ID   CATS_SAIBB              Reviewed;         330 AA.
AC   Q8HY82;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Cathepsin S;
DE            EC=3.4.22.27;
DE   Flags: Precursor;
GN   Name=CTSS;
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12651112; DOI=10.1016/s1046-5928(02)00646-0;
RA   Baker S.M., Karlsson L., Thurmond R.L.;
RT   "Cloning, expression, purification, and activity of dog (Canis familiaris)
RT   and monkey (Saimiri boliviensis) cathepsin S.";
RL   Protein Expr. Purif. 28:93-101(2003).
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   -!- 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY156691; AAO13008.1; -; mRNA.
DR   RefSeq; NP_001266935.1; NM_001280006.1.
DR   AlphaFoldDB; Q8HY82; -.
DR   SMR; Q8HY82; -.
DR   STRING; 39432.ENSSBOP00000021880; -.
DR   MEROPS; C01.034; -.
DR   MEROPS; I29.004; -.
DR   GeneID; 101044698; -.
DR   CTD; 1520; -.
DR   Proteomes; UP000233220; Whole Genome Shotgun Assembly.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..114
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026319"
FT   CHAIN           115..330
FT                   /note="Cathepsin S"
FT                   /id="PRO_0000026320"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        277
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        126..223
FT                   /evidence="ECO:0000250"
FT   DISULFID        136..179
FT                   /evidence="ECO:0000250"
FT   DISULFID        170..212
FT                   /evidence="ECO:0000250"
FT   DISULFID        271..319
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   330 AA;  37346 MW;  4ECE3129F2418C34 CRC64;
     MKQLVCVLFV CSSAVTQLHK DPTLDHHWNL WKKTYGKQYK EKNEEAVRRL IWEKNLKFVM
     LHNLEHSMGM HSYDLGMNHL GDMTSEEVMS LMSSLRVPNQ WQRNITYKSN PNQMLPDSVD
     WREKGCVTEV KYQGSCGACW AFSAVGALEA QLKLKTGKLV SLSAQNLVDC SEKYGNKGCN
     GGFMTEAFQY IIDNKGIDSE ASYPYKATDQ KCQYDSKYRA ATCSKYTELP YGREDVLKEA
     VANKGPVCVG VDASHPSFFL YRSGVYYDPA CTQKVNHGVL VIGYGDLNGK EYWLVKNSWG
     SNFGEQGYIR MARNKGNHCG IASYPSYPEI