variant | 48 | 1 | Q → R Reduced secretion and activity. Ref.6 | VAR_043519 | |||||||
| Natural variant | 73 | 1 | A → T Reduced secretion; abolishes activity. Ref.6 | VAR_043520 | |||||||
| Natural variant | 80 | 1 | R → W Ref.1 | VAR_010928 | |||||||
| Natural variant | 172 | 1 | K → E: dbSNP rs34949635. Ref.6 | VAR_043521 | |||||||
| Natural variant | 217 | 1 | G → R Ref.6 | VAR_043522 | |||||||
| Natural variant | 217 | 1 | G → S Reduced secretion and activity. Ref.6 | VAR_043523 | |||||||
| Natural variant | 218 | 1 | G → S Ref.6 | VAR_043524 | |||||||
| Natural variant | 220 | 1 | L → R Ref.6 | VAR_043525 | |||||||
| Natural variant | 225 | 1 | E → A Ref.6 | VAR_043526 | |||||||
| Natural variant | 235 | 1 | V → I Slightly reduced secretion and activity. Ref.6 | VAR_043527 | |||||||
| Natural variant | 249 | 1 | P → L Ref.6 | VAR_043528 | |||||||
| Natural variant | 254 | 1 | R → W Reduced secretion; normal activity. Ref.6 | VAR_043529 | |||||||
| Natural variant | 260 | 1 | D → N Ref.6 | VAR_043530 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 16 | 1 | S → T in AAB47104. Ref.1 | ||||||||
| Sequence conflict | 52 | 1 | N → D in CAA74031. Ref.4 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning and expression of human caldecrin." Tomomura A., Akiyama M., Itoh H., Yoshino I., Tomomura M., Nishii Y., Noikura T., Saheki T. FEBS Lett. 386:26-28(1996) [PubMed: 8635596] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TRP-80. Tissue: Pancreas. |
| [2] | "The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R.Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas. |
| [4] | "A human pancreatic chymotrypsin: biochemical and molecular characterization." Sziegoleit A. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-268. Tissue: Pancreas. |
| [5] | "Caldecrin is a novel-type serine protease expressed in pancreas, but its homologue, elastase IV, is an artifact during cloning derived from caldecrin gene." Yoshino-Yasuda I., Kobayashi K., Akiyama M., Itoh H., Tomomura A., Saheki T. J. Biochem. 123:546-554(1998) [PubMed: 9538241] [Abstract] Cited for: CHARACTERIZATION. |
| [6] | "Chymotrypsin C (CTRC) variants that diminish activity or secretion are associated with chronic pancreatitis." Rosendahl J., Witt H., Szmola R., Bhatia E., Ozsvari B., Landt O., Schulz H.-U., Gress T.M., Pfuetzer R., Loehr M., Kovacs P., Blueher M., Stumvoll M., Choudhuri G., Hegyi P., te Morsche R.H.M., Drenth J.P.H., Truninger K. Sahin-Toth M.Nat. Genet. 40:78-82(2008) [PubMed: 18059268] [Abstract] Cited for: VARIANTS HIS-35; ASN-35; GLN-37; ARG-48; THR-73; GLU-172; SER-217; ARG-217; SER-218; ARG-220; ALA-225; ILE-235; LEU-249; TRP-254 AND ASN-260, CHARACTERIZATION OF VARIANTS GLN-37; ARG-48; THR-73; SER-217; ILE-235 AND TRP-254, INVOLVEMENT IN CHRONIC PANCREATITIS. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| S82198 mRNA. Translation: AAB47104.2. Sequence problems. AL031283 Genomic DNA. Translation: CAB77355.1. BC015118 mRNA. Translation: AAH15118.1. Y13697 mRNA. Translation: CAA74031.1. | |
| IPI | IPI00018553. |
| PIR | S68825. S68826. |
| RefSeq | NP_009203.2. |
| UniGene | Hs.631869 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1PYT based on UniProtKB P05805. |
| SMR | Q99895. Positions 17-268. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S01.157. |
Genome annotation databases | |
| Ensembl | ENSG00000162438. Homo sapiens. [Contig view] |
| GeneID | 11330. |
| KEGG | hsa:11330. |
| NMPDR | fig|9606.3.peg.354. |
Organism-specific databases | |
| GeneCards | GC01P015637. |
| H-InvDB | HIX0000151. |
| HGNC | HGNC:2523. CTRC. |
| MIM | 167800. phenotype. 601405. gene. |
| Orphanet | 676. Pancreatitis, hereditary. |
| PharmGKB | PA27024. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | Q99895. |
| HOVERGEN | Q99895. |
| OMA | Q99895. CISNTRT. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.2. 247. |
Gene expression databases | |
| ArrayExpress | Q99895. |
| Bgee | Q99895. |
| CleanEx | HS_CTRC. |
| GermOnline | ENSG00000162438. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view] |
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| PROSITE | PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 43039. |
| SOURCE | Search... |
Entry information
| Entry name | CTRC_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q99895 Secondary accession number(s): O00765, Q9NUH5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 1 Human chromosome 1: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


