ID B5T1M7_EPICO Unreviewed; 333 AA.
AC B5T1M7;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Cathepsin B {ECO:0000256|ARBA:ARBA00015559};
DE EC=3.4.22.1 {ECO:0000256|ARBA:ARBA00012537};
OS Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Serranoidei; Serranidae; Epinephelinae;
OC Epinephelini; Epinephelus.
OX NCBI_TaxID=94232 {ECO:0000313|EMBL:ACH73069.1};
RN [1] {ECO:0000313|EMBL:ACH73069.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:ACH73069.1};
RX PubMed=18519026; DOI=10.1016/j.bbrc.2008.05.126;
RA Yeh C.H., Chen Y.S., Wu M.S., Chen C.W., Yuan C.H., Pan K.W., Chang Y.N.,
RA Chuang N.N., Chang C.Y.;
RT "Differential display of grouper iridovirus-infected grouper cells by
RT immunostaining.";
RL Biochem. Biophys. Res. Commun. 372:674-680(2008).
RN [2] {ECO:0000313|EMBL:ACH73069.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:ACH73069.1};
RA Chang C.-Y., Yeh C.-H., Wu M.-S., Chen Y.-S., Chen C.-W.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule
CC substrates (thus differing from cathepsin L). In addition to being an
CC endopeptidase, shows peptidyl-dipeptidase activity, liberating C-
CC terminal dipeptides.; EC=3.4.22.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001754};
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; EU714151; ACH73069.1; -; mRNA.
DR AlphaFoldDB; B5T1M7; -.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02620; Peptidase_C1A_CathepsinB; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR012599; Propeptide_C1A.
DR PANTHER; PTHR12411:SF895; CATHEPSIN B; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR Pfam; PF08127; Propeptide_C1; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..333
FT /note="Cathepsin B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018667713"
FT DOMAIN 79..324
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 333 AA; 36191 MW; 7B1A10B9EDF2E3D5 CRC64;
MWRAALLLLA ASLSVSLARP HLKPLSSDMV NYINKLNTTW KAGHNFNNVD YSYVQKLCGT
MLKGPKLPVL VQYSGDMKLP KNFDSREQWP NCPTLKEIRD QGSCGSCWAF GAAEAISDRL
CIHSNGKVSV EISSEDLLTC CDSCGMGCNG GYPSAAWDFW TDVGLVSGGL YDSHVGCRPY
TIPPCEHHVN GTRPPCTGEG GDTPQCILQC ESGYTPSYKA DKHYGKSSYS VPSDEEQIQS
EIYKNGPVEG AFTVYEDFLL YKTGVYQHMT GSAVGGHAIK SWLGEEVCSL LALCHSDTDW
GDMVSLSSAG SDHCGIESEI VAGIPITQSF ELH
//
