Cathepsin S

Details

Name
Cathepsin S
Synonyms
  • 3.4.22.27
Gene Name
CTSS
Organism
Humans
Amino acid sequence
>lcl|BSEQ0003265|Cathepsin S
MKRLVCVLLVCSSAVAQLHKDPTLDHHWHLWKKTYGKQYKEKNEEAVRRLIWEKNLKFVM
LHNLEHSMGMHSYDLGMNHLGDMTSEEVMSLMSSLRVPSQWQRNITYKSNPNRILPDSVD
WREKGCVTEVKYQGSCGACWAFSAVGALEAQLKLKTGKLVSLSAQNLVDCSTEKYGNKGC
NGGFMTTAFQYIIDNKGIDSDASYPYKAMDQKCQYDSKYRAATCSKYTELPYGREDVLKE
AVANKGPVSVGVDARHPSFFLYRSGVYYEPSCTQNVNHGVLVVGYGDLNGKEYWLVKNSW
GHNFGEEGYIRMARNKGNHCGIASFPSYPEI
Number of residues
331
Molecular Weight
37495.49
Theoretical pI
8.45
GO Classification
Functions
collagen binding / cysteine-type endopeptidase activity / fibronectin binding / laminin binding / proteoglycan binding
Processes
adaptive immune response / antigen processing and presentation / antigen processing and presentation of exogenous peptide antigen via MHC class I / antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent / antigen processing and presentation of exogenous peptide antigen via MHC class II / antigen processing and presentation of peptide antigen / antigen processing and presentation of peptide antigen via MHC class I / basement membrane disassembly / cellular response to thyroid hormone stimulus / collagen catabolic process / extracellular matrix disassembly / extracellular matrix organization / immune response / innate immune response / positive regulation of cation channel activity / positive regulation of inflammatory response / protein processing / proteolysis / proteolysis involved in cellular protein catabolic process / response to acidic pH / toll-like receptor signaling pathway
Components
endolysosome lumen / extracellular region / extracellular space / intracellular membrane-bounded organelle / lysosomal lumen / lysosome / membrane
General Function
Proteoglycan binding
Specific Function
Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Lysosome
Gene sequence
>lcl|BSEQ0019157|Cathepsin S (CTSS)
ATGAAACGGCTGGTTTGTGTGCTCTTGGTGTGCTCCTCTGCAGTGGCACAGTTGCATAAA
GATCCTACCCTGGATCACCACTGGCATCTCTGGAAGAAAACCTATGGCAAACAATACAAG
GAAAAGAATGAAGAAGCAGTACGACGTCTCATCTGGGAAAAGAATCTAAAGTTTGTGATG
CTTCACAACCTGGAGCATTCAATGGGAATGCACTCATACGATCTGGGCATGAACCACCTG
GGAGACATGGGTTCTTGTGGTGCTTGCTGGGCTTTCAGTGCTGTGGGGGCCCTGGAAGCA
CAGCTGAAGCTGAAAACAGGAAAGCTGGTGTCTCTCAGTGCCCAGAACCTGGTGGATTGC
TCAACTGAAAAATATGGAAACAAAGGCTGCAATGGTGGCTTCATGACAACGGCTTTCCAG
TACATCATTGATAACAAGGGCATCGACTCAGACGCTTCCTATCCCTACAAAGCCATGGAT
CAGAAATGTCAATATGACTCAAAATATCGTGCTGCCACATGTTCAAAGTACACTGAACTT
CCTTATGGCAGAGAAGATGTCCTGAAAGAAGCTGTGGCCAATAAAGGCCCAGTGTCTGTT
GGTGTAGATGCGCGTCATCCTTCTTTCTTCCTCTACAGAAGTGGTGTCTACTATGAACCA
TCCTGTACTCAGAATGTGAATCATGGTGTACTTGTGGTTGGCTATGGTGATCTTAATGGG
AAAGAATACTGGCTTGTGAAAAACAGCTGGGGCCACAACTTTGGTGAAGAAGGATATATT
CGGATGGCAAGAAATAAAGGAAATCATTGTGGGATTGCTAGCTTTCCCTCTTACCCAGAA
ATCTAG
Chromosome Location
1
Locus
1q21
External Identifiers
ResourceLink
UniProtKB IDP25774
UniProtKB Entry NameCATS_HUMAN
GenBank Protein ID248406
GenBank Gene IDS93414
GenAtlas IDCTSS
HGNC IDHGNC:2545
General References
  1. Shi GP, Munger JS, Meara JP, Rich DH, Chapman HA: Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. J Biol Chem. 1992 Apr 15;267(11):7258-62. [Article]
  2. Wiederanders B, Bromme D, Kirschke H, von Figura K, Schmidt B, Peters C: Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S. J Biol Chem. 1992 Jul 5;267(19):13708-13. [Article]
  3. Shi GP, Webb AC, Foster KE, Knoll JH, Lemere CA, Munger JS, Chapman HA: Human cathepsin S: chromosomal localization, gene structure, and tissue distribution. J Biol Chem. 1994 Apr 15;269(15):11530-6. [Article]
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  10. Fengler A, Brandt W: Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics. Protein Eng. 1998 Nov;11(11):1007-13. [Article]
  11. Turkenburg JP, Lamers MB, Brzozowski AM, Wright LM, Hubbard RE, Sturt SL, Williams DH: Structure of a Cys25-->Ser mutant of human cathepsin S. Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):451-5. Epub 2002 Feb 21. [Article]
  12. Inagaki H, Tsuruoka H, Hornsby M, Lesley SA, Spraggon G, Ellman JA: Characterization and optimization of selective, nonpeptidic inhibitors of cathepsin S with an unprecedented binding mode. J Med Chem. 2007 May 31;50(11):2693-9. Epub 2007 May 1. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03767Morpholine-4-Carboxylic Acid [1s-(2-Benzyloxy-1r-Cyano-Ethylcarbamoyl)-3-Methyl-Butyl]AmideexperimentalunknownDetails
DB03837Morpholine-4-Carboxylic Acid (1-(3-Benzenesulfonyl-1-Phenethylallylcarbamoyl)-3-Methylbutyl)-AmideexperimentalunknownDetails
DB03984Morpholine-4-Carboxylic Acid [1-(2-Benzylsulfanyl-1-Formyl-Ethylcarbamoyl)-2-Phenyl-Ethyl]-AmideexperimentalunknownDetails
DB07520N-[1-(AMINOMETHYL)CYCLOPROPYL]-3-(MORPHOLIN-4-YLSULFONYL)-N~2~-[(1S)-2,2,2-TRIFLUORO-1-(4-FLUOROPHENYL)ETHYL]-L-ALANINAMIDEexperimentalunknownDetails
DB07587N-(1-CYANOCYCLOPROPYL)-3-({[(2S)-5-OXOPYRROLIDIN-2-YL]METHYL}SULFONYL)-N~2~-[(1S)-2,2,2-TRIFLUORO-1-(4-FLUOROPHENYL)ETHYL]-L-ALANINAMIDEexperimentalunknownDetails
DB07589N-[1-(AMINOMETHYL)CYCLOPROPYL]-3-(BENZYLSULFONYL)-N~2~-[(1S)-2,2,2-TRIFLUORO-1-(4-HYDROXYPHENYL)ETHYL]-L-ALANINAMIDEexperimentalunknownDetails
DB07839N~2~-1,3-BENZOXAZOL-2-YL-3-CYCLOHEXYL-N-{2-[(4-METHOXYPHENYL)AMINO]ETHYL}-L-ALANINAMIDEexperimentalunknownDetails
DB07878N-[(1S)-1-{1-[(1R,3E)-1-ACETYLPENT-3-EN-1-YL]-1H-1,2,3-TRIAZOL-4-YL}-1,2-DIMETHYLPROPYL]BENZAMIDEexperimentalunknownDetails
DB08195(1R)-2-[(CYANOMETHYL)AMINO]-1-({[2-(DIFLUOROMETHOXY)BENZYL]SULFONYL}METHYL)-2-OXOETHYL MORPHOLINE-4-CARBOXYLATEexperimentalunknownDetails
DB086112-[(2',3',4'-TRIFLUOROBIPHENYL-2-YL)OXY]ETHANOLexperimentalunknownDetails
DB08752N-[(1S)-2-[(4-cyano-1-methylpiperidin-4-yl)amino]-1-(cyclohexylmethyl)-2-oxoethyl]morpholine-4-carboxamideexperimentalunknownDetails
DB08755N-[(1S)-2-{[(1R)-2-(benzyloxy)-1-cyano-1-methylethyl]amino}-1-(cyclohexylmethyl)-2-oxoethyl]morpholine-4-carboxamideexperimentalunknownDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails