[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Mammary gland; PubMed=8001549 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Spinal cord; Lubec G., Afjehi-Sadat L.; Submitted (NOV-2006) to UniProtKB.
[5]	PROTEOLYTIC PROCESSING. PubMed=1639824 [NCBI, ExPASy, EBI, Israel, Japan] 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). DOI=10.1074/jbc.270.10.5527; PubMed=7890671 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/S0969-2126(96)00046-9; PubMed=8740363 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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: Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.
SUBCELLULAR LOCATION: Lysosome. Melanosome (By similarity).
SIMILARITY: Belongs to the peptidase C1 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X82396; CAA57792.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11305; AAA40993.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S51041; KHRTB.

UniGene

Rn.100909

3D structure databases

PDB

1CPJ; X-ray; 2.20 A; A/B=74-333.	[ExPASy / RCSB / EBI]
1CTE; X-ray; 2.10 A; A/B=80-333.	[ExPASy / RCSB / EBI]
1MIR; X-ray; 2.80 A; A/B=18-339.	[ExPASy / RCSB / EBI]
1THE; X-ray; 1.90 A; A/B=74-333.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1CPJ; -.
1CTE; -.
1MIR; -.
1THE; -.

ModBase

P00787.

Protein family/group databases

MEROPS

C01.060; -.

Organism-specific databases

RGD

621509; Ctsb.

Gene expression databases

ArrayExpress

P00787; -.

GermOnline

ENSRNOG00000010331; Rattus norvegicus.

Ontologies

GO:0005764;	Cellular component: lysosome (inferred from electronic annotation from UniProtKB-KW).
GO:0042470;	Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR015643; Peptidase_C1A_cathepsin-B.
IPR012599; Propeptide_C1A.
Graphical view of domain structure.

PANTHER

PTHR12411:SF16; CathepsinB_like; 1.
PTHR12411; Peptidase_C1A; 1.

Pfam

PF00112; Peptidase_C1; 1.
PF08127; Propeptide_C1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00705; PAPAIN.

ProDom

PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00645; Pept_C1; 1.
SMART graphical view of domain structure.

PROSITE

PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.

Genome annotation databases

Ensembl

ENSRNOG00000010331; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P00787; -.

Other

LinkHub

P00787; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Lysosome; Protease; Signal; Thiol protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`	`Potential.`
`PROPEP`	`18 79`	`62`	`Activation peptide.`	`PRO_0000026153`
`CHAIN`	`80 333`	`254`	`Cathepsin B.`	`PRO_0000026154`
`CHAIN`	`80 126`	`47`	`Cathepsin B light chain.`	`PRO_0000026155`
`CHAIN`	`129 333`	`205`	`Cathepsin B heavy chain.`	`PRO_0000026156`
`PROPEP`	`334 339`	`6`		`PRO_0000026157`
`ACT_SITE`	`108 108`
`ACT_SITE`	`278 278`
`ACT_SITE`	`298 298`
`CARBOHYD`	`192 192`		`N-linked (GlcNAc...).`
`DISULFID`	`93 122`
`DISULFID`	`105 150`
`DISULFID`	`141 207`
`DISULFID`	`142 146`
`DISULFID`	`179 211`
`DISULFID`	`187 198`
`VARIANT`	`302 302`	`1`	`V -> A.`
`CONFLICT`	`159 159`		`W -> G (in Ref. 3; AA sequence).`
`HELIX`	`86 89`	`4`
`TURN`	`90 92`	`3`
`HELIX`	`95 97`	`3`
`HELIX`	`108 124`	`17`
`TURN`	`125 127`	`3`
`HELIX`	`135 141`	`7`
`HELIX`	`149 151`	`3`
`HELIX`	`155 164`	`10`
`STRAND`	`188 191`	`4`
`TURN`	`219 222`	`4`
`STRAND`	`226 232`	`7`
`HELIX`	`236 246`	`11`
`STRAND`	`249 252`	`4`
`HELIX`	`257 259`	`3`
`STRAND`	`264 267`	`4`
`STRAND`	`274 276`	`3`
`STRAND`	`279 288`	`10`
`STRAND`	`291 297`	`7`
`STRAND`	`309 313`	`5`
`HELIX`	`318 320`	`3`
`TURN`	`321 323`	`3`
`STRAND`	`325 330`	`6`
`HELIX`	`333 338`	`6`

Sequence information

Length: 339 AA [This is the length of the unprocessed precursor]

Molecular weight: 37470 Da [This is the MW of the unprocessed precursor]

CRC64: 925E2E58C2B03CDA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWWSLIPLSC LLALTSAHDK PSSHPLSDDM INYINKQNTT WQAGRNFYNV DISYLKKLCG 

        70         80         90        100        110        120 
TVLGGPNLPE RVGFSEDINL PESFDAREQW SNCPTIAQIR DQGSCGSCWA FGAVEAMSDR 

       130        140        150        160        170        180 
ICIHTNGRVN VEVSAEDLLT CCGIQCGDGC NGGYPSGAWN FWTRKGLVSG GVYNSHIGCL 

       190        200        210        220        230        240 
PYTIPPCEHH VNGSRPPCTG EGDTPKCNKM CEAGYSTSYK EDKHYGYTSY SVSDSEKEIM 

       250        260        270        280        290        300 
AEIYKNGPVE GAFTVFSDFL TYKSGVYKHE AGDVMGGHAI RILGWGIENG VPYWLVANSW 

       310        320        330 
NVDWGDNGFF KILRGENHCG IESEIVAGIP RTQQYWGRF

P00787 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools