Cathepsin S

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Cathepsin S
PDB rendering based on 1glo.
Available structures: 1glo, 1ms6, 1npz, 1nqc, 2c0y, 2f1g, 2fq9, 2fra, 2frq, 2ft2, 2fud, 2fye, 2g6d, 2g7y, 2h7j, 2hh5, 2hhn, 2hxz, 2op3
Identifiers
Symbol(s) CTSS; MGC3886
External IDs OMIM: 116845 MGI: 107341 HomoloGene: 20867
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 1520 13040
Ensembl ENSG00000163131 ENSMUSG00000038642
Uniprot P25774 Q3U5K1
Refseq NM_004079 (mRNA)
NP_004070 (protein)		 NM_021281 (mRNA)
NP_067256 (protein)
Location Chr 1: 148.97 - 149.01 Mb Chr 3: 95.61 - 95.64 Mb
Pubmed search [1] [2]

Cathepsin S, also known as CTSS, is a human gene.[1]

The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that may participate in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. The encoded protein can function as an elastase over a broad pH range in alveolar macrophages. Transcript variants utilizing alternative polyadenylation signals exist for this gene.[1]

[edit] See also

[edit] References

  1. ^ a b Entrez Gene: CTSS cathepsin S.

[edit] Further reading

  • Shi GP, Munger JS, Meara JP, et al. (1992). "Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease.". J. Biol. Chem. 267 (11): 7258–62. PMID 1373132. 
  • Wiederanders B, Brömme D, Kirschke H, et al. (1992). "Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S.". J. Biol. Chem. 267 (19): 13708–13. PMID 1377692. 
  • Ritonja A, Colić A, Dolenc I, et al. (1991). "The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L.". FEBS Lett. 283 (2): 329–31. PMID 2044774. 
  • Munger JS, Haass C, Lemere CA, et al. (1995). "Lysosomal processing of amyloid precursor protein to A beta peptides: a distinct role for cathepsin S.". Biochem. J. 311 ( Pt 1): 299–305. PMID 7575468. 
  • Lemere CA, Munger JS, Shi GP, et al. (1995). "The lysosomal cysteine protease, cathepsin S, is increased in Alzheimer's disease and Down syndrome brain. An immunocytochemical study.". Am. J. Pathol. 146 (4): 848–60. PMID 7717452. 
  • Hall A, Håkansson K, Mason RW, et al. (1995). "Structural basis for the biological specificity of cystatin C. Identification of leucine 9 in the N-terminal binding region as a selectivity-conferring residue in the inhibition of mammalian cysteine peptidases.". J. Biol. Chem. 270 (10): 5115–21. PMID 7890620. 
  • Balbín M, Hall A, Grubb A, et al. (1994). "Structural and functional characterization of two allelic variants of human cystatin D sharing a characteristic inhibition spectrum against mammalian cysteine proteinases.". J. Biol. Chem. 269 (37): 23156–62. PMID 8083219. 
  • Shi GP, Webb AC, Foster KE, et al. (1994). "Human cathepsin S: chromosomal localization, gene structure, and tissue distribution.". J. Biol. Chem. 269 (15): 11530–6. PMID 8157683. 
  • Turk B, Stoka V, Turk V, et al. (1996). "High-molecular-weight kininogen binds two molecules of cysteine proteinases with different rate constants.". FEBS Lett. 391 (1-2): 109–12. PMID 8706894. 
  • Baumgrass R, Williamson MK, Price PA (1997). "Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S.". J. Bone Miner. Res. 12 (3): 447–55. PMID 9076588. 
  • Würl P, Taubert H, Meye A, et al. (1997). "Immunohistochemical and clinical evaluation of cathepsin expression in soft tissue sarcomas.". Virchows Arch. 430 (3): 221–5. PMID 9099979. 
  • Gelb BD, Shi GP, Heller M, et al. (1997). "Structure and chromosomal assignment of the human cathepsin K gene.". Genomics 41 (2): 258–62. doi:10.1006/geno.1997.4631. PMID 9143502. 
  • Baldassare JJ, Henderson PA, Tarver A, Fisher GJ (1997). "Thrombin activation of human platelets dissociates a complex containing gelsolin and actin from phosphatidylinositide-specific phospholipase Cgamma1.". Biochem. J. 324 ( Pt 1): 283–7. PMID 9164868. 
  • Nissler K, Kreusch S, Rommerskirch W, et al. (1998). "Sorting of non-glycosylated human procathepsin S in mammalian cells.". Biol. Chem. 379 (2): 219–24. PMID 9524075. 
  • Claus V, Jahraus A, Tjelle T, et al. (1998). "Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages. Enrichment of cathepsin H in early endosomes.". J. Biol. Chem. 273 (16): 9842–51. PMID 9545324. 
  • Schick C, Pemberton PA, Shi GP, et al. (1998). "Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis.". Biochemistry 37 (15): 5258–66. doi:10.1021/bi972521d. PMID 9548757. 
  • Fengler A, Brandt W (1999). "Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics.". Protein Eng. 11 (11): 1007–13. PMID 9876921. 
  • Söderström M, Salminen H, Glumoff V, et al. (1999). "Cathepsin expression during skeletal development.". Biochim. Biophys. Acta 1446 (1-2): 35–46. PMID 10395917. 
  • Cao H, Hegele RA (2000). "Human cathepsin S gene (CTSS) promoter -25G/A polymorphism.". J. Hum. Genet. 45 (2): 94–5. PMID 10721671. 
  • Luke C, Schick C, Tsu C, et al. (2000). "Simple modifications of the serpin reactive site loop convert SCCA2 into a cysteine proteinase inhibitor: a critical role for the P3' proline in facilitating RSL cleavage.". Biochemistry 39 (24): 7081–91. PMID 10852705. 
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v • d • e
Hydrolase: proteases (EC 3.4)
Exopeptidase 3.4.11-19
Endopeptidase 3.4.21-24
Cathepsin 3.4.18,21,22,23
A - B - C - D - E - F - G - H - K - L1/L2 - S - W - Z