CATK_BOVIN
ID CATK_BOVIN Reviewed; 329 AA.
AC Q5E968;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cathepsin K;
DE EC=3.4.22.38;
DE Flags: Precursor;
GN Name=CTSK;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI09854.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAX09069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BT021052; AAX09069.1; ALT_INIT; mRNA.
DR EMBL; BC109853; AAI09854.1; ALT_INIT; mRNA.
DR RefSeq; NP_001029607.1; NM_001034435.1.
DR AlphaFoldDB; Q5E968; -.
DR SMR; Q5E968; -.
DR STRING; 9913.ENSBTAP00000028016; -.
DR MEROPS; C01.036; -.
DR MEROPS; I29.007; -.
DR PaxDb; Q5E968; -.
DR PRIDE; Q5E968; -.
DR Ensembl; ENSBTAT00000028016; ENSBTAP00000028016; ENSBTAG00000021035.
DR GeneID; 513038; -.
DR KEGG; bta:513038; -.
DR CTD; 1513; -.
DR VEuPathDB; HostDB:ENSBTAG00000021035; -.
DR VGNC; VGNC:27817; CTSK.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000157759; -.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q5E968; -.
DR OMA; PVGNEKA; -.
DR OrthoDB; 1275401at2759; -.
DR TreeFam; TF313739; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000021035; Expressed in uterine cervix and 104 other tissues.
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..15
FT /evidence="ECO:0000255"
FT PROPEP 16..114
FT /note="Activation peptide"
FT /id="PRO_0000236236"
FT CHAIN 115..329
FT /note="Cathepsin K"
FT /id="PRO_0000236237"
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; 36947 MW; A459B4651A3F8B2C CRC64;
MWGLTVLLLP VVSFALYPEE ILDTQWELWK KTYRKQYNSK GDEISRRLIW EKNLKHISIH
NLEASLGVHT YELAMNHLGD MTSEEVVQKM TGLKVPASRS RSNDTLYIPD WEGRAPDSVD
YRKKGYVTPV KNQGQCGSCW AFSSVGALEG QLKKKTGKLL NLSPQNLVDC VSENDGCGGG
YMTNAFQYVQ KNRGIDSEDA YPYVGQDENC MYNPTGKAAK CRGYREIPEG NEKALKRAVA
RVGPISVAID ASLTSFQFYR KGVYYDENCN SDNLNHAVLA VGYGIQKGNK HWIIKNSWGE
NWGNKGYILM ARNKNNACGI ANLASFPKM
