ID   CATS_CANLF              Reviewed;         331 AA.
AC   Q8HY81;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Cathepsin S;
DE            EC=3.4.22.27;
DE   Flags: Precursor;
GN   Name=CTSS;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
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}.
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DR   EMBL; AY156692; AAO13009.1; -; mRNA.
DR   RefSeq; NP_001002938.2; NM_001002938.2.
DR   AlphaFoldDB; Q8HY81; -.
DR   SMR; Q8HY81; -.
DR   STRING; 9612.ENSCAFP00000017782; -.
DR   PaxDb; Q8HY81; -.
DR   PRIDE; Q8HY81; -.
DR   GeneID; 403400; -.
DR   KEGG; cfa:403400; -.
DR   CTD; 1520; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   InParanoid; Q8HY81; -.
DR   OrthoDB; 1275401at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISS:UniProtKB.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..114
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026311"
FT   CHAIN           115..331
FT                   /note="Cathepsin S"
FT                   /id="PRO_0000026312"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        126..224
FT                   /evidence="ECO:0000250"
FT   DISULFID        136..180
FT                   /evidence="ECO:0000250"
FT   DISULFID        170..213
FT                   /evidence="ECO:0000250"
FT   DISULFID        272..320
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  37228 MW;  8E873B7A02105C6A CRC64;
     MKWLVGLLPL CSYAVAQVHK DPTLDHHWNL WKKTYSKQYK EENEEVARRL IWEKNLKFVM
     LHNLEHSMGM HSYDLGMNHL GDMTGEEVIS LMGSLRVPSQ WQRNVTYRSN SNQKLPDSVD
     WREKGCVTEV KYQGSCGACW AFSAVGALEA QLKLKTGKLV SLSAQNLVDC STEKYGNKGC
     NGGFMTTAFQ YIIDNNGIDS EASYPYKAMN GKCRYDSKKR AATCSKYTEL PFGSEDALKE
     AVANKGPVSV AIDASHYSFF LYRSGVYYEP SCTQNVNHGV LVVGYGNLNG KDYWLVKNSW
     GLNFGDQGYI RMARNSGNHC GIASYPSYPE I