Reviewed, UniProtKB/Swiss-Prot Q5R6D1 (CATB_PONAB)

Names and origin

Protein names

Recommended name:
    Cathepsin B
    EC=3.4.22.1
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

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

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 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 By similarity.
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 By similarity.
Subcellular location	Lysosome By similarity. 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 electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
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 By similarity		PRO_0000330880
	Chain	80 – 333	254	Cathepsin B		PRO_0000330881
	Chain	80 – 126	47	Cathepsin B light chain By similarity		PRO_0000330882
	Chain	129 – 333	205	Cathepsin B heavy chain By similarity		PRO_0000330883
	Propeptide	334 – 339	6	By similarity		PRO_0000330884
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...) Potential
	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

Sequences

	Sequence		Length	Mass (Da)
	Q5R6D1-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 18EC5EFC7B2C6455	FASTA	339	37,820
	10 20 30 40 50 60 MWQLWASLCC LLALADARSR PSFHPLSDEL VNYVNKRNTT WQAGHNFYNV DVSYLKKLCG 70 80 90 100 110 120 TFLGGPKPPQ RVMFTEDLKL PESFDAREQW PQCPTIKEIR DQGSCGSCWA FGAVEAISDR 130 140 150 160 170 180 ICIHTNAHVS VEVSAEDLLT CCGSMCGDGC NGGYPAEAWN FWTRKGLVSG GLYESHVGCR 190 200 210 220 230 240 PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSERDIM 250 260 270 280 290 300 AEIYKNGPVE GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW 310 320 330 NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR860464 mRNA. Translation: CAH92586.1. CR860560 mRNA. Translation: CAH92685.1.
RefSeq	NP_001126573.1.
UniGene	Pab.17972
3D structure databases
HSSP	HSSP built from PDB template 1HUC based on UniProtKB P07858.
SMR	Q5R6D1. Positions 18-333.
ModBase	Search...
Protein family/group databases
MEROPS	C01.060.
Genome annotation databases
GeneID	100173564.
Organism-specific databases
CTD	100173564.
Phylogenomic databases
HOVERGEN	Q5R6D1.
InParanoid	Q5R6D1.
OMA	YDSHVGC.
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.
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_PONAB

Accession

Primary (citable) accession number: Q5R6D1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	December 21, 2004
Last modified:	December 15, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)