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Database: UniProt
Entry: Q8HY81
LinkDB: Q8HY81
Original site: Q8HY81 
ID   CATS_CANFA              Reviewed;         331 AA.
AC   Q8HY81;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   13-NOV-2013, entry version 67.
DE   RecName: Full=Cathepsin S;
DE            EC=3.4.22.27;
DE   Flags: Precursor;
GN   Name=CTSS;
OS   Canis familiaris (Dog) (Canis lupus familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   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
RT   familiaris) and monkey (Saimiri boliviensis) cathepsin S.";
RL   Protein Expr. Purif. 28:93-101(2003).
CC   -!- FUNCTION: Thiol protease. Key protease responsible for the removal
CC       of the invariant chain from MHC class II molecules. The bond-
CC       specificity of this proteinase is in part similar to the
CC       specificities of cathepsin L and cathepsin N (By similarity).
CC   -!- CATALYTIC ACTIVITY: Similar to cathepsin L, but with much less
CC       activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-
CC       Arg-|-Xaa compound.
CC   -!- SUBCELLULAR LOCATION: Lysosome (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
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DR   EMBL; AY156692; AAO13009.1; -; mRNA.
DR   RefSeq; NP_001002938.2; NM_001002938.2.
DR   UniGene; Cfa.1661; -.
DR   ProteinModelPortal; Q8HY81; -.
DR   SMR; Q8HY81; 18-331.
DR   STRING; 9615.ENSCAFP00000017782; -.
DR   MEROPS; C01.034; -.
DR   GeneID; 403400; -.
DR   KEGG; cfa:403400; -.
DR   CTD; 1520; -.
DR   eggNOG; COG4870; -.
DR   HOGENOM; HOG000230774; -.
DR   HOVERGEN; HBG011513; -.
DR   InParanoid; Q8HY81; -.
DR   KO; K01368; -.
DR   NextBio; 20816922; -.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; PTHR12411; 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   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   Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW   Protease; Reference proteome; Signal; Thiol protease; Zymogen.
FT   SIGNAL        1     16       Potential.
FT   PROPEP       17    114       Activation peptide (By similarity).
FT                                /FTId=PRO_0000026311.
FT   CHAIN       115    331       Cathepsin S.
FT                                /FTId=PRO_0000026312.
FT   ACT_SITE    139    139       By similarity.
FT   ACT_SITE    278    278       By similarity.
FT   ACT_SITE    298    298       By similarity.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) (Potential).
FT   DISULFID    126    224       By similarity.
FT   DISULFID    136    180       By similarity.
FT   DISULFID    170    213       By similarity.
FT   DISULFID    272    320       By similarity.
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
//
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