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P10605 (CATB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin B

EC=3.4.22.1
Alternative name(s):
Cathepsin B1

Cleaved into the following 2 chains:

  1. Cathepsin B light chain
  2. Cathepsin B heavy chain
Gene names
Name:Ctsb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

Interacts with SRPX2 By similarity. Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.

Subcellular location

Lysosome. Melanosome By similarity. Secretedextracellular space By similarity.

Sequence similarities

Belongs to the peptidase C1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 7962Activation peptide
PRO_0000026148
Chain80 – 333254Cathepsin B
PRO_0000026149
Chain80 – 12647Cathepsin B light chain By similarity
PRO_0000026150
Chain129 – 333205Cathepsin B heavy chain By similarity
PRO_0000026151
Propeptide334 – 3396 By similarity
PRO_0000026152

Sites

Active site1081 By similarity
Active site2781 By similarity
Active site2981 By similarity

Amino acid modifications

Modified residue2201N6-acetyllysine Ref.8
Glycosylation1921N-linked (GlcNAc...) Probable
Disulfide bond93 ↔ 122 By similarity
Disulfide bond105 ↔ 150 By similarity
Disulfide bond141 ↔ 207 By similarity
Disulfide bond142 ↔ 146 By similarity
Disulfide bond179 ↔ 211 By similarity
Disulfide bond187 ↔ 198 By similarity

Experimental info

Sequence conflict1601S → N in AAA37494. Ref.3
Sequence conflict1741N → D in AAA37494. Ref.3
Sequence conflict1771V → I in AAA37494. Ref.3
Sequence conflict2841G → V in AAA37494. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P10605 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 9F0A3CDF70A94040

FASTA33937,280
        10         20         30         40         50         60 
MWWSLILLSC LLALTSAHDK PSFHPLSDDL INYINKQNTT WQAGRNFYNV DISYLKKLCG 

        70         80         90        100        110        120 
TVLGGPKLPG RVAFGEDIDL PETFDAREQW SNCPTIGQIR DQGSCGSCWA FGAVEAISDR 

       130        140        150        160        170        180 
TCIHTNGRVN VEVSAEDLLT CCGIQCGDGC NGGYPSGAWS FWTKKGLVSG GVYNSHVGCL 

       190        200        210        220        230        240 
PYTIPPCEHH VNGSRPPCTG EGDTPRCNKS CEAGYSPSYK EDKHFGYTSY SVSNSVKEIM 

       250        260        270        280        290        300 
AEIYKNGPVE GAFTVFSDFL TYKSGVYKHE AGDMMGGHAI RILGWGVENG VPYWLAANSW 

       310        320        330 
NLDWGDNGFF KILRGENHCG IESEIVAGIP RTDQYWGRF 

« Hide

References

« Hide 'large scale' references
[1]"The structure of the mouse cathepsin B gene and its putative promoter."
Qian F., Frankfater A., Chan S.J., Steiner D.F.
DNA Cell Biol. 10:159-168(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Gene structure of mouse cathepsin B."
Ferrara M., Wojcik F., Rhaissi H., Mordier S., Roux M.-P., Bechet D.
FEBS Lett. 273:195-199(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs."
Chan S.J., San Segundo B., McCormick M.B., Steiner D.F.
Proc. Natl. Acad. Sci. U.S.A. 83:7721-7725(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Characterization of multiple cathepsin B mRNAs in murine B16a melanoma."
Qian F., Frankfater A., Steiner D.F., Bajkowski A.S., Chan S.J.
Anticancer Res. 11:1445-1451(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Placenta and Thymus.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[7]"Isolation of a cathepsin B-encoding cDNA from murine osteogenic cells."
Friemert C., Closs E.I., Silbermann M., Erfle V., Strauss P.G.
Gene 103:259-261(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 314-339.
[8]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M65270 expand/collapse EMBL AC list , M65263, M65264, M65265, M65266, M65267, M65268, M65269 Genomic DNA. Translation: AAA37375.1.
M14222 mRNA. Translation: AAA37494.1.
X54966 mRNA. Translation: CAA38713.1.
S69034 mRNA. Translation: AAB20536.1.
AK083393 mRNA. Translation: BAC38900.1.
AK147192 mRNA. Translation: BAE27751.1.
AK149884 mRNA. Translation: BAE29144.1.
AK151790 mRNA. Translation: BAE30691.1.
AK167361 mRNA. Translation: BAE39458.1.
BC006656 mRNA. Translation: AAH06656.1.
CCDSCCDS27197.1.
PIRKHMSB. A38458.
RefSeqNP_031824.1. NM_007798.3.
UniGeneMm.236553.

3D structure databases

ProteinModelPortalP10605.
SMRP10605. Positions 27-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP10605. 3 interactions.
MINTMINT-4089890.

Chemistry

BindingDBP10605.
ChEMBLCHEMBL5187.

PTM databases

PhosphoSiteP10605.

2D gel databases

SWISS-2DPAGEP10605.

Proteomic databases

MaxQBP10605.
PaxDbP10605.
PRIDEP10605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006235; ENSMUSP00000006235; ENSMUSG00000021939.
GeneID13030.
KEGGmmu:13030.
UCSCuc007uhh.2. mouse.

Organism-specific databases

CTD1508.
MGIMGI:88561. Ctsb.

Phylogenomic databases

eggNOGCOG4870.
GeneTreeENSGT00730000110701.
HOGENOMHOG000241341.
HOVERGENHBG003480.
InParanoidP10605.
KOK01363.
OMACTGEGDT.
OrthoDBEOG7034HR.
PhylomeDBP10605.
TreeFamTF314576.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14810.
BRENDA3.4.22.1. 3474.

Gene expression databases

BgeeP10605.
CleanExMM_CTSB.
GenevestigatorP10605.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR015643. Peptidase_C1A_cathepsin-B.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF285. PTHR12411:SF285. 1 hit.
PfamPF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTSB. mouse.
NextBio282900.
PROP10605.
SOURCESearch...

Entry information

Entry nameCATB_MOUSE
AccessionPrimary (citable) accession number: P10605
Secondary accession number(s): Q3UDW7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot