ID CATB_CHICK Reviewed; 340 AA.
AC P43233;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Cathepsin B;
DE EC=3.4.22.1;
DE AltName: Full=Cathepsin B1;
DE Contains:
DE RecName: Full=Cathepsin B light chain;
DE Contains:
DE RecName: Full=Cathepsin B heavy chain;
DE Flags: Precursor;
GN Name=CTSB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Bone;
RX PubMed=7647095; DOI=10.1016/0167-4838(95)00103-2;
RA Dong S.S., Stransky G.I., Whitaker C.H., Jordan S.E., Schlesinger P.H.,
RA Edwards J.C., Blair H.C.;
RT "Avian cathepsin B cDNA: sequence and demonstration that mRNAs of two sizes
RT are produced in cell types producing large quantities of the enzyme.";
RL Biochim. Biophys. Acta 1251:69-73(1995).
CC -!- FUNCTION: Thiol protease which is believed to participate in
CC intracellular degradation and turnover of proteins. Has also been
CC implicated in tumor invasion and metastasis.
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 -!- SUBUNIT: Dimer of a heavy chain and a light chain cross-linked by a
CC disulfide bond.
CC -!- SUBCELLULAR LOCATION: Lysosome.
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}.
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DR EMBL; U18083; AAA87075.1; -; mRNA.
DR PIR; S58770; S58770.
DR AlphaFoldDB; P43233; -.
DR SMR; P43233; -.
DR STRING; 9031.ENSGALP00000061589; -.
DR MEROPS; C01.060; -.
DR GlyCosmos; P43233; 2 sites, No reported glycans.
DR PaxDb; 9031-ENSGALP00000035933; -.
DR VEuPathDB; HostDB:geneid_396329; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; P43233; -.
DR PhylomeDB; P43233; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IEP:AgBase.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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: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 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; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..79
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026158"
FT CHAIN 80..340
FT /note="Cathepsin B"
FT /id="PRO_0000026159"
FT CHAIN 80..126
FT /note="Cathepsin B light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026160"
FT CHAIN 129..340
FT /note="Cathepsin B heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026161"
FT ACT_SITE 108
FT /evidence="ECO:0000250"
FT ACT_SITE 279
FT /evidence="ECO:0000250"
FT ACT_SITE 299
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..122
FT /evidence="ECO:0000250"
FT DISULFID 105..150
FT /evidence="ECO:0000250"
FT DISULFID 141..208
FT /evidence="ECO:0000250"
FT DISULFID 142..146
FT /evidence="ECO:0000250"
FT DISULFID 179..212
FT /evidence="ECO:0000250"
FT DISULFID 187..198
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 37587 MW; FCD7178ABB167704 CRC64;
MSWSRSILCL LGAFANARSI PYYPPLSSDL VNHINKLNTT GRAGHNFHNT DMSYVKKLCG
TFLGGPKAPE RVDFAEDMDL PDTFDTRKQW PNCPTISEIR DQGSCGSCWA FGAVEAISDR
ICVHTNAKVS VEVSAEDLLS CCGFECGMGC NGGYPSGAWR YWTERGLVSG GLYDSHVGCR
AYTIPPCEHH VNGSRPPCTG EGGETPRCSR HCEPGYSPSY KEDKHYGITS YGVPRSEKEI
MAEIYKNGPV EGAFIVYEDF LMYKSGVYQH VSGEQVGGHA IRILGWGVEN GTPYWLAANS
WNTDWGITGF FKILRGEDHC GIESEIVAGV PRMEQYWTRV
//
