ID A0A1S3NRI0_SALSA Unreviewed; 331 AA.
AC A0A1S3NRI0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cathepsin K {ECO:0000256|ARBA:ARBA00015572};
DE EC=3.4.22.38 {ECO:0000256|ARBA:ARBA00012474};
GN Name=LOC106580864 {ECO:0000313|RefSeq:XP_014017845.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014017845.1};
RN [1] {ECO:0000313|RefSeq:XP_014017845.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014017845.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001773};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004296};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004296};
CC Extracellular side {ECO:0000256|ARBA:ARBA00004296}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014017845.1; XM_014162370.1.
DR AlphaFoldDB; A0A1S3NRI0; -.
DR GeneID; 106580864; -.
DR KEGG; sasa:106580864; -.
DR OrthoDB; 5472948at2759; -.
DR Proteomes; UP000087266; Chromosome ssa02.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 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:SF741; CATHEPSIN K; 1.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..331
FT /note="Cathepsin K"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018753409"
FT DOMAIN 28..88
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 116..330
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 331 AA; 36368 MW; 02E4CD0042645120 CRC64;
MLLCGCVLLL LGSVLAHPLI EMSLDAEWDS WKTTHLREYN GLGEEAIRRT IWEKNMRLIE
AHNEEAALGI HSYELGMNHL GDMTSEEIVA KLTGLQVPMN RDRSNTWIPD NNVVKLPRSI
DYRKKGMVTP VKNQLSCGSC WAFSSAGALE GQLAKTTGKL IDLSPQNLVD CVTENNGCGG
GYMTNAFEYV EENGGIDTEE AYPYLGQDEQ CAYNASGVGA QCRGFKEIPE GDEQALTKAV
AKVGPVAVGI DATLSSFQFY QRGVYYDPNC NKDDINHAVL AVGYGQTAKG EKFWIVKNSW
SESWGNQGYI KMARNRGNAC GIANLASYPI M
//
