Cathepsin S

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound. EC:3.4.22.27

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• collagen binding Source: RGDInferred from sequence orthologyⁱ
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]
• cysteine-type endopeptidase activity Source: RGDInferred from sequence orthologyⁱ
  • "New functions of lactoferrin and beta-casein in mammalian milk as cysteine protease inhibitors."
    Ohashi A., Murata E., Yamamoto K., Majima E., Sano E., Le Q.T., Katunuma N.
    Biochem. Biophys. Res. Commun. 306:98-103(2003) [PubMed] [Europe PMC] [Abstract]
  • "Important role of cathepsin S in generating peptides for TAP-independent MHC class I crosspresentation in vivo."
    Shen L., Sigal L.J., Boes M., Rock K.L.
    Immunity 21:155-165(2004) [PubMed] [Europe PMC] [Abstract]
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]
  • "Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading."
    Riese R.J., Wolf P.R., Bromme D., Natkin L.R., Villadangos J.A., Ploegh H.L., Chapman H.A.
    Immunity 4:357-366(1996) [PubMed] [Europe PMC] [Abstract]
• cysteine-type peptidase activity Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Baculoviral expression and characterization of rodent cathepsin S."
    Mason C.S., Lamers M.B., Henderson I.M., Monk T., Williams D.H.
    Protein Expr. Purif. 23:45-54(2001) [PubMed] [Europe PMC] [Abstract]
• fibronectin binding Source: RGDInferred from sequence orthologyⁱ
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]
• laminin binding Source: RGDInferred from sequence orthologyⁱ
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]
• peptidase activity Source: RGDInferred from sequence orthologyⁱ
  • "Dynamics of major histocompatibility complex class II compartments during B cell receptor-mediated cell activation."
    Lankar D., Vincent-Schneider H., Briken V., Yokozeki T., Raposo G., Bonnerot C.
    J. Exp. Med. 195:461-472(2002) [PubMed] [Europe PMC] [Abstract]
• proteoglycan binding Source: RGDInferred from sequence orthologyⁱ
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• adaptive immune response Source: RGDInferred from sequence orthologyⁱ
  • "Inhibitory p41 isoform of invariant chain and its potential target enzymes cathepsins L and H in distinct populations of macrophages in human lymph nodes."
    Zavasnik-Bergant V., Schweiger A., Bevec T., Golouh R., Turk V., Kos J.
    Immunology 112:378-385(2004) [PubMed] [Europe PMC] [Abstract]
• antigen processing and presentation of exogenous peptide antigen via MHC class II Source: UniProtKB
• antigen processing and presentation of peptide antigen Source: RGDInferred from sequence orthologyⁱ
  • "Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading."
    Riese R.J., Wolf P.R., Bromme D., Natkin L.R., Villadangos J.A., Ploegh H.L., Chapman H.A.
    Immunity 4:357-366(1996) [PubMed] [Europe PMC] [Abstract]
• basement membrane disassembly Source: RGDInferred from sequence orthologyⁱ
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]
• bone resorption Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Study of the functional share of lysosomal cathepsins by the development of specific inhibitors."
    Katunuma N., Matsui A., Kakegawa T., Murata E., Asao T., Ohba Y.
    Adv. Enzyme Regul. 39:247-260(1999) [PubMed] [Europe PMC] [Abstract]
• cellular response to thyroid hormone stimulus Source: RGDInferred from sequence orthologyⁱ
  • "Cathepsin H regulated by the thyroid hormone receptors associate with tumor invasion in human hepatoma cells."
    Wu S.M., Huang Y.H., Yeh C.T., Tsai M.M., Liao C.H., Cheng W.L., Chen W.J., Lin K.H.
    Oncogene 30:2057-2069(2011) [PubMed] [Europe PMC] [Abstract]
• collagen catabolic process Source: RGDInferred from sequence orthologyⁱ
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]
• immune response Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• metanephros development Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Functional interface between cathepsins and growth factors in the kidney development."
    Vattimo M.d.e. F., Santos O.F.
    Ren Fail 27:615-622(2005) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cation channel activity Source: RGDInferred from sequence orthologyⁱ
  • "Proteolytic activation of the epithelial sodium channel (ENaC) by the cysteine protease cathepsin-S."
    Haerteis S., Krappitz M., Bertog M., Krappitz A., Baraznenok V., Henderson I., Lindstrom E., Murphy J.E., Bunnett N.W., Korbmacher C.
    Pflugers Arch. 464:353-365(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of inflammatory response Source: RGDInferred from sequence orthologyⁱ
  • "Cathepsin S inhibitor prevents autoantigen presentation and autoimmunity."
    Saegusa K., Ishimaru N., Yanagi K., Arakaki R., Ogawa K., Saito I., Katunuma N., Hayashi Y.
    J. Clin. Invest. 110:361-369(2002) [PubMed] [Europe PMC] [Abstract]
• protein processing Source: RGDInferred from sequence orthologyⁱ
  • "Proteolytic activation of the epithelial sodium channel (ENaC) by the cysteine protease cathepsin-S."
    Haerteis S., Krappitz M., Bertog M., Krappitz A., Baraznenok V., Henderson I., Lindstrom E., Murphy J.E., Bunnett N.W., Korbmacher C.
    Pflugers Arch. 464:353-365(2012) [PubMed] [Europe PMC] [Abstract]
• proteolysis Source: RGDInferred from sequence orthologyⁱ
  • "Dynamics of major histocompatibility complex class II compartments during B cell receptor-mediated cell activation."
    Lankar D., Vincent-Schneider H., Briken V., Yokozeki T., Raposo G., Bonnerot C.
    J. Exp. Med. 195:461-472(2002) [PubMed] [Europe PMC] [Abstract]
  • "New functions of lactoferrin and beta-casein in mammalian milk as cysteine protease inhibitors."
    Ohashi A., Murata E., Yamamoto K., Majima E., Sano E., Le Q.T., Katunuma N.
    Biochem. Biophys. Res. Commun. 306:98-103(2003) [PubMed] [Europe PMC] [Abstract]
  • "Proteolytic activation of the epithelial sodium channel (ENaC) by the cysteine protease cathepsin-S."
    Haerteis S., Krappitz M., Bertog M., Krappitz A., Baraznenok V., Henderson I., Lindstrom E., Murphy J.E., Bunnett N.W., Korbmacher C.
    Pflugers Arch. 464:353-365(2012) [PubMed] [Europe PMC] [Abstract]
• proteolysis involved in cellular protein catabolic process Source: RGDInferred from sequence orthologyⁱ
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]
• regulation of sensory perception of pain Source: RGDInferred from mutant phenotypeⁱ
  • "Inhibition of spinal microglial cathepsin S for the reversal of neuropathic pain."
    Clark A.K., Yip P.K., Grist J., Gentry C., Staniland A.A., Marchand F., Dehvari M., Wotherspoon G., Winter J., Ullah J., Bevan S., Malcangio M.
    Proc. Natl. Acad. Sci. U.S.A. 104:10655-10660(2007) [PubMed] [Europe PMC] [Abstract]
• response to acidic pH Source: RGDInferred from sequence orthologyⁱ
  • "Proteolytic activation of the epithelial sodium channel (ENaC) by the cysteine protease cathepsin-S."
    Haerteis S., Krappitz M., Bertog M., Krappitz A., Baraznenok V., Henderson I., Lindstrom E., Murphy J.E., Bunnett N.W., Korbmacher C.
    Pflugers Arch. 464:353-365(2012) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• fibronectin binding Source: RGDInferred from sequence orthologyⁱ
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]
• laminin binding Source: RGDInferred from sequence orthologyⁱ
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]
• proteoglycan binding Source: RGDInferred from sequence orthologyⁱ
  • "Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners."
    Sage J., Leblanc-Noblesse E., Nizard C., Sasaki T., Schnebert S., Perrier E., Kurfurst R., Bromme D., Lalmanach G., Lecaille F.
    PLoS ONE 7:e43494-e43494(2012) [PubMed] [Europe PMC] [Abstract]

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MAVLGAPGVL CDNGATAERP TLDHHWDLWK KTRMRRNTDQ NEEDVRRLIW 
        60         70         80         90        100
EKNLKFIMLH NLEHSMGMHS YSVGMNHMGD MTPEEVIGYM GSLRIPRPWN 
       110        120        130        140        150
RSGTLKSSSN QTLPDSVDWR EKGCVTNVKY QGSCGSCWAF SAEGALEGQL 
       160        170        180        190        200
KLKTGKLVSL SAQNLVDCST EEKYGNKGCG GGFMTEAFQY IIDTSIDSEA 
       210        220        230        240        250
SYPYKAMDEK CLYDPKNRAA TCSRYIELPF GDEEALKEAV ATKGPVSVGI 
       260        270        280        290        300
DDASHSSFFL YQSGVYDDPS CTENMNHGVL VVGYGTLDGK DYWLVKNSWG 
       310        320        330
LHFGDQGYIR MARNNKNHCG IASYCSYPEI                       

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Chemistry databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Peptidase families
   Classification of peptidase families and list of entries
2. SIMILARITY comments
   Index of protein domains and families