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Cathepsin B (EC 3.4.22.1) (Cathepsin B1) (RSG-2) [Cleaved into: Cathepsin B light chain; Cathepsin B heavy chain]

 CATB_RAT                Reviewed;         339 AA.
P00787;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
22-NOV-2017, entry version 166.
RecName: Full=Cathepsin B;
EC=3.4.22.1;
AltName: Full=Cathepsin B1;
AltName: Full=RSG-2;
Contains:
RecName: Full=Cathepsin B light chain;
Contains:
RecName: Full=Cathepsin B heavy chain;
Flags: Precursor;
Name=Ctsb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Mammary gland;
PubMed=8001549; DOI=10.1111/j.1432-1033.1994.tb20055.x;
Guenette R.S., Mooibroek M., Wong K., Wong P., Tenniswood M.;
"Cathepsin B, a cysteine protease implicated in metastatic
progression, is also expressed during regression of the rat prostate
and mammary glands.";
Eur. J. Biochem. 226:311-321(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 69-339.
PubMed=2986112; DOI=10.1073/pnas.82.8.2320;
San Segundo B., Chan S.J., Steiner D.F.;
"Identification of cDNA clones encoding a precursor of rat liver
cathepsin B.";
Proc. Natl. Acad. Sci. U.S.A. 82:2320-2324(1985).
[3]
PROTEIN SEQUENCE OF 80-126 AND 129-333.
TISSUE=Liver;
PubMed=6574504; DOI=10.1073/pnas.80.12.3666;
Takio K., Towatari T., Katunuma N., Teller D.C., Titani K.;
"Homology of amino acid sequences of rat liver cathepsins B and H with
that of papain.";
Proc. Natl. Acad. Sci. U.S.A. 80:3666-3670(1983).
[4]
PROTEIN SEQUENCE OF 246-263, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
PROTEOLYTIC PROCESSING.
PubMed=1639824;
Rowan A.D., Mason P., Mach L., Mort J.S.;
"Rat procathepsin B. Proteolytic processing to the mature form in
vitro.";
J. Biol. Chem. 267:15993-15999(1992).
[6]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=7890671; DOI=10.1074/jbc.270.10.5527;
Jia Z., Hasnain S., Hirama T., Lee X., Mort J.S., To R., Huber C.P.;
"Crystal structures of recombinant rat cathepsin B and a cathepsin B-
inhibitor complex. Implications for structure-based inhibitor
design.";
J. Biol. Chem. 270:5527-5533(1995).
[7]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 18-339.
PubMed=8740363; DOI=10.1016/S0969-2126(96)00046-9;
Cygler M., Sivaraman J., Grochulski P., Coulombe R., Storer A.C.,
Mort J.S.;
"Structure of rat procathepsin B: model for inhibition of cysteine
protease activity by the proregion.";
Structure 4:405-416(1996).
-!- FUNCTION: Thiol protease which is believed to participate in
intracellular degradation and turnover of proteins. Has also been
implicated in tumor invasion and metastasis.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity
for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in
small molecule substrates (thus differing from cathepsin L). In
addition to being an endopeptidase, shows peptidyl-dipeptidase
activity, liberating C-terminal dipeptides.
-!- SUBUNIT: Interacts with SRPX2 (By similarity). Dimer of a heavy
chain and a light chain cross-linked by a disulfide bond (By
similarity). Directly interacts with SHKBP1 (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P07858}.
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P07858}.
Melanosome {ECO:0000250}. Secreted, extracellular space
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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EMBL; X82396; CAA57792.1; -; mRNA.
EMBL; M11305; AAA40993.1; -; mRNA.
PIR; S51041; KHRTB.
UniGene; Rn.100909; -.
PDB; 1CPJ; X-ray; 2.20 A; A/B=74-333.
PDB; 1CTE; X-ray; 2.10 A; A/B=80-333.
PDB; 1MIR; X-ray; 2.80 A; A/B=18-339.
PDB; 1THE; X-ray; 1.90 A; A/B=74-333.
PDBsum; 1CPJ; -.
PDBsum; 1CTE; -.
PDBsum; 1MIR; -.
PDBsum; 1THE; -.
ProteinModelPortal; P00787; -.
SMR; P00787; -.
MINT; MINT-4996314; -.
STRING; 10116.ENSRNOP00000014178; -.
BindingDB; P00787; -.
ChEMBL; CHEMBL2602; -.
MEROPS; C01.060; -.
iPTMnet; P00787; -.
PhosphoSitePlus; P00787; -.
SwissPalm; P00787; -.
PaxDb; P00787; -.
PRIDE; P00787; -.
UCSC; RGD:621509; rat.
RGD; 621509; Ctsb.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
HOGENOM; HOG000241341; -.
HOVERGEN; HBG003480; -.
InParanoid; P00787; -.
PhylomeDB; P00787; -.
BRENDA; 3.4.22.1; 5301.
SABIO-RK; P00787; -.
EvolutionaryTrace; P00787; -.
PRO; PR:P00787; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005576; C:extracellular region; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005764; C:lysosome; IDA:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0042383; C:sarcolemma; IDA:RGD.
GO; GO:0005518; F:collagen binding; ISO:RGD.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:CAFA.
GO; GO:0008234; F:cysteine-type peptidase activity; ISO:RGD.
GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
GO; GO:0030984; F:kininogen binding; IPI:RGD.
GO; GO:0008233; F:peptidase activity; ISO:RGD.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0043621; F:protein self-association; IDA:RGD.
GO; GO:0043394; F:proteoglycan binding; ISO:RGD.
GO; GO:0006914; P:autophagy; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:RGD.
GO; GO:0030574; P:collagen catabolic process; ISO:RGD.
GO; GO:0046697; P:decidualization; ISO:RGD.
GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
GO; GO:0006508; P:proteolysis; IDA:CAFA.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; ISO:RGD.
GO; GO:0050790; P:regulation of catalytic activity; IEA:InterPro.
GO; GO:0014075; P:response to amine; IEP:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0070670; P:response to interleukin-4; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0009611; P:response to wounding; IEP:RGD.
GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
GO; GO:0007283; P:spermatogenesis; IEP:RGD.
GO; GO:0046718; P:viral entry into host cell; ISO:RGD.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
InterPro; IPR012599; Propeptide_C1A.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF00112; Peptidase_C1; 1.
Pfam; PF08127; Propeptide_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00645; Pept_C1; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Lysosome; Protease; Reference proteome; Secreted; Signal;
Thiol protease; Zymogen.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 79 Activation peptide.
{ECO:0000269|PubMed:6574504}.
/FTId=PRO_0000026153.
CHAIN 80 333 Cathepsin B.
/FTId=PRO_0000026154.
CHAIN 80 126 Cathepsin B light chain.
/FTId=PRO_0000026155.
CHAIN 129 333 Cathepsin B heavy chain.
/FTId=PRO_0000026156.
PROPEP 334 339
/FTId=PRO_0000026157.
ACT_SITE 108 108
ACT_SITE 278 278
ACT_SITE 298 298
MOD_RES 220 220 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10605}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:6574504}.
DISULFID 93 122
DISULFID 105 150
DISULFID 141 207
DISULFID 142 146
DISULFID 179 211
DISULFID 187 198
VARIANT 302 302 V -> A.
CONFLICT 159 159 W -> G (in Ref. 3; AA sequence).
{ECO:0000305}.
HELIX 28 37 {ECO:0000244|PDB:1MIR}.
STRAND 40 43 {ECO:0000244|PDB:1MIR}.
HELIX 52 58 {ECO:0000244|PDB:1MIR}.
TURN 75 77 {ECO:0000244|PDB:1MIR}.
HELIX 86 89 {ECO:0000244|PDB:1THE}.
TURN 90 92 {ECO:0000244|PDB:1CPJ}.
TURN 94 97 {ECO:0000244|PDB:1THE}.
STRAND 104 106 {ECO:0000244|PDB:1CTE}.
HELIX 108 124 {ECO:0000244|PDB:1THE}.
TURN 125 127 {ECO:0000244|PDB:1THE}.
HELIX 135 141 {ECO:0000244|PDB:1THE}.
HELIX 144 146 {ECO:0000244|PDB:1THE}.
HELIX 149 151 {ECO:0000244|PDB:1THE}.
HELIX 155 164 {ECO:0000244|PDB:1THE}.
STRAND 178 180 {ECO:0000244|PDB:1THE}.
STRAND 188 191 {ECO:0000244|PDB:1THE}.
STRAND 193 195 {ECO:0000244|PDB:1THE}.
HELIX 220 222 {ECO:0000244|PDB:1THE}.
STRAND 226 232 {ECO:0000244|PDB:1THE}.
HELIX 236 246 {ECO:0000244|PDB:1THE}.
STRAND 249 256 {ECO:0000244|PDB:1THE}.
HELIX 257 259 {ECO:0000244|PDB:1THE}.
STRAND 264 267 {ECO:0000244|PDB:1THE}.
STRAND 274 288 {ECO:0000244|PDB:1THE}.
STRAND 291 297 {ECO:0000244|PDB:1THE}.
STRAND 309 313 {ECO:0000244|PDB:1THE}.
HELIX 318 320 {ECO:0000244|PDB:1THE}.
TURN 321 323 {ECO:0000244|PDB:1THE}.
STRAND 325 330 {ECO:0000244|PDB:1THE}.
HELIX 333 338 {ECO:0000244|PDB:1MIR}.
SEQUENCE 339 AA; 37470 MW; 925E2E58C2B03CDA CRC64;
MWWSLIPLSC LLALTSAHDK PSSHPLSDDM INYINKQNTT WQAGRNFYNV DISYLKKLCG
TVLGGPNLPE RVGFSEDINL PESFDAREQW SNCPTIAQIR DQGSCGSCWA FGAVEAMSDR
ICIHTNGRVN VEVSAEDLLT CCGIQCGDGC NGGYPSGAWN FWTRKGLVSG GVYNSHIGCL
PYTIPPCEHH VNGSRPPCTG EGDTPKCNKM CEAGYSTSYK EDKHYGYTSY SVSDSEKEIM
AEIYKNGPVE GAFTVFSDFL TYKSGVYKHE AGDVMGGHAI RILGWGIENG VPYWLVANSW
NVDWGDNGFF KILRGENHCG IESEIVAGIP RTQQYWGRF


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