ID A0A4Z2H4N1_9TELE Unreviewed; 330 AA.
AC A0A4Z2H4N1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Cathepsin B {ECO:0000256|ARBA:ARBA00015559};
DE EC=3.4.22.1 {ECO:0000256|ARBA:ARBA00012537};
GN Name=CTSB_2 {ECO:0000313|EMBL:TNN60817.1};
GN ORFNames=EYF80_028987 {ECO:0000313|EMBL:TNN60817.1};
OS Liparis tanakae (Tanaka's snailfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Cottales; Liparidae; Liparis.
OX NCBI_TaxID=230148 {ECO:0000313|EMBL:TNN60817.1, ECO:0000313|Proteomes:UP000314294};
RN [1] {ECO:0000313|EMBL:TNN60817.1, ECO:0000313|Proteomes:UP000314294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:TNN60817.1};
RA Kim W., Song I., Jeong J.-H., Kim D., Kim S., Ryu S., Song J.Y., Lee S.K.;
RT "First draft genome of Liparis tanakae, snailfish: a comprehensive survey
RT of snailfish specific genes.";
RL Submitted (MAR-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TNN60817.1}.
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DR EMBL; SRLO01000327; TNN60817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Z2H4N1; -.
DR Proteomes; UP000314294; Unassembled WGS sequence.
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 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:UP000314294};
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_5021470268"
FT DOMAIN 79..328
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 330 AA; 36160 MW; 82A5FE7E29AAF28A CRC64;
MWRSAVLLLA ASLSVSLARP HFKALSSEMV NYINKVNTTW KAGHNFHNVD YGYVKRLCGT
MLNGPKLPVM VQYAGDLELP ANFDCREQWP NCPTLKEIRD QGSCGSCWAF GAAEAISDRV
CIHSNAKVSV EISSEDLLSC CESCGMGCNG GYPAAAWEFW TSEGLVSGGL YDSHIGCRPY
TIAPCEHHVN GSRPSCSGEG GHTPECVYRC EPGYTPSYKV DKHFGKTSYS VLSEEEQIQT
EIYKNGPVEG AFTVFEDFVM YKSGVYQHVS GSALGGHAIK ILGWGEEDSV PYWLCANSWN
TDWGDNGFFK ILRGSNHCGI ESEIVAGIPK
//
