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Protein

Cathepsin B

Gene

CTSB

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei108By similarity1
Active sitei278By similarity1
Active sitei298By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Protein family/group databases

MEROPSiC01.060.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin B (EC:3.4.22.1)
Cleaved into the following 2 chains:
Gene namesi
Name:CTSB
ORF Names:QccE-13673
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000033087518 – 79Activation peptideBy similarityAdd BLAST62
ChainiPRO_000033087680 – 333Cathepsin BAdd BLAST254
ChainiPRO_000033087780 – 126Cathepsin B light chainBy similarityAdd BLAST47
ChainiPRO_0000330878129 – 333Cathepsin B heavy chainBy similarityAdd BLAST205
PropeptideiPRO_0000330879334 – 339By similarity6

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi93 ↔ 122By similarity
Disulfide bondi105 ↔ 150By similarity
Disulfide bondi141 ↔ 207By similarity
Disulfide bondi142 ↔ 146By similarity
Disulfide bondi179 ↔ 211By similarity
Disulfide bondi187 ↔ 198By similarity
Glycosylationi192N-linked (GlcNAc...)Sequence analysis1
Modified residuei220N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiQ4R5M2.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ4R5M2. 1 interactor.
MINTiMINT-7266161.

Structurei

3D structure databases

ProteinModelPortaliQ4R5M2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG003480.
KOiK01363.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4R5M2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWWLWASLCC LLALGDARSR PSFHPLSDEL VNYVNKQNTT WQAGHNFYNV
60 70 80 90 100
DVSYLKRLCG TFLGGPKPPQ RVMFTEDLKL PESFDAREQW PQCPTIKEIR
110 120 130 140 150
DQGSCGSCWA FGAVEAISDR ICIHTNAHVS VEVSAEDLLT CCGIMCGDGC
160 170 180 190 200
NGGYPAGAWN FWTRKGLVSG GLYDSHVGCR PYSIPPCEHH VNGSRPPCTG
210 220 230 240 250
EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSEKDIM AEIYKNGPVE
260 270 280 290 300
GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW
310 320 330
NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI
Length:339
Mass (Da):37,776
Last modified:July 19, 2005 - v1
Checksum:i57D18B0CE1CD56CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB169521 mRNA. Translation: BAE01603.1.
RefSeqiNP_001270414.1. NM_001283485.1.
UniGeneiMfa.8363.

Genome annotation databases

GeneIDi101865017.
KEGGimcf:101865017.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB169521 mRNA. Translation: BAE01603.1.
RefSeqiNP_001270414.1. NM_001283485.1.
UniGeneiMfa.8363.

3D structure databases

ProteinModelPortaliQ4R5M2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ4R5M2. 1 interactor.
MINTiMINT-7266161.

Protein family/group databases

MEROPSiC01.060.

Proteomic databases

PRIDEiQ4R5M2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101865017.
KEGGimcf:101865017.

Organism-specific databases

CTDi1508.

Phylogenomic databases

HOVERGENiHBG003480.
KOiK01363.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATB_MACFA
AccessioniPrimary (citable) accession number: Q4R5M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: July 19, 2005
Last modified: October 5, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.