CATS_RAT
ID CATS_RAT Reviewed; 330 AA.
AC Q02765;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cathepsin S;
DE EC=3.4.22.27;
DE Flags: Precursor;
GN Name=Ctss;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1281481; DOI=10.1016/s0021-9258(18)35713-2;
RA Petanceska S., Devi L.;
RT "Sequence analysis, tissue distribution, and expression of rat cathepsin
RT S.";
RL J. Biol. Chem. 267:26038-26043(1992).
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 -!- SUBUNIT: Monomer.
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: Highest levels occur in the ileum followed by
CC spleen, brain, thyroid, ovary and uterus. Low levels are found in the
CC liver, kidney, jejunum and lung with lowest levels in the heart.
CC -!- INDUCTION: By thyroid-stimulating hormone.
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}.
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DR EMBL; L03201; AAA40994.1; -; mRNA.
DR PIR; A45087; A45087.
DR RefSeq; NP_059016.1; NM_017320.1.
DR AlphaFoldDB; Q02765; -.
DR SMR; Q02765; -.
DR ChEMBL; CHEMBL1075217; -.
DR GuidetoPHARMACOLOGY; 2353; -.
DR MEROPS; C01.034; -.
DR MEROPS; I29.004; -.
DR GlyGen; Q02765; 2 sites.
DR PhosphoSitePlus; Q02765; -.
DR GeneID; 50654; -.
DR KEGG; rno:50654; -.
DR UCSC; RGD:621513; rat.
DR CTD; 1520; -.
DR RGD; 621513; Ctss.
DR InParanoid; Q02765; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q02765; -.
DR BRENDA; 3.4.22.27; 5301.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q02765; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005518; F:collagen binding; ISO:RGD.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:RGD.
DR GO; GO:0001968; F:fibronectin binding; ISO:RGD.
DR GO; GO:0043236; F:laminin binding; ISO:RGD.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0043394; F:proteoglycan binding; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
DR GO; GO:0002250; P:adaptive immune response; ISO:RGD.
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:RGD.
DR GO; GO:0034769; P:basement membrane disassembly; ISO:RGD.
DR GO; GO:0045453; P:bone resorption; IMP:RGD.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:RGD.
DR GO; GO:0030574; P:collagen catabolic process; ISO:RGD.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0001656; P:metanephros development; IEP:UniProtKB.
DR GO; GO:2001259; P:positive regulation of cation channel activity; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:0016485; P:protein processing; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0010447; P:response to acidic pH; ISO:RGD.
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 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW Protease; Reference proteome; Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..112
FT /note="Activation peptide"
FT /id="PRO_0000026317"
FT CHAIN 113..330
FT /note="Cathepsin S"
FT /id="PRO_0000026318"
FT ACT_SITE 137
FT /evidence="ECO:0000250"
FT ACT_SITE 277
FT /evidence="ECO:0000250"
FT ACT_SITE 297
FT /evidence="ECO:0000250"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 124..222
FT /evidence="ECO:0000250"
FT DISULFID 134..179
FT /evidence="ECO:0000250"
FT DISULFID 168..211
FT /evidence="ECO:0000250"
FT DISULFID 271..319
FT /evidence="ECO:0000250"
SQ SEQUENCE 330 AA; 36833 MW; 670E3F08D7749EFE CRC64;
MAVLGAPGVL CDNGATAERP TLDHHWDLWK KTRMRRNTDQ NEEDVRRLIW EKNLKFIMLH
NLEHSMGMHS YSVGMNHMGD MTPEEVIGYM GSLRIPRPWN RSGTLKSSSN QTLPDSVDWR
EKGCVTNVKY QGSCGSCWAF SAEGALEGQL KLKTGKLVSL SAQNLVDCST EEKYGNKGCG
GGFMTEAFQY IIDTSIDSEA SYPYKAMDEK CLYDPKNRAA TCSRYIELPF GDEEALKEAV
ATKGPVSVGI DDASHSSFFL YQSGVYDDPS CTENMNHGVL VVGYGTLDGK DYWLVKNSWG
LHFGDQGYIR MARNNKNHCG IASYCSYPEI
