ID   CATK_MACFA              Reviewed;         329 AA.
AC   P61276; O77641;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   04-NOV-2026, entry version 104.
DE   RecName: Full=Cathepsin K;
DE            EC=3.4.22.38;
DE   Flags: Precursor;
GN   Name=CTSK;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone marrow;
RA   Feild J.A., Brun K.A., McQueney M.S., Amegdazie B.Y.;
RL   Submitted (JUN-1998) 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; AF070927; AAC23694.1; -; mRNA.
DR   RefSeq; XP_005542025.2; XM_005541968.4.
DR   RefSeq; XP_045220208.1; XM_045364273.3.
DR   AlphaFoldDB; P61276; -.
DR   SMR; P61276; -.
DR   STRING; 9541.ENSMFAP00000045350; -.
DR   GlyCosmos; P61276; 1 site, No reported glycans.
DR   GeneID; 102120416; -.
DR   KEGG; mcf:102120416; -.
DR   CTD; 1513; -.
DR   VEuPathDB; HostDB:ENSMFAG00000000402; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   OMA; AACKGYK; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0036021; C:endolysosome lumen; IEA:UniProtKB-ARBA.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001968; F:fibronectin binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0043394; F:proteoglycan binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0022617; P:extracellular matrix disassembly; IEA:UniProtKB-ARBA.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0006590; P:thyroid hormone generation; ISS:UniProtKB.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   FunFam; 3.90.70.10:FF:000006; Cathepsin S; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 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; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 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; Cysteine proteinases; 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..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..114
FT                   /note="Activation peptide"
FT                   /id="PRO_0000026297"
FT   CHAIN           115..329
FT                   /note="Cathepsin K"
FT                   /id="PRO_0000026298"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        136..177
FT                   /evidence="ECO:0000250"
FT   DISULFID        170..210
FT                   /evidence="ECO:0000250"
FT   DISULFID        269..318
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   329 AA;  36942 MW;  652DD8DFC37FB984 CRC64;
     MWGLKVLLLP VMSFALYPEE ILDTHWELWK KTHRKQYNSK VDEISRRLIW EKNLKYISIH
     NLEASLGVHT YELAMNHLGD MTNEEVVQKM TGLKVPASHS RSNDTLYIPD WEGRAPDSVD
     YRKKGYVTPV KNQGQCGSCW AFSSVGALEG QLKKKTGKLL NLSPQNLVDC VSENDGCGGG
     YMTNAFQYVQ KNRGIDSEDA YPYVGQEESC MYNPTGKAAK CRGYREIPEG NEKALKRAVA
     RVGPVSVAID ASLTSFQFYS KGVYYDESCN SDNLNHAVLA VGYGIQKGNK HWIIKNSWGE
     NWGNKGYILM ARNKNNACGI ANLASFPKM
//