P43233 (CATB_CHICK) 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

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of catalytic activity Inferred from electronic annotation. Source: InterPro
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
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 Potential		PRO_0000026158
	Chain	80 – 340	261	Cathepsin B		PRO_0000026159
	Chain	80 – 126	47	Cathepsin B light chain By similarity		PRO_0000026160
	Chain	129 – 340	212	Cathepsin B heavy chain By similarity		PRO_0000026161
Sites
	Active site	108	1	By similarity
	Active site	279	1	By similarity
	Active site	299	1	By similarity
Amino acid modifications
	Glycosylation	38	1	N-linked (GlcNAc...) Potential
	Glycosylation	192	1	N-linked (GlcNAc...) Potential
	Disulfide bond	93 ↔ 122		By similarity
	Disulfide bond	105 ↔ 150		By similarity
	Disulfide bond	141 ↔ 208		By similarity
	Disulfide bond	142 ↔ 146		By similarity
	Disulfide bond	179 ↔ 212		By similarity
	Disulfide bond	187 ↔ 198		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43233 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: FCD7178ABB167704	FASTA	340	37,587
	10 20 30 40 50 60 MSWSRSILCL LGAFANARSI PYYPPLSSDL VNHINKLNTT GRAGHNFHNT DMSYVKKLCG 70 80 90 100 110 120 TFLGGPKAPE RVDFAEDMDL PDTFDTRKQW PNCPTISEIR DQGSCGSCWA FGAVEAISDR 130 140 150 160 170 180 ICVHTNAKVS VEVSAEDLLS CCGFECGMGC NGGYPSGAWR YWTERGLVSG GLYDSHVGCR 190 200 210 220 230 240 AYTIPPCEHH VNGSRPPCTG EGGETPRCSR HCEPGYSPSY KEDKHYGITS YGVPRSEKEI 250 260 270 280 290 300 MAEIYKNGPV EGAFIVYEDF LMYKSGVYQH VSGEQVGGHA IRILGWGVEN GTPYWLAANS 310 320 330 340 WNTDWGITGF FKILRGEDHC GIESEIVAGV PRMEQYWTRV

References

[1]	"Avian cathepsin B cDNA: sequence and demonstration that mRNAs of two sizes are produced in cell types producing large quantities of the enzyme." Dong S.S., Stransky G.I., Whitaker C.H., Jordan S.E., Schlesinger P.H., Edwards J.C., Blair H.C. Biochim. Biophys. Acta 1251:69-73(1995) [PubMed: 7647095] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: White leghorn. Tissue: Bone.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U18083 mRNA. Translation: AAA87075.1.
IPI	IPI00573387.
PIR	S58770.
RefSeq	NP_990702.1. NM_205371.1.
UniGene	Gga.3854.
3D structure databases
ProteinModelPortal	P43233.
SMR	P43233. Positions 18-334.
ModBase	Search...
Protein-protein interaction databases
STRING	P43233.
Protein family/group databases
MEROPS	C01.060.
Proteomic databases
PRIDE	P43233.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396329.
KEGG	gga:396329.
Organism-specific databases
CTD	1508.
Phylogenomic databases
eggNOG	veNOG09181.
HOGENOM	HBG385498.
HOVERGEN	HBG003480.
InParanoid	P43233.
OrthoDB	EOG4K6G4C.
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]
KO	K01363.
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.
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...

Entry information

Entry name

CATB_CHICK

Accession

Primary (citable) accession number: P43233

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program