Reviewed, UniProtKB/Swiss-Prot P10605 (CATB_MOUSE)

Names and origin

Protein names

Recommended name:
    Cathepsin B
    EC=3.4.22.1
Alternative name(s):
    Cathepsin B1
Cleaved into the following 2 chains:
    1- Recommended name:
            Cathepsin B light chain
    2- Recommended name:
            Cathepsin B heavy chain

Gene names

Name:

Ctsb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.
Subcellular location	Lysosome. Melanosome By similarity.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro regulation of catalytic activity Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Inferred from direct assay. Source: MGI melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay. Source: MGI
Molecular function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Propeptide	18 – 79	62	Activation peptide		PRO_0000026148
	Chain	80 – 333	254	Cathepsin B		PRO_0000026149
	Chain	80 – 126	47	Cathepsin B light chain By similarity		PRO_0000026150
	Chain	129 – 333	205	Cathepsin B heavy chain By similarity		PRO_0000026151
	Propeptide	334 – 339	6	By similarity		PRO_0000026152
Sites
	Active site	108	1	By similarity
	Active site	278	1	By similarity
	Active site	298	1	By similarity
Amino acid modifications
	Glycosylation	192	1	N-linked (GlcNAc...) Probable
	Disulfide bond	93 ↔ 122		By similarity
	Disulfide bond	105 ↔ 150		By similarity
	Disulfide bond	141 ↔ 207		By similarity
	Disulfide bond	142 ↔ 146		By similarity
	Disulfide bond	179 ↔ 211		By similarity
	Disulfide bond	187 ↔ 198		By similarity
Experimental info
	Sequence conflict	160	1	S → N in AAA37494. Ref.3
	Sequence conflict	174	1	N → D in AAA37494. Ref.3
	Sequence conflict	177	1	V → I in AAA37494. Ref.3
	Sequence conflict	284	1	G → V in AAA37494. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P10605-1 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: 9F0A3CDF70A94040	FASTA	339	37,280
	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

References

	« Hide 'large scale' referencesShow '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: 2012677] [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: 2226854] [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: 3463996] [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: 1746902] [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. , 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: 16141072] [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: 15489334] [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: 1889751] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 314-339.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M65270 , 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.
IPI	IPI00113517.
PIR	KHMSB. A38458.
RefSeq	NP_031824.1.
UniGene	Mm.236553 Mm.465417 Mm.472420
3D structure databases
HSSP	HSSP built from PDB template 1THE based on UniProtKB P00787.
SMR	P10605. Positions 27-339.
ModBase	Search...
Protein-protein interaction databases
STRING	P10605.
Protein family/group databases
MEROPS	C01.060.
PTM databases
PhosphoSite	P10605.
2-D gel databases
SWISS-2DPAGE	P10605.
Proteomic databases
PRIDE	P10605.
Genome annotation databases
Ensembl	ENSMUST00000006235; ENSMUSP00000006235; ENSMUSG00000021939; Mus musculus. [Genome view]
GeneID	13030.
KEGG	mmu:13030.
UCSC	uc007uhh.1. mouse.
Organism-specific databases
CTD	13030.
MGI	MGI:88561. Ctsb.
Phylogenomic databases
HOGENOM	P10605.
HOVERGEN	P10605.
OMA	TFLGGPK.
Enzyme and pathway databases
BRENDA	3.4.22.1. 244.
Gene expression databases
ArrayExpress	P10605.
Bgee	P10605.
CleanEx	MM_CTSB.
Genevestigator	P10605.
GermOnline	ENSMUSG00000021939. Mus musculus.
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]
PANTHER	PTHR12411:SF16. CathepsinB_like. 1 hit. PTHR12411. Peptidase_C1A. 1 hit.
Pfam	PF00112. Peptidase_C1. 1 hit. PF08127. Propeptide_C1. 1 hit. [Graphical view]
PRINTS	PR00705. PAPAIN.
ProDom	PD000158. Peptidase_C1. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00645. Pept_C1. 1 hit. [Graphical view]
PROSITE	PS00640. THIOL_PROTEASE_ASN. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	282900.
SOURCE	Search...

Entry information

Entry name

CATB_MOUSE

Accession

Primary (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:	November 3, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)