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Protein

Cathepsin B

Gene

CTSB

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 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.

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081By similarity
Active sitei279 – 2791By similarity
Active sitei299 – 2991By similarity

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)
Alternative name(s):
Cathepsin B1
Cleaved into the following 2 chains:
Gene namesi
Name:CTSB
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Propeptidei18 – 7962Activation peptideSequence analysisPRO_0000026158Add
BLAST
Chaini80 – 340261Cathepsin BPRO_0000026159Add
BLAST
Chaini80 – 12647Cathepsin B light chainBy similarityPRO_0000026160Add
BLAST
Chaini129 – 340212Cathepsin B heavy chainBy similarityPRO_0000026161Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi93 ↔ 122By similarity
Disulfide bondi105 ↔ 150By similarity
Disulfide bondi141 ↔ 208By similarity
Disulfide bondi142 ↔ 146By similarity
Disulfide bondi179 ↔ 212By similarity
Disulfide bondi187 ↔ 198By similarity
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP43233.
PRIDEiP43233.

Interactioni

Subunit structurei

Dimer of a heavy chain and a light chain cross-linked by a disulfide bond.

Protein-protein interaction databases

STRINGi9031.ENSGALP00000035934.

Structurei

3D structure databases

ProteinModelPortaliP43233.
SMRiP43233. Positions 18-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiP43233.
PhylomeDBiP43233.

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.

P43233-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWSRSILCL LGAFANARSI PYYPPLSSDL VNHINKLNTT GRAGHNFHNT
60 70 80 90 100
DMSYVKKLCG TFLGGPKAPE RVDFAEDMDL PDTFDTRKQW PNCPTISEIR
110 120 130 140 150
DQGSCGSCWA FGAVEAISDR ICVHTNAKVS VEVSAEDLLS CCGFECGMGC
160 170 180 190 200
NGGYPSGAWR YWTERGLVSG GLYDSHVGCR AYTIPPCEHH VNGSRPPCTG
210 220 230 240 250
EGGETPRCSR HCEPGYSPSY KEDKHYGITS YGVPRSEKEI MAEIYKNGPV
260 270 280 290 300
EGAFIVYEDF LMYKSGVYQH VSGEQVGGHA IRILGWGVEN GTPYWLAANS
310 320 330 340
WNTDWGITGF FKILRGEDHC GIESEIVAGV PRMEQYWTRV
Length:340
Mass (Da):37,587
Last modified:November 1, 1995 - v1
Checksum:iFCD7178ABB167704
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18083 mRNA. Translation: AAA87075.1.
PIRiS58770.
UniGeneiGga.3854.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18083 mRNA. Translation: AAA87075.1.
PIRiS58770.
UniGeneiGga.3854.

3D structure databases

ProteinModelPortaliP43233.
SMRiP43233. Positions 18-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000035934.

Protein family/group databases

MEROPSiC01.060.

Proteomic databases

PaxDbiP43233.
PRIDEiP43233.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiP43233.
PhylomeDBiP43233.

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_CHICK
AccessioniPrimary (citable) accession number: P43233
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.