| Nomenclature | Genomic Location |
| Symbol | Ctsc | Chromosome | 1 |
| Name | Cathepsin C | Linkage map | unknown |
| Species | Dracomimus familiaris | Genome Coordinates | 1: 3 Mbp |
| Molecular Function |
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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.
Molecular Function Terms:
binding
ion binding
anion binding
protein binding
protein self-association
catalytic activity
hydrolase activity
peptidase activity
peptidase activity, acting on L-amino acid peptides
cysteine-type peptidase activity
cysteine-type endopeptidase activity
endopeptidase activity
cysteine-type endopeptidase activity
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| Human Disease Association |
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Defects in CTSC are a cause of Papillon-Lefevre syndrome (PLS) [MIM:245000];
also known as keratosis palmoplantaris with periodontopathia. PLS is 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.
Defects in CTSC are a cause of Haim-Munk syndrome (HMS) [MIM:245010]; also known
as keratosis palmoplantaris with periodontopathia and onychogryposis or Cochin
Jewish disorder. HMS is an autosomal recessive disorder characterized by palmoplantar
keratosis, onychogryphosis and periodontitis. Additional features are pes planus,
arachnodactyly, and acroosteolysis.
Defects in CTSC are a cause of aggressive periodontititis type 1 (AP1) [MIM:170650];
also known as juvenile periodontitis (JPD) and prepubertal periodontitis (PPP).
AP1 is characterized by severe and protracted gingival infections, leading to
tooth loss. AP1 inheritance is autosomal dominant.
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1 CCGGGACGCCTCGCGCCTTTCACGTGTCTCCTCCTCCTCTTCTTCCAGCTGAACCCGGGT
61 GCGGCCGACACGCCGGCCAACTGCACCTATGAAGACCTGCAAGGCTCCTGGGTCTTCCAG
121 GTGGGTCGGGGCCAGGCGGGTCCCTACCGGCGCATTAACTGCTCCGATCCTGGACCGGTG
181 GAAGGGGAAATAACTGTGACCCTTCAAAAACTCGATGTCGCCCAGGACAGTCTAGGGAAC
241 TACGGCTTCTTCACACTAATATACAACCAAGGCTTTGAGGTTGTGTTGAACAACTACAAG
301 TGGTTTGCATTTTTTAAGTATAAAGAAGAAGGCTCCAATGTAACCAGTTACTGCCATGAA
361 ACTTTACCAGGATGGGTCCATGATGTGCTAGGCCATAATTGGGCATGTTTCACTGGACAT
421 AAGATCTCCCCTTCTCCCTCTAGTGTTCGTGTAAATCAGCTGCCTTTTGGGAAACCACAC
481 AGAAAATCTCTGCAGAAGACCTATGTCAACAATTTCGACTTCGTGAAAGCCATCAACACT
541 GTCCAGAAGTCATGGAAGGCAACAACCTATGAGGAATATGAAGCCCTCACCTTAGAAGAT
601 ATTGTTCGGAGAGCTGGTGGATTGAGTTCCAGATTTCCAAGGCCCAAACCTGCTCCTCTG
661 ACAGCAGATGTGATCAAAGAAGTTTATAGTCTGCCAAAATCGTGGGACTGGAGGAATGTG
721 AATGGTGTGAATTATGTCAGCCCAGTACGAAACCAAGCATCCTGTGGCAGCTGCTATGCC
781 TTTGCCTCCATGGGCATGCTGGAAAGTAGGATTCGTATCCTCACTAACAATTCACAGACT
841 CCAACACTCAGCCCCCAAAAGGTTGTGTCCTGCAGTCAGTATTCCCAAGGTTGTGATGGA
901 GGGTTCCCTTACCTTATTGCTGGCAAATACGCTCAGGATTTTGGTGTGGTTGAAGAGGAC
961 TGCTTCCCTTACACAGCCACGGATTCCCCTTGCAATTTTACGCACAGCTGTTACCACTAT
1021 TATGCCACTAACTACTACTATGTTGGTGGGTTTTATGGTGGATGCAATGAAGCTCTAATG
1081 AAACTGGAACTTGTGAAGCATGGACCCATGGCCGTTGCTTTTGAAGTATATAGTGACTTC
1141 ATGCATTACAGAGGGGGGATCTACCATCACACGGGGCTGATGGATCCATTCAATCCTTTT
1201 GAATTGACCAATCACGCTGTCCTCCTGGTGGGTTATGGTACTGACCCAGAGACCGGGGAG
1261 CCCTTCTGGATTGTGAAGAACAGCTGGGGACCCGCTTGGGGTGAGCAGGGTTACTTCAGG
1321 ATCCGCAGAGGCACGGATGAATGTGCCATAGAAAGCATAGCAGTGGCTTCCACCCCAATT
1381 CCTAAATTGTAA
| Predicted Protein Product |
PGRLAPFTCLLLLFFQLNPGAADTPANCTYEDLQGSWVFQVGRGQAGPYRRINCSDPGPV
EGEITVTLQKLDVAQDSLGNYGFFTLIYNQGFEVVLNNYKWFAFFKYKEEGSNVTSYCHE
TLPGWVHDVLGHNWACFTGHKISPSPSSVRVNQLPFGKPHRKSLQKTYVNNFDFVKAINT
VQKSWKATTYEEYEALTLEDIVRRAGGLSSRFPRPKPAPLTADVIKEVYSLPKSWDWRNV
NGVNYVSPVRNQASCGSCYAFASMGMLESRIRILTNNSQTPTLSPQKVVSCSQYSQGCDG
GFPYLIAGKYAQDFGVVEEDCFPYTATDSPCNFTHSCYHYYATNYYYVGGFYGGCNEALM
KLELVKHGPMAVAFEVYSDFMHYRGGIYHHTGLMDPFNPFELTNHAVLLVGYGTDPETGE
PFWIVKNSWGPAWGEQGYFRIRRGTDECAIESIAVASTPIPKL
| Protein Alignment to Mouse |
sp|P97821|CATC_MOUSE Dipeptidyl peptidase 1 OS=Mus musculus GN=Ctsc PE=2 SV=1
MGI:109553 Ctsc cathepsin C (Chr 7)
Length = 462
Score = 1679 (596.1 bits), Expect = 1.8e-173, P = 1.8e-173
Identities = 306/454 (67%), Positives = 349/454 (76%)
Query: 10 LLLLFFQLNPGAADTPANCTYEDLQGSWVFQVGRGQAGPYRRINCSDPGPVEGEITVTLQ 69
LLL+ + +DTPANCTY DL G+WVFQVG + INCS E ++ V L+
Sbjct: 12 LLLVLLGVCTVRSDTPANCTYPDLLGTWVFQVGPRSSRS--DINCSVMEATEEKVVVHLK 69
Query: 70 KLDVAQDSLGNYGFFTLIYNQGFEVVLNNYKWFAFFKYKEEGSNVTSYCHETLPGWVHDV 129
KLD A D LGN G FTLIYNQGFE+VLN+YKWFAFFKY+ G SYCHET+ GWVHDV
Sbjct: 70 KLDTAYDELGNSGHFTLIYNQGFEIVLNDYKWFAFFKYEVRGHTAISYCHETMTGWVHDV 129
Query: 130 LGHNWACFTGHKISPSPSSVRVNQLPFGKPHRKSLQKTYVNNFDFVKAINTVQKSWKXXX 189
LG NWACF G K+ V +N G + ++ Y +N +FVKAINTVQKSW
Sbjct: 130 LGRNWACFVGKKVESHIEKVNMNAAHLGGLQERYSERLYTHNHNFVKAINTVQKSWTATA 189
Query: 190 XXXXXXXXXXDIVRRAGGLSSRFPRPKPAPLTADVIKEVYSLPKSWDWRNVNGVNYVSPV 249
D++RR+G S R PRPKPAP+T ++ +++ +LP+SWDWRNV GVNYVSPV
Sbjct: 190 YKEYEKMSLRDLIRRSGH-SQRIPRPKPAPMTDEIQQQILNLPESWDWRNVQGVNYVSPV 248
Query: 250 RNQASCGSCYAFASMGMLESRIRILTNNSQTPTLSPQKVVSCSQYSQGCDGGFPYLIAGK 309
RNQ SCGSCY+FASMGMLE+RIRILTNNSQTP LSPQ+VVSCS Y+QGCDGGFPYLIAGK
Sbjct: 249 RNQESCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSPYAQGCDGGFPYLIAGK 308
Query: 310 YAQDFGVVEEDCFPYTATDSPCNFTHSCYHYYATNYYYVGGFYGGCNEALMKLELVKHGP 369
YAQDFGVVEE CFPYTA DSPC +C YY+++YYYVGGFYGGCNEALMKLELVKHGP
Sbjct: 309 YAQDFGVVEESCFPYTAKDSPCKPRENCLRYYSSDYYYVGGFYGGCNEALMKLELVKHGP 368
Query: 370 MAVAFEVYSDFMHYRGGIYHHTGLMDPFNPFELTNHAVLLVGYGTDPETGEPFWIVKNSW 429
MAVAFEV+ DF+HY GIYHHTGL DPFNPFELTNHAVLLVGYG DP TG +WI+KNSW
Sbjct: 369 MAVAFEVHDDFLHYHSGIYHHTGLSDPFNPFELTNHAVLLVGYGRDPVTGIEYWIIKNSW 428
Query: 430 GPAWGEQGYFRIRRGTDECAIESIAVASTPIPKL 463
G WGE GYFRIRRGTDECAIESIAVA+ PIPKL
Sbjct: 429 GSNWGESGYFRIRRGTDECAIESIAVAAIPIPKL 462
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