CATK_CANLF
ID CATK_CANLF Reviewed; 330 AA.
AC Q3ZKN1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Cathepsin K;
DE EC=3.4.22.38;
DE Flags: Precursor;
GN Name=CTSK;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; 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: Thiol protease involved in osteoclastic bone resorption and
CC may participate partially in the disorder of bone remodeling. Displays
CC potent endoprotease activity against fibrinogen at acid pH. May play an
CC important role in extracellular matrix degradation. Involved in the
CC release of thyroid hormone thyroxine (T4) by limited proteolysis of
CC TG/thyroglobulin in the thyroid follicle lumen.
CC {ECO:0000250|UniProtKB:P43235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad proteolytic activity. With small-molecule substrates and
CC inhibitors, the major determinant of specificity is P2, which is
CC preferably Leu, Met > Phe, and not Arg.; EC=3.4.22.38;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P43235}. Secreted
CC {ECO:0000250|UniProtKB:P43235}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P43235}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P43235}; Extracellular side
CC {ECO:0000250|UniProtKB:P43235}. Note=Localizes to the lumen of thyroid
CC follicles and to the apical membrane of thyroid epithelial cells.
CC {ECO:0000250|UniProtKB:P43235}.
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; AY738221; AAW65150.1; -; mRNA.
DR RefSeq; NP_001029168.1; NM_001033996.2.
DR AlphaFoldDB; Q3ZKN1; -.
DR SMR; Q3ZKN1; -.
DR STRING; 9612.ENSCAFP00000017808; -.
DR BindingDB; Q3ZKN1; -.
DR ChEMBL; CHEMBL2069160; -.
DR MEROPS; C01.036; -.
DR MEROPS; I29.007; -.
DR PaxDb; Q3ZKN1; -.
DR PRIDE; Q3ZKN1; -.
DR Ensembl; ENSCAFT00000019492; ENSCAFP00000018081; ENSCAFG00000012149.
DR Ensembl; ENSCAFT00030011860; ENSCAFP00030010389; ENSCAFG00030006444.
DR Ensembl; ENSCAFT00040021021; ENSCAFP00040018251; ENSCAFG00040011336.
DR Ensembl; ENSCAFT00845034366; ENSCAFP00845026906; ENSCAFG00845019461.
DR GeneID; 608843; -.
DR KEGG; cfa:608843; -.
DR CTD; 1513; -.
DR VEuPathDB; HostDB:ENSCAFG00845019461; -.
DR VGNC; VGNC:57505; ARNT.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000157759; -.
DR InParanoid; Q3ZKN1; -.
DR OrthoDB; 1275401at2759; -.
DR Reactome; R-CFA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CFA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-CFA-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-CFA-2132295; MHC class II antigen presentation.
DR Reactome; R-CFA-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
DR PRO; PR:Q3ZKN1; -.
DR Proteomes; UP000002254; Chromosome 17.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0043394; F:proteoglycan binding; IEA:Ensembl.
DR GO; GO:0045453; P:bone resorption; 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:0061037; P:negative regulation of cartilage development; IEA:Ensembl.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0006590; P:thyroid hormone generation; ISS:UniProtKB.
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; IPR015644; Peptidase_C1A_cathepsin-K.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411:SF55; PTHR12411:SF55; 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; SSF54001; 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 Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Membrane;
KW Protease; Reference proteome; Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..115
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000270518"
FT CHAIN 116..330
FT /note="Cathepsin K"
FT /id="PRO_0000270519"
FT ACT_SITE 140
FT /evidence="ECO:0000250"
FT ACT_SITE 277
FT /evidence="ECO:0000250"
FT ACT_SITE 297
FT /evidence="ECO:0000250"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 137..178
FT /evidence="ECO:0000250"
FT DISULFID 171..211
FT /evidence="ECO:0000250"
FT DISULFID 270..319
FT /evidence="ECO:0000250"
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
