P81494 (CATB_COTJA) Reviewed, UniProtKB/Swiss-Prot

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. Cathepsin B light chain
2. Cathepsin B heavy chain

Gene names

Name:

CTSB

Organism

Coturnix coturnix japonica (Japanese quail) (Coturnix japonica)

Taxonomic identifier

93934 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Perdicinae › Coturnix

Protein attributes

Sequence length	48 AA.
Sequence status	Fragments.
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.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›25	›25	Cathepsin B		PRO_0000026162
	Chain	1 – ›25	›25	Cathepsin B light chain		PRO_0000409492
	Chain	26 – ›48	›23	Cathepsin B heavy chain		PRO_0000026163
Experimental info
	Non-adjacent residues	25 – 26	2
	Non-terminal residue	48	1

Sequences

	Sequence		Length	Mass (Da)
	P81494 [UniParc]. Last modified December 15, 1998. Version 1. Checksum: F1763CC54BF91ACC	FASTA	48	5,226
	10 20 30 40 LPDTFDSRKQ WPNCPTISEI RDQGSVSVEV SAEDLLSCCG FECGMGCN

References

[1]	"Proteolytic enzymes in yolk-sac membrane of quail egg. Purification and enzymatic characterisation." Gerhartz B., Auerswald E.A., Mentele R., Fritz H., Machleidt W., Kolb H.J., Wittmann J. Comp. Biochem. Physiol. 118B:159-166(1997) [PubMed: 9418005] [Abstract] Cited for: PROTEIN SEQUENCE.
+	Additional computationally mapped references.

Cross-references

3D structure databases
ProteinModelPortal	P81494.
ModBase	Search...
Protein family/group databases
MEROPS	C01.060.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR013128. Peptidase_C1A. IPR015643. Peptidase_C1A_cathepsin-B. [Graphical view]
PANTHER	PTHR12411:SF16. CathepsinB_like. 1 hit. PTHR12411. Peptidase_C1A. 1 hit.
PROSITE	PS00640. THIOL_PROTEASE_ASN. Partial match. PS00139. THIOL_PROTEASE_CYS. Partial match. PS00639. THIOL_PROTEASE_HIS. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATB_COTJA

Accession

Primary (citable) accession number: P81494

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 15, 1998
Last modified:	November 16, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program