CATB_BOVIN
ID CATB_BOVIN Reviewed; 335 AA.
AC P07688; Q3ZC03;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 5.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Cathepsin B;
DE EC=3.4.22.1 {ECO:0000269|PubMed:1856234};
DE AltName: Full=BCSB;
DE Contains:
DE RecName: Full=Cathepsin B light chain {ECO:0000303|PubMed:3379063, ECO:0000303|PubMed:7106283};
DE Contains:
DE RecName: Full=Cathepsin B heavy chain {ECO:0000303|PubMed:3144290, ECO:0000303|PubMed:3379063};
DE Flags: Precursor;
GN Name=CTSB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1856234; DOI=10.1016/s0021-9258(18)92815-2;
RA Bechet D.M., Ferrara M.J., Mordier S.B., Roux M.-P., Deval C., Obled A.;
RT "Expression of lysosomal cathepsin B during calf myoblast-myotube
RT differentiation. Characterization of a cDNA encoding bovine cathepsin B.";
RL J. Biol. Chem. 266:14104-14112(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Spleen;
RX PubMed=8373811; DOI=10.1016/0167-4781(93)90205-r;
RA Mordier S., Bechet D., Roux M.-P., Obled A., Ferrara M.;
RT "Nucleotide sequence of bovine preprocathepsin B. A study of polymorphism
RT in the protein coding region.";
RL Biochim. Biophys. Acta 1174:305-311(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 80-332, GLYCOSYLATION AT ASN-192, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=3379063; DOI=10.1016/s0021-9258(19)76512-0;
RA Meloun B., Baudys M., Pohl J., Pavlik M., Kostka V.;
RT "Amino acid sequence of bovine spleen cathepsin B.";
RL J. Biol. Chem. 263:9087-9093(1988).
RN [5]
RP PRELIMINARY PROTEIN SEQUENCE OF 80-332.
RC TISSUE=Spleen;
RA Meloun B., Pohl J., Kostka V.;
RT "Tentative amino acid sequence of bovine spleen cathepsin B.";
RL (In) Turk V. (eds.);
RL Cysteine proteinases and their inhibitors, pp.19-29, Walter de Gruyter,
RL Berlin and New York (1986).
RN [6]
RP PROTEIN SEQUENCE OF 80-126, DISULFIDE BONDS, AND ACTIVE SITE.
RC TISSUE=Spleen;
RX PubMed=7106283; DOI=10.1016/0014-5793(82)80210-x;
RA Pohl J., Baudys M., Tomasek V., Kostka V.;
RT "Identification of the active site cysteine and of the disulfide bonds in
RT the N-terminal part of the molecule of bovine spleen cathepsin B.";
RL FEBS Lett. 142:23-26(1982).
RN [7]
RP PROTEIN SEQUENCE OF 224-237 AND 310-332, AND DISULFIDE BONDS.
RC TISSUE=Spleen;
RX PubMed=3144290;
RA Baudys M., Meloun B., Pohl J., Kostka V.;
RT "Identification of the second (buried) cysteine residue and of the C-
RT terminal disulfide bridge of bovine spleen cathepsin B.";
RL Biol. Chem. Hoppe-Seyler 369:169-174(1988).
RN [8]
RP DISULFIDE BONDS.
RX PubMed=2390214; DOI=10.1515/bchm3.1990.371.1.485;
RA Baudys M., Meloun B., Gan-Erdene T., Pohl J., Kostka V.;
RT "Disulfide bridges of bovine spleen cathepsin B.";
RL Biol. Chem. Hoppe-Seyler 371:485-491(1990).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 80-332, DISULFIDE BONDS, AND
RP ACTIVE SITE.
RX PubMed=10739956; DOI=10.1093/oxfordjournals.jbchem.a022651;
RA Yamamoto A., Tomoo K., Hara T., Murata M., Kitamura K., Ishida T.;
RT "Substrate specificity of bovine cathepsin B and its inhibition by CA074,
RT based on crystal structure refinement of the complex.";
RL J. Biochem. 127:635-643(2000).
CC -!- FUNCTION: Thiol protease which is believed to participate in
CC intracellular degradation and turnover of proteins (PubMed:1856234).
CC Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity).
CC Involved in the solubilization of cross-linked TG/thyroglobulin in the
CC thyroid follicle lumen (By similarity). Has also been implicated in
CC tumor invasion and metastasis (By similarity).
CC {ECO:0000250|UniProtKB:P07858, ECO:0000250|UniProtKB:P10605,
CC ECO:0000269|PubMed:1856234}.
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:0000269|PubMed:1856234};
CC -!- SUBUNIT: Dimer of a heavy chain and a light chain cross-linked by a
CC disulfide bond. Interacts with SRPX2. Directly interacts with SHKBP1.
CC {ECO:0000250|UniProtKB:P07858}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:1856234}. Melanosome
CC {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular space
CC {ECO:0000250|UniProtKB:A1E295}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P10605}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P10605}; Extracellular side
CC {ECO:0000250|UniProtKB:P10605}. Note=Localizes to the lumen of thyroid
CC follicles and to the apical membrane of thyroid epithelial cells.
CC {ECO:0000250|UniProtKB:P10605}.
CC -!- TISSUE SPECIFICITY: Expressed in myoblasts, the myotube, fibroblasts
CC and fetal muscle (at protein level) (PubMed:1856234). Expressed in the
CC spleen (at protein level) (PubMed:3379063).
CC {ECO:0000269|PubMed:1856234, ECO:0000269|PubMed:3379063}.
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; L06075; AAA03064.1; -; mRNA.
DR EMBL; M64620; AAA30434.1; -; mRNA.
DR EMBL; U16336; AAA80198.1; -; Genomic_DNA.
DR EMBL; U16337; AAA80198.1; JOINED; Genomic_DNA.
DR EMBL; U16338; AAA80198.1; JOINED; Genomic_DNA.
DR EMBL; U16339; AAA80198.1; JOINED; Genomic_DNA.
DR EMBL; U16341; AAA80198.1; JOINED; Genomic_DNA.
DR EMBL; U16342; AAA80198.1; JOINED; Genomic_DNA.
DR EMBL; U16343; AAA80198.1; JOINED; Genomic_DNA.
DR EMBL; BC102997; AAI02998.1; -; mRNA.
DR PIR; S38328; KHBOB.
DR RefSeq; NP_776456.1; NM_174031.2.
DR RefSeq; XP_005209879.1; XM_005209822.3.
DR RefSeq; XP_010805998.1; XM_010807696.2.
DR PDB; 1ITO; X-ray; 2.29 A; A=80-335.
DR PDB; 1QDQ; X-ray; 2.18 A; A=80-332.
DR PDB; 1SP4; X-ray; 2.20 A; A=80-127, B=128-332.
DR PDB; 2DC6; X-ray; 2.30 A; A=80-335.
DR PDB; 2DC7; X-ray; 1.94 A; A=80-335.
DR PDB; 2DC8; X-ray; 1.94 A; A=80-335.
DR PDB; 2DC9; X-ray; 1.94 A; A=80-335.
DR PDB; 2DCA; X-ray; 2.11 A; A=80-335.
DR PDB; 2DCB; X-ray; 1.94 A; A=80-335.
DR PDB; 2DCC; X-ray; 1.93 A; A=80-335.
DR PDB; 2DCD; X-ray; 2.50 A; A=80-335.
DR PDBsum; 1ITO; -.
DR PDBsum; 1QDQ; -.
DR PDBsum; 1SP4; -.
DR PDBsum; 2DC6; -.
DR PDBsum; 2DC7; -.
DR PDBsum; 2DC8; -.
DR PDBsum; 2DC9; -.
DR PDBsum; 2DCA; -.
DR PDBsum; 2DCB; -.
DR PDBsum; 2DCC; -.
DR PDBsum; 2DCD; -.
DR AlphaFoldDB; P07688; -.
DR SMR; P07688; -.
DR BioGRID; 158468; 1.
DR STRING; 9913.ENSBTAP00000036650; -.
DR BindingDB; P07688; -.
DR ChEMBL; CHEMBL2323; -.
DR MEROPS; C01.060; -.
DR CarbonylDB; P07688; -.
DR iPTMnet; P07688; -.
DR PaxDb; P07688; -.
DR PeptideAtlas; P07688; -.
DR PRIDE; P07688; -.
DR Ensembl; ENSBTAT00000036795; ENSBTAP00000036650; ENSBTAG00000012442.
DR GeneID; 281105; -.
DR KEGG; bta:281105; -.
DR CTD; 1508; -.
DR VEuPathDB; HostDB:ENSBTAG00000012442; -.
DR VGNC; VGNC:27813; CTSB.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000158680; -.
DR HOGENOM; CLU_012184_3_3_1; -.
DR InParanoid; P07688; -.
DR OMA; DEKIPYW; -.
DR OrthoDB; 865289at2759; -.
DR TreeFam; TF314576; -.
DR BRENDA; 3.4.22.1; 908.
DR Reactome; R-BTA-2132295; MHC class II antigen presentation.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; P07688; -.
DR PRO; PR:P07688; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000012442; Expressed in monocyte and 107 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:1904090; C:peptidase inhibitor complex; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0030574; P:collagen catabolic process; IEA:Ensembl.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0010466; P:negative regulation of peptidase activity; IEA:Ensembl.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0006590; P:thyroid hormone generation; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
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; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR012599; Propeptide_C1A.
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; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Membrane; Protease;
KW Reference proteome; Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..79
FT /note="Activation peptide"
FT /id="PRO_0000026138"
FT CHAIN 80..332
FT /note="Cathepsin B"
FT /evidence="ECO:0000269|PubMed:3379063"
FT /id="PRO_0000026139"
FT CHAIN 80..126
FT /note="Cathepsin B light chain"
FT /evidence="ECO:0000269|PubMed:3379063,
FT ECO:0000269|PubMed:7106283"
FT /id="PRO_0000026140"
FT CHAIN 129..332
FT /note="Cathepsin B heavy chain"
FT /evidence="ECO:0000269|PubMed:3144290,
FT ECO:0000269|PubMed:3379063"
FT /id="PRO_0000026141"
FT PROPEP 333..335
FT /evidence="ECO:0000250|UniProtKB:P07858"
FT /id="PRO_0000026142"
FT ACT_SITE 108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10088,
FT ECO:0000269|PubMed:10739956, ECO:0000269|PubMed:7106283"
FT ACT_SITE 278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089,
FT ECO:0000269|PubMed:10739956"
FT ACT_SITE 298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090,
FT ECO:0000269|PubMed:10739956"
FT MOD_RES 220
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10605"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3379063"
FT DISULFID 93..122
FT /evidence="ECO:0000269|PubMed:10739956,
FT ECO:0000269|PubMed:2390214, ECO:0000269|PubMed:7106283"
FT DISULFID 105..150
FT /evidence="ECO:0000269|PubMed:10739956,
FT ECO:0000269|PubMed:2390214, ECO:0000269|PubMed:7106283"
FT DISULFID 141..207
FT /evidence="ECO:0000269|PubMed:10739956,
FT ECO:0000269|PubMed:2390214"
FT DISULFID 142..146
FT /evidence="ECO:0000269|PubMed:10739956,
FT ECO:0000269|PubMed:2390214"
FT DISULFID 179..211
FT /evidence="ECO:0000269|PubMed:10739956,
FT ECO:0000269|PubMed:2390214"
FT DISULFID 187..198
FT /evidence="ECO:0000269|PubMed:10739956,
FT ECO:0000269|PubMed:2390214"
FT DISULFID 227..331
FT /evidence="ECO:0000269|PubMed:10739956,
FT ECO:0000269|PubMed:2390214, ECO:0000269|PubMed:3144290"
FT CONFLICT 143
FT /note="G -> D (in Ref. 3; AAI02998)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="F -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="S -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="G -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2DCC"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2DC7"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:2DCC"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:2DCC"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:2DCC"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2DCC"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1QDQ"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:2DCC"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:2DCC"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 274..288
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:2DCC"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:2DCC"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:2DCC"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:2DCC"
SQ SEQUENCE 335 AA; 36661 MW; 865794C8B7F2AED1 CRC64;
MWRLLATLSC LLVLTSARSS LYFPPLSDEL VNFVNKQNTT WKAGHNFYNV DLSYVKKLCG
AILGGPKLPQ RDAFAADVVL PESFDAREQW PNCPTIKEIR DQGSCGSCWA FGAVEAISDR
ICIHSNGRVN VEVSAEDMLT CCGGECGDGC NGGFPSGAWN FWTKKGLVSG GLYNSHVGCR
PYSIPPCEHH VNGSRPPCTG EGDTPKCSKT CEPGYSPSYK EDKHFGCSSY SVANNEKEIM
AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV SGEIMGGHAI RILGWGVENG TPYWLVGNSW
NTDWGDNGFF KILRGQDHCG IESEIVAGMP CTHQY
