P53634A8K7V2B5MDD5Q2HIY8Q53G93Q71E75Q71E76Q7M4N9Q7Z3G7Q7Z5U7Q8WY99Q8WYA7Q8WYA8CATC_HUMANDipeptidyl peptidase 13.4.14.1Cathepsin CCathepsin JDipeptidyl peptidase IDPP-IDPPIDipeptidyl transferaseDipeptidyl peptidase 1 exclusion domain chainDipeptidyl peptidase I exclusion domain chainDipeptidyl peptidase 1 heavy chainDipeptidyl peptidase I heavy chainDipeptidyl peptidase 1 light chainDipeptidyl peptidase I light chainCTSCCPPIHomo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoMolecular cloning and sequence analysis of human preprocathepsin C.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)VARIANT THR-153Human dipeptidyl-peptidase I. Gene characterization, localization, and expression.NUCLEOTIDE SEQUENCE [GENOMIC DNA]INDUCTIONTISSUE SPECIFICITYVARIANT THR-153Cathepsin C gene: first compound heterozygous patient with Papillon-Lefevre syndrome and a novel symptomless mutation.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)VARIANTS PLS TYR-236; ARG-286 AND TYR-291VARIANT THR-153A genetic study of cathepsin C gene in two families with Papillon-Lefevre syndrome.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)VARIANT THR-153VARIANT PLS HIS-294Complete sequencing and characterization of 21,243 full-length human cDNAs.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2)VARIANT THR-153NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)VARIANT THR-153The full-ORF clone resource of the German cDNA consortium.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)Human chromosome 11 DNA sequence and analysis including novel gene identification.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]VARIANT THR-153The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3)Stoichiometry and heterogeneity of the pro-region chain in tetrameric human cathepsin C.PROTEIN SEQUENCE OF 25-71; 122-143; 231-235 AND 395-399CHARACTERIZATION OF EXCLUSION DOMAINGLYCOSYLATIONOligomeric structure and substrate induced inhibition of human cathepsin C.PROTEIN SEQUENCE OF 25-34; 231-239 AND 395-404SUBCELLULAR LOCATIONThe residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme.PROTEIN SEQUENCE OF 25-28; 51-61; 114-117 AND 133-139CHARACTERIZATION OF EXCLUSION DOMAINDISULFIDE BONDSPurification and characterization of dipeptidyl peptidase I from human spleen.PROTEIN SEQUENCE OF 231-290; 310-328 AND 340-383FUNCTIONCATALYTIC ACTIVITYACTIVITY REGULATIONBIOPHYSICOCHEMICAL PROPERTIESSUBUNITGLYCOSYLATIONVARIANT THR-153Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I.FUNCTIONCotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.GLYCOSYLATION AT ASN-29; ASN-53; ASN-119 AND ASN-276Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53Initial characterization of the human central proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]N-terminome analysis of the human mitochondrial proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases.X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 25-143 AND 231-463 IN COMPLEX WITH CHLORIDE IONSSUBUNITDISULFIDE BONDSGLYCOSYLATION AT ASN-29Loss-of-function mutations in the cathepsin C gene result in periodontal disease and palmoplantar keratosis.VARIANTS PLS PHE-249; LEU-252; PRO-272; SER-301; CYS-339 AND CYS-347Haim-Munk syndrome and Papillon-Lefevre syndrome are allelic mutations in cathepsin C.VARIANT HMS ARG-286Localisation of a gene for prepubertal periodontitis to chromosome 11q14 and identification of a cathepsin C gene mutation.VARIANTS PLS CYS-339 AND CYS-340VARIANT AP1 CYS-347Identification of cathepsin C mutations in ethnically diverse Papillon-Lefevre syndrome patients.VARIANTS PLS 67-TYR--ALA-74 DEL; PRO-272; SER-300; VAL-301; SER-301; ASN-304; GLY-319; CYS-339; CYS-340 AND GLY-447VARIANT THR-153Papillon-Lefevre syndrome: mutations and polymorphisms in the cathepsin C gene.VARIANTS PLS SER-39 AND SER-301VARIANT VAL-453Novel point mutations, deletions, and polymorphisms in the cathepsin C gene in nine families from Europe and North Africa with Papillon-Lefevre syndrome.VARIANTS PLS PRO-127; PRO-272; CYS-339 AND CYS-429VARIANTS THR-153 AND LYS-401Evidence of a founder effect for four cathepsin C gene mutations in Papillon-Lefevre syndrome patients.VARIANTS PLS PRO-272 AND ASP-300Biochemical and mutational analyses of the cathepsin c gene (CTSC) in three North American families with Papillon Lefevre syndrome.VARIANTS PLS ARG-139 AND PRO-272VARIANT THR-153The role of cathepsin C in Papillon-Lefevre syndrome, prepubertal periodontitis, and aggressive periodontitis.VARIANTS PLS GLU-129; ARG-139; TYR-236; PHE-249; LEU-252; HIS-272; SER-301; ARG-312; CYS-339; CYS-347 AND GLY-447VARIANTS AP1 HIS-272 AND CYS-412VARIANT THR-153Loss-of-function mutations in cathepsin C in two families with Papillon-Lefevre syndrome are associated with deficiency of serine proteinases in PMNs.VARIANT PLS ASN-405Gene symbol: CTSC. Disease: Papillon-Lefevre syndrome.VARIANT PLS ARG-405ERRATUM OF PUBMED:15991336Proxy molecular diagnosis from whole-exome sequencing reveals Papillon-Lefevre syndrome caused by a missense mutation in CTSC.VARIANT PLS ASP-300Thiol protease (PubMed:1586157). Has dipeptidylpeptidase activity (PubMed:1586157). Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids (PubMed:1586157). Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate (PubMed:1586157). Can act as both an exopeptidase and endopeptidase (PubMed:1586157). Activates serine proteases such as elastase, cathepsin G and granzymes A and B (PubMed:8428921).Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.chlorideBinds 1 Cl(-) ion per heavy chain.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.High activity at pH 4.5-6.8.Tetramer of heterotrimers consisting of exclusion domain, heavy- and light chains.P53634O76096false2P53634G5E9A7false3P53634Q7Z699false3LysosomeP53634-11P53634-22P53634-33Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas.Up-regulated in lymphocytes by IL2/interleukin-2.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.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.Papillon-Lefevre syndrome
PLS
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.The disease is caused by variants affecting the gene represented in this entry.Haim-Munk syndrome
HMS
An autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.The disease is caused by variants affecting the gene represented in this entry.Periodontititis, aggressive, 1
AP1
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.The disease is caused by variants affecting the gene represented in this entry.Belongs to the peptidase C1 family.Extended N-terminus.CTSC mutation db3D-structureAlternative splicingChlorideDirect protein sequencingDisease variantDisulfide bondGlycoproteinHydrolaseLysosomePalmoplantar keratodermaProteaseReference proteomeSignalThiol proteaseZymogenchloridechloridechlorideYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKDVTDFISHLFMQLGTVGIYDLPHLRNKLAMNRRWGYKEEGSKVTTYCNETMTGWVHDVLGRNWACFDVTDFISHLFMQLGTVGIYDLPHLRNKLVIKWSHPVEGRITDYVFQLRHRPQRCYYHGDGSGSGVYNQREGRCYCYCEKHNHRYCWCEGIVKIWVCSCMHRVYDYVYMGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL
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