ID   CATK_CANFA              Reviewed;         330 AA.
AC   Q3ZKN1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Cathepsin K;
DE            EC=3.4.22.38;
DE   Flags: Precursor;
GN   Name=CTSK;
OS   Canis familiaris (Dog).
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].
RA   Muir P., Argyle D.J., Manley P.A., Hao Z.;
RT   "Cloning and sequencing of the canine cathepsin K gene.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Closely involved in osteoclastic bone resorption and may
CC       participate partially in the disorder of bone remodeling. Displays
CC       potent endoprotease activity against fibrinogen at acid pH. May
CC       play an important role in extracellular matrix degradation (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Broad proteolytic activity. With small-
CC       molecule substrates and inhibitors, the major determinant of
CC       specificity is P2, which is preferably Leu, Met > Phe, and not
CC       Arg.
CC   -!- SUBCELLULAR LOCATION: Lysosome (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
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DR   EMBL; AY738221; AAW65150.1; -; mRNA.
DR   RefSeq; NP_001029168.1; -.
DR   UniGene; Cfa.588; -.
DR   SMR; Q3ZKN1; 21-330.
DR   MEROPS; C01.036; -.
DR   Ensembl; ENSCAFG00000012093; Canis familiaris.
DR   GeneID; 608843; -.
DR   KEGG; cfa:608843; -.
DR   HOVERGEN; Q3ZKN1; -.
DR   BRENDA; 3.4.22.38; 463.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR015644; Peptidase_C1A_cathepsin-K.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411:SF55; CathpsnK_like; 1.
DR   PANTHER; PTHR12411; Peptidase_C1A; 1.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   ProDom; PD000158; Peptidase_C1; 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   Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease; Signal;
KW   Thiol protease; Zymogen.
FT   SIGNAL        1     16       Potential.
FT   PROPEP       17    115       Activation peptide (By similarity).
FT                                /FTId=PRO_0000270518.
FT   CHAIN       116    330       Cathepsin K.
FT                                /FTId=PRO_0000270519.
FT   ACT_SITE    140    140       By similarity.
FT   ACT_SITE    277    277       By similarity.
FT   ACT_SITE    297    297       By similarity.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) (Potential).
FT   DISULFID    137    178       By similarity.
FT   DISULFID    171    211       By similarity.
FT   DISULFID    270    319       By similarity.
SQ   SEQUENCE   330 AA;  37061 MW;  5276C7222A295678 CRC64;
     MWGLEVLLLL PMASFALYPE EILDTQWDLW KKTYRKQYNS KVDELSRRLI WEKNLKHISI
     HNLEASLGVH TYELAMNHLG DMTSEEVVQK MTGLKVPPSH SRSNDTLYIP DWESRAPDSV
     DYRKKGYVTP VKNQGQCGSC WAFSSVGALE GQLKKKTGKL LNLSPQNLVD CVSENDGCGG
     GYMTNAFQYV QKNRGIDSED AYPYVGQDES CMYNPTGKAA KCRGYREIPE GNEKALKRAV
     ARVGPISVAI DASLTSFQFY SKGVYYDENC NSDNLNHAVL AVGYGIQKGN KHWIIKNSWG
     ENWGNKGYIL MARNKNNACG IANLASFPKM
//