CATK_PIG
ID CATK_PIG Reviewed; 330 AA.
AC Q9GLE3;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cathepsin K;
DE EC=3.4.22.38;
DE Flags: Precursor;
GN Name=CTSK;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Thyroid;
RX PubMed=11082042; DOI=10.1242/jcs.113.24.4487;
RA Tepel C., Broemme D., Herzog V., Brix K.;
RT "Cathepsin K in thyroid epithelial cells: sequence, localization and
RT possible function in extracellular proteolysis of thyroglobulin.";
RL J. Cell Sci. 113:4487-4498(2000).
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 (By similarity).
CC Involved in the release of thyroid hormone thyroxine (T4) by limited
CC proteolysis of TG/thyroglobulin in the thyroid follicle lumen.
CC {ECO:0000250, ECO:0000269|PubMed:11082042}.
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:0000269|PubMed:11082042}. Secreted
CC {ECO:0000269|PubMed:11082042}. Apical cell membrane
CC {ECO:0000269|PubMed:11082042}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11082042}; Extracellular side
CC {ECO:0000269|PubMed:11082042}. Note=Localizes to the lumen of thyroid
CC follicles and to the apical membrane of thyroid epithelial cells.
CC {ECO:0000269|PubMed:11082042}.
CC -!- TISSUE SPECIFICITY: Expressed in the thyroid epithelial cells.
CC {ECO:0000269|PubMed:11082042}.
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; AF292030; AAG12340.1; -; mRNA.
DR RefSeq; NP_999467.1; NM_214302.1.
DR RefSeq; XP_005663523.1; XM_005663466.2.
DR AlphaFoldDB; Q9GLE3; -.
DR SMR; Q9GLE3; -.
DR STRING; 9823.ENSSSCP00000007088; -.
DR MEROPS; C01.036; -.
DR MEROPS; I29.007; -.
DR PaxDb; Q9GLE3; -.
DR PRIDE; Q9GLE3; -.
DR Ensembl; ENSSSCT00070000544; ENSSSCP00070000469; ENSSSCG00070000306.
DR GeneID; 397569; -.
DR KEGG; ssc:397569; -.
DR CTD; 1513; -.
DR eggNOG; KOG1543; Eukaryota.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q9GLE3; -.
DR OrthoDB; 1275401at2759; -.
DR TreeFam; TF313739; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 4.
DR Genevisible; Q9GLE3; SS.
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; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA: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 /id="PRO_0000026303"
FT CHAIN 116..330
FT /note="Cathepsin K"
FT /id="PRO_0000026304"
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; 37069 MW; ABF089EFE5FFB170 CRC64;
MWGLKVVLLL PVMSSALYPE EILDTQWELW KKTYRKQYNS KVDEISRRLI WEKNLKHISI
HNLEASLGVH TYELAMNHLG DMTSEEVVQK MTGLKVPPSH SRSNDTLYIP DWEGRTPDSI
DYRKKGYVTP VKNQGQCGSC WAFSSVGALE GQLKKKTGKL LNLSPQNLVD CVSENDGCGG
GYMTNAFQYV QKNRGIDSED AYPYVGQDEN CMYNPTGKAA KCRGYREIPE GNEKALKRAV
ARVGPVSVAI DASLTSFQFY SKGVYYDENC NSDNLNHAVL AVGYGIQKGK KHWIIKNSWG
ENWGNKGYIL MARNKNNACG IANLASFPKM
