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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
 
 
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