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   03-AUG-2022, entry version 149.
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. 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   -!- 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; 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_010803003.2.
DR   RefSeq; XP_010801306.1; XM_010803004.2.
DR   AlphaFoldDB; P25326; -.
DR   SMR; P25326; -.
DR   STRING; 9913.ENSBTAP00000022774; -.
DR   PaxDb; P25326; -.
DR   PRIDE; P25326; -.
DR   Ensembl; ENSBTAT00000022774; ENSBTAP00000022774; ENSBTAG00000017135.
DR   GeneID; 327711; -.
DR   KEGG; bta:327711; -.
DR   CTD; 1520; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017135; -.
DR   VGNC; VGNC:27818; CTSS.
DR   eggNOG; KOG1543; Eukaryota.
DR   GeneTree; ENSGT00940000155176; -.
DR   HOGENOM; CLU_012184_1_2_1; -.
DR   InParanoid; P25326; -.
DR   OMA; EMDGAFQ; -.
DR   OrthoDB; 1275401at2759; -.
DR   TreeFam; TF313739; -.
DR   Reactome; R-BTA-2132295; MHC class II antigen presentation.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000017135; Expressed in monocyte and 106 other tissues.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR   GO; GO:0043236; F:laminin binding; IEA:Ensembl.
DR   GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR   GO; GO:0002250; P:adaptive immune response; IEA:Ensembl.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISS:UniProtKB.
DR   GO; GO:0034769; P:basement membrane disassembly; IEA:Ensembl.
DR   GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR   GO; GO:0030574; P:collagen catabolic process; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; IBA:GO_Central.
DR   GO; GO:2001259; P:positive regulation of cation channel activity; IEA:Ensembl.
DR   GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   GO; GO:0010447; P:response to acidic pH; IEA:Ensembl.
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   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: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;  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