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 03-APR-2013, entry version 66.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 OrthoDB; EOG4JM7Q2; -.
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
//
