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MGP000532

UniProt Annotations

Entry Information

Gene Name	cathepsin C
Protein Entry	CATC_HUMAN
UniProt ID	P53634
Species	Human

Comments

Comment type	Description
Alternative Products	Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P53634-1; Sequence=Displayed; Name=2; IsoId=P53634-2; Sequence=VSP_039123, VSP_039124; Name=3; IsoId=P53634-3; Sequence=VSP_043232, VSP_043233; Note=No experimental confirmation available.;
Biophysicochemical Properties	pH dependence: High activity at pH 4.5-6.8. {ECO:0000269\|PubMed:1586157};
Catalytic Activity	Release of an N-terminal dipeptide, Xaa-Yaa-\|- Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.
Cofactor	Name=chloride; Xref=ChEBI:CHEBI:17996; Note=Binds 1 Cl(-) ion per heavy chain.;
Disease	Haim-Munk syndrome (HMS) [MIM:245010]: An autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis. {ECO:0000269\|PubMed:10662807}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Disease	Papillon-Lefevre syndrome (PLS) [MIM:245000]: An autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees. {ECO:0000269\|PubMed:10581027, ECO:0000269\|PubMed:10662808, ECO:0000269\|PubMed:11106356, ECO:0000269\|PubMed:11158173, ECO:0000269\|PubMed:11180012, ECO:0000269\|PubMed:11180601, ECO:0000269\|PubMed:11886537, ECO:0000269\|PubMed:12112662, ECO:0000269\|PubMed:12809647, ECO:0000269\|PubMed:14974080, ECO:0000269\|PubMed:15108292, ECO:0000269\|PubMed:15991336}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Disease	Periodontititis, aggressive, 1 (AP1) [MIM:170650]: A disease characterized by severe and protracted gingival infections, generalized or localized, leading to tooth loss. Amounts of microbial deposits are generally inconsistent with the severity of periodontal tissue destruction and the progression of attachment and bone loss may be self arresting. {ECO:0000269\|PubMed:10662808, ECO:0000269\|PubMed:14974080}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Enzyme Regulation	Strongly inhibited by the cysteine peptidase inhibitors mersalyl acid, iodoacetic acid and cystatin. Inhibited by N-ethylmaleimide, Gly-Phe-diazomethane, TLCK, TPCK and, at low pH, by dithiodipyridine. Not inhibited by the serine peptidase inhibitor PMSF, the aminopeptidase inhibitor bestatin, or metal ion chelators. {ECO:0000269\|PubMed:1586157}.
Function	Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII. {ECO:0000269\|PubMed:1586157}.
Induction	Up-regulated in lymphocytes by IL2/interleukin-2. {ECO:0000269\|PubMed:9092576}.
Interaction	O76096:CST7; NbExp=2; IntAct=EBI-1047323, EBI-2807448;
Ptm	In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond.
Ptm	N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes. {ECO:0000269\|PubMed:11726493, ECO:0000269\|PubMed:1586157, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:19167329, ECO:0000269\|PubMed:9507095}.
Sequence Caution	Sequence=CAD97897.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Similarity	Belongs to the peptidase C1 family. {ECO:0000255\|PROSITE-ProRule:PRU10088, ECO:0000255\|PROSITE- ProRule:PRU10089, ECO:0000255\|PROSITE-ProRule:PRU10090}.
Subcellular Location	Lysosome.
Subunit	Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains. {ECO:0000269\|PubMed:11726493, ECO:0000269\|PubMed:1586157}.
Tissue Specificity	Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas. {ECO:0000269\|PubMed:9092576}.
Web Resource	Name=CTSCbase; Note=CTSC mutation db; URL="http://structure.bmc.lu.se/idbase/CTSCbase/";