ID   CATS_BOVIN              Reviewed;         331 AA.
AC   P25326; Q3T0V8;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   04-NOV-2026, entry version 164.
DE   RecName: Full=Cathepsin S;
DE            EC=3.4.22.27;
DE   Flags: Precursor;
GN   Name=CTSS;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 115-331.
RC   TISSUE=Spleen;
RX   PubMed=2044774; DOI=10.1016/0014-5793(91)80620-i;
RA   Ritonja A., Colic A., Dolenc I., Ogrinc T., Podobnik M., Turk V.;
RT   "The complete amino acid sequence of bovine cathepsin S and a partial
RT   sequence of bovine cathepsin L.";
RL   FEBS Lett. 283:329-331(1991).
RN   [3]
RP   PROTEIN SEQUENCE OF 115-331.
RC   TISSUE=Spleen;
RX   PubMed=1515067; DOI=10.1515/bchm3.1992.373.2.407;
RA   Dolenc I., Ritonja A., Colic A., Podobnik M., Ogrinc T., Turk V.;
RT   "Bovine cathepsins S and L: isolation and amino acid sequences.";
RL   Biol. Chem. Hoppe-Seyler 373:407-412(1992).
RN   [4]
RP   PROTEIN SEQUENCE OF 115-331, AND NUCLEOTIDE SEQUENCE [MRNA] OF 136-331.
RC   TISSUE=Spleen;
RX   PubMed=1864368; DOI=10.1016/0014-5793(91)80971-5;
RA   Wiederanders B., Broemme D., Kirschke H., Kalkkinen N., Rinne A.,
RA   Paquette T., Toothman P.;
RT   "Primary structure of bovine cathepsin S. Comparison to cathepsins L, H, B
RT   and papain.";
RL   FEBS Lett. 286:189-192(1991).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=2604727; DOI=10.1042/bj2640475;
RA   Broemme D., Steinert A., Friebe S., Fittkau S., Wiederanders B.,
RA   Kirschke H.;
RT   "The specificity of bovine spleen cathepsin S. A comparison with rat liver
RT   cathepsins L and B.";
RL   Biochem. J. 264:475-481(1989).
CC   -!- FUNCTION: Thiol protease (By similarity). Key protease responsible for
CC       the removal of the invariant chain from MHC class II molecules and MHC
CC       class II antigen presentation. The bond-specificity of this proteinase
CC       is in part similar to the specificities of cathepsin L (By similarity).
CC       Elicits itch by mediating cleavage and activation of MRGPRX1 (By
CC       similarity). {ECO:0000250|UniProtKB:O70370,
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   -!- 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; BC102245; AAI02246.1; -; mRNA.
DR   EMBL; M95211; AAA30435.1; -; mRNA.
DR   EMBL; X62001; CAA43971.1; -; mRNA.
DR   PIR; S15844; S15844.
DR   RefSeq; NP_001028787.1; NM_001033615.2.
DR   RefSeq; XP_010801305.1; XM_010803003.4.
DR   RefSeq; XP_010801306.1; XM_010803004.4.
DR   AlphaFoldDB; P25326; -.
DR   SMR; P25326; -.
DR   FunCoup; P25326; 700.
DR   STRING; 9913.ENSBTAP00000022774; -.
DR   GlyCosmos; P25326; 1 site, No reported glycans.
DR   GlyGen; P25326; 1 site.
DR   PaxDb; 9913-ENSBTAP00000022774; -.
DR   GeneID; 327711; -.
DR   KEGG; bta:327711; -.
DR   CTD; 1520; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017135; -.
DR   VGNC; VGNC:27818; CTSS.
DR   eggNOG; KOG1543; Eukaryota.
DR   HOGENOM; CLU_012184_1_2_1; -.
DR   InParanoid; P25326; -.
DR   OMA; AAFRMRW; -.
DR   OrthoDB; 190265at2759; -.
DR   Reactome; R-BTA-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-BTA-1679131; Trafficking and processing of endosomal TLR.
DR   Reactome; R-BTA-2132295; MHC class II antigen presentation.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Reactome; R-BTA-9979719; Processing of antigen in germinal center B cells.
DR   PRO; PR:P25326; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000017135; Expressed in monocyte and 106 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
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:0030163; P:protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   FunFam; 3.90.70.10:FF:000006; Cathepsin S; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
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; Cysteine proteinases; 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   Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome; Secreted;
KW   Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..114
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:1515067,
FT                   ECO:0000269|PubMed:1864368, ECO:0000269|PubMed:2044774"
FT                   /id="PRO_0000238120"
FT   CHAIN           115..331
FT                   /note="Cathepsin S"
FT                   /id="PRO_0000050543"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        298
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        126..224
FT                   /evidence="ECO:0000250|UniProtKB:P25774"
FT   DISULFID        136..180
FT                   /evidence="ECO:0000250|UniProtKB:P25774"
FT   DISULFID        170..213
FT                   /evidence="ECO:0000250|UniProtKB:P25774"
FT   DISULFID        272..320
FT                   /evidence="ECO:0000250|UniProtKB:P25774"
SQ   SEQUENCE   331 AA;  37176 MW;  7F5547389F75DD58 CRC64;
     MNWLVWALLL CSSAMAHVHR DPTLDHHWDL WKKTYGKQYK EKNEEVARRL IWEKNLKTVT
     LHNLEHSMGM HSYELGMNHL GDMTSEEVIS LMSSLRVPSQ WPRNVTYKSD PNQKLPDSMD
     WREKGCVTEV KYQGACGSCW AFSAVGALEA QVKLKTGKLV SLSAQNLVDC STAKYGNKGC
     NGGFMTEAFQ YIIDNNGIDS EASYPYKAMD GKCQYDVKNR AATCSRYIEL PFGSEEALKE
     AVANKGPVSV GIDASHSSFF LYKTGVYYDP SCTQNVNHGV LVVGYGNLDG KDYWLVKNSW
     GLHFGDQGYI RMARNSGNHC GIANYPSYPE I
//