CATS_MOUSE
ID CATS_MOUSE Reviewed; 340 AA.
AC O70370; E9QK18; O54973;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Cathepsin S;
DE EC=3.4.22.27;
DE Flags: Precursor;
GN Name=Ctss; Synonyms=Cats;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv, and BALB/cJ; TISSUE=Brain;
RA Doh-ura K.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RA Rommerskirch W.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 144-306, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Cartilage;
RX PubMed=10395917; DOI=10.1016/s0167-4781(99)00068-8;
RA Soederstroem M., Salminen H., Glumoff V., Kirschke H., Aro H., Vuorio E.;
RT "Cathepsin expression during skeletal development.";
RL Biochim. Biophys. Acta 1446:35-46(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 296-340.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9516475; DOI=10.1074/jbc.273.13.7691;
RA Dandoy-Dron F., Guillo F., Benboudjema L., Deslys J.-P., Lasmesas C.,
RA Dormont D., Tovey M.G., Dron M.;
RT "Gene expression in scrapie. Cloning of a new scrapie-responsive gene and
RT the identification of increased levels of seven other mRNA transcripts.";
RL J. Biol. Chem. 273:7691-7697(1998).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=9545226; DOI=10.1126/science.280.5362.450;
RA Nakagawa T., Roth W., Wong P., Nelson A., Farr A., Deussing J.,
RA Villadangos J.A., Ploegh H., Peters C., Rudensky A.Y.;
RT "Cathepsin L: critical role in Ii degradation and CD4 T cell selection in
RT the thymus.";
RL Science 280:450-453(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Thiol protease. Key protease responsible for the removal of
CC the invariant chain from MHC class II molecules and MHC class II
CC antigen presentation. The bond-specificity of this proteinase is in
CC part similar to the specificities of cathepsin L.
CC {ECO:0000250|UniProtKB:P25774}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Similar to cathepsin L, but with much less activity on Z-Phe-
CC Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.;
CC EC=3.4.22.27;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P25774}. Secreted
CC {ECO:0000250|UniProtKB:P25774}. Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:P25774}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression found in
CC non-skeletal tissues. Relatively high levels found in skeletal tissues.
CC Expressed in spleen, B cells, dendritic cells and macrophages
CC (PubMed:9545226). {ECO:0000269|PubMed:10395917,
CC ECO:0000269|PubMed:9545226}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA05360.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF051732; AAC05781.1; -; Genomic_DNA.
DR EMBL; AF051727; AAC05781.1; JOINED; Genomic_DNA.
DR EMBL; AF051728; AAC05781.1; JOINED; Genomic_DNA.
DR EMBL; AF051729; AAC05781.1; JOINED; Genomic_DNA.
DR EMBL; AF051726; AAC05781.1; JOINED; Genomic_DNA.
DR EMBL; AF051730; AAC05781.1; JOINED; Genomic_DNA.
DR EMBL; AF051731; AAC05781.1; JOINED; Genomic_DNA.
DR EMBL; AF038546; AAB94925.1; -; mRNA.
DR EMBL; AJ002386; CAA05360.1; ALT_FRAME; mRNA.
DR EMBL; AC092203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Y18466; CAA77184.1; -; mRNA.
DR EMBL; AJ223208; CAA11182.1; -; mRNA.
DR CCDS; CCDS50992.1; -.
DR RefSeq; NP_067256.4; NM_021281.3.
DR PDB; 4BPV; X-ray; 2.00 A; A/B/C/D/E/K=116-340.
DR PDB; 4BQV; X-ray; 1.70 A; A/B/C/D/E/F/G/H=116-340.
DR PDB; 4BS5; X-ray; 1.25 A; A=116-340.
DR PDB; 4BS6; X-ray; 1.20 A; A/B=116-340.
DR PDB; 4BSQ; X-ray; 1.96 A; A=116-340.
DR PDB; 4MZO; X-ray; 1.47 A; A/B/C/D/E/F/G/H=116-340.
DR PDB; 4MZS; X-ray; 1.85 A; A/B=116-340.
DR PDBsum; 4BPV; -.
DR PDBsum; 4BQV; -.
DR PDBsum; 4BS5; -.
DR PDBsum; 4BS6; -.
DR PDBsum; 4BSQ; -.
DR PDBsum; 4MZO; -.
DR PDBsum; 4MZS; -.
DR AlphaFoldDB; O70370; -.
DR SMR; O70370; -.
DR BioGRID; 198976; 2.
DR STRING; 10090.ENSMUSP00000015667; -.
DR BindingDB; O70370; -.
DR ChEMBL; CHEMBL4098; -.
DR GuidetoPHARMACOLOGY; 2353; -.
DR MEROPS; C01.034; -.
DR GlyGen; O70370; 1 site.
DR iPTMnet; O70370; -.
DR PhosphoSitePlus; O70370; -.
DR SwissPalm; O70370; -.
DR CPTAC; non-CPTAC-3897; -.
DR EPD; O70370; -.
DR MaxQB; O70370; -.
DR PaxDb; O70370; -.
DR PRIDE; O70370; -.
DR ProteomicsDB; 265335; -.
DR Antibodypedia; 849; 468 antibodies from 36 providers.
DR DNASU; 13040; -.
DR Ensembl; ENSMUST00000116304; ENSMUSP00000112006; ENSMUSG00000038642.
DR GeneID; 13040; -.
DR KEGG; mmu:13040; -.
DR UCSC; uc008qjz.3; mouse.
DR CTD; 1520; -.
DR MGI; MGI:107341; Ctss.
DR VEuPathDB; HostDB:ENSMUSG00000038642; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000155176; -.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; O70370; -.
DR OMA; EMDGAFQ; -.
DR BRENDA; 3.4.22.27; 3474.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 13040; 2 hits in 67 CRISPR screens.
DR ChiTaRS; Ctss; mouse.
DR PRO; PR:O70370; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O70370; protein.
DR Bgee; ENSMUSG00000038642; Expressed in stroma of bone marrow and 246 other tissues.
DR ExpressionAtlas; O70370; baseline and differential.
DR Genevisible; O70370; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0031905; C:early endosome lumen; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; EXP:Reactome.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISS:UniProtKB.
DR GO; GO:0048002; P:antigen processing and presentation of peptide antigen; ISO:MGI.
DR GO; GO:0034769; P:basement membrane disassembly; IMP:BHF-UCL.
DR GO; GO:0045453; P:bone resorption; ISO:MGI.
DR GO; GO:0030574; P:collagen catabolic process; ISO:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:2001259; P:positive regulation of cation channel activity; IDA:CACAO.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IGI:MGI.
DR GO; GO:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:BHF-UCL.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0010447; P:response to acidic pH; ISO:MGI.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Protease; Reference proteome; Secreted; Signal; Thiol protease;
KW Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..122
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026315"
FT CHAIN 123..340
FT /note="Cathepsin S"
FT /id="PRO_0000026316"
FT ACT_SITE 147
FT /evidence="ECO:0000250"
FT ACT_SITE 287
FT /evidence="ECO:0000250"
FT ACT_SITE 307
FT /evidence="ECO:0000250"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 134..233
FT /evidence="ECO:0000250"
FT DISULFID 144..189
FT /evidence="ECO:0000250"
FT DISULFID 178..222
FT /evidence="ECO:0000250"
FT DISULFID 281..329
FT /evidence="ECO:0000250"
FT CONFLICT 34
FT /note="Y -> H (in Ref. 2; CAA05360)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="L -> S (in Ref. 1; AAB94925/AAC05781)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="P -> S (in Ref. 1; AAB94925/AAC05781)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="A -> S (in Ref. 3; CAA77184)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="T -> M (in Ref. 1; AAB94925 and 2; CAA05360)"
FT /evidence="ECO:0000305"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:4BS6"
FT HELIX 147..164
FT /evidence="ECO:0007829|PDB:4BS6"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:4BS6"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:4BS6"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4MZO"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:4BS6"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4BS6"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:4BS6"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:4BS6"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4BS6"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:4BS6"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:4BS6"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:4BS6"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:4BS6"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:4MZO"
FT STRAND 287..297
FT /evidence="ECO:0007829|PDB:4BS6"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:4BS6"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:4BS6"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:4BS6"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:4BS6"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:4BS6"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:4BS6"
SQ SEQUENCE 340 AA; 38475 MW; 10550C5106318C47 CRC64;
MRAPGHAAIR WLFWMPLVCS VAMEQLQRDP TLDYHWDLWK KTHEKEYKDK NEEEVRRLIW
EKNLKFIMIH NLEYSMGMHT YQVGMNDMGD MTNEEILCRM GALRIPRQSP KTVTFRSYSN
RTLPDTVDWR EKGCVTEVKY QGSCGACWAF SAVGALEGQL KLKTGKLISL SAQNLVDCSN
EEKYGNKGCG GGYMTEAFQY IIDNGGIEAD ASYPYKATDE KCHYNSKNRA ATCSRYIQLP
FGDEDALKEA VATKGPVSVG IDASHSSFFF YKSGVYDDPS CTGNVNHGVL VVGYGTLDGK
DYWLVKNSWG LNFGDQGYIR MARNNKNHCG IASYCSYPEI
