ID A0A024CJP3_SPAAU Unreviewed; 330 AA.
AC A0A024CJP3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Cathepsin B {ECO:0000256|ARBA:ARBA00015559};
DE EC=3.4.22.1 {ECO:0000256|ARBA:ARBA00012537};
GN Name=CTSB {ECO:0000313|EMBL:AHZ34284.1};
GN Synonyms=LOC115580670 {ECO:0000313|Ensembl:ENSSAUP00010017967.1};
OS Sparus aurata (Gilthead sea bream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Sparus.
OX NCBI_TaxID=8175 {ECO:0000313|EMBL:AHZ34284.1};
RN [1] {ECO:0000313|EMBL:AHZ34284.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25880457; DOI=10.1186/s13104-015-1121-0;
RA Salmeron C., Navarro I., Johnston I.A., Gutierrez J., Capilla E.;
RT "Characterisation and expression analysis of cathepsins and ubiquitin-
RT proteasome genes in gilthead sea bream (Sparus aurata) skeletal muscle.";
RL BMC Res. Notes 8:149-149(2015).
RN [2] {ECO:0000313|Ensembl:ENSSAUP00010017967.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; KJ524457; AHZ34284.1; -; mRNA.
DR SMR; A0A024CJP3; -.
DR MEROPS; C01.060; -.
DR Ensembl; ENSSAUT00010018989.1; ENSSAUP00010017967.1; ENSSAUG00010008071.1.
DR GeneTree; ENSGT00940000158680; -.
DR OrthoDB; 808912at2759; -.
DR Proteomes; UP000472265; Unplaced.
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; 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; IPR012599; Propeptide_C1A.
DR PANTHER; PTHR12411:SF978; 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 PRINTS; PR00705; PAPAIN.
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000472265};
KW 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..330
FT /note="Cathepsin B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040664683"
FT DOMAIN 79..328
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 330 AA; 36410 MW; 6BA4950A221708A8 CRC64;
MWRAAFLLLA ASLSVSLARP HLKPLSNEMV NYINKFNTTW KAGHNFHNVD YSYVQRLCGT
MLKGPKLPVM VQYAGDLELP KEFDSRVQWP NCPTLKEIRD QGSCGSCWAF GAAEAISDRV
CIHSNAKVSV EISSEDLLTC CDSCGMGCNG GYPSAAWDFW TKDGLVSGGL YDSHVGCRPY
TIAPCEHHVN GSRPPCTGEG GETPQCIFQC EAGYTPSYKQ DKHYGKTSYS VLSDEEQIQY
EIYKNGPVEG AFIVYEDFVL YKSGVYQHVS GSQVGGHAIK ILGWGEEAGV PYWLCANSWN
TDWGDNGFFK FLRGSDHCGI ESEIVAGIPK
//
