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Protein

Cathepsin B

Gene

CTSB

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
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 (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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081By similarity
Active sitei278 – 2781By similarity
Active sitei298 – 2981By 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)
Cleaved into the following 2 chains:
Gene namesi
Name:CTSB
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Chromosome 8

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Propeptidei18 – 7962Activation peptideBy similarityPRO_0000330880Add
BLAST
Chaini80 – 333254Cathepsin BPRO_0000330881Add
BLAST
Chaini80 – 12647Cathepsin B light chainBy similarityPRO_0000330882Add
BLAST
Chaini129 – 333205Cathepsin B heavy chainBy similarityPRO_0000330883Add
BLAST
Propeptidei334 – 3396By similarityPRO_0000330884

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi93 ↔ 122By similarity
Disulfide bondi105 ↔ 150By similarity
Disulfide bondi141 ↔ 207By similarity
Disulfide bondi142 ↔ 146By similarity
Disulfide bondi179 ↔ 211By similarity
Disulfide bondi187 ↔ 198By similarity
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence analysis
Modified residuei220 – 2201N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiQ5R6D1.

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

STRINGi9601.ENSPPYP00000020558.

Structurei

3D structure databases

ProteinModelPortaliQ5R6D1.
SMRiQ5R6D1. Positions 18-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00780000121937.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiQ5R6D1.
KOiK01363.
OMAiEDMLTCC.
OrthoDBiEOG7034HR.
TreeFamiTF314576.

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.

Q5R6D1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWQLWASLCC LLALADARSR PSFHPLSDEL VNYVNKRNTT WQAGHNFYNV
60 70 80 90 100
DVSYLKKLCG TFLGGPKPPQ RVMFTEDLKL PESFDAREQW PQCPTIKEIR
110 120 130 140 150
DQGSCGSCWA FGAVEAISDR ICIHTNAHVS VEVSAEDLLT CCGSMCGDGC
160 170 180 190 200
NGGYPAEAWN FWTRKGLVSG GLYESHVGCR PYSIPPCEHH VNGSRPPCTG
210 220 230 240 250
EGDTPKCSKI CEPGYSPTYK QDKHYGYNSY SVSNSERDIM AEIYKNGPVE
260 270 280 290 300
GAFSVYSDFL LYKSGVYQHV TGEMMGGHAI RILGWGVENG TPYWLVANSW
310 320 330
NTDWGDNGFF KILRGQDHCG IESEVVAGIP RTDQYWEKI
Length:339
Mass (Da):37,820
Last modified:December 21, 2004 - v1
Checksum:i18EC5EFC7B2C6455
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860464 mRNA. Translation: CAH92586.1.
CR860560 mRNA. Translation: CAH92685.1.
RefSeqiNP_001126573.1. NM_001133101.1.

Genome annotation databases

EnsembliENSPPYT00000021385; ENSPPYP00000020558; ENSPPYG00000018345.
GeneIDi100173564.
KEGGipon:100173564.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860464 mRNA. Translation: CAH92586.1.
CR860560 mRNA. Translation: CAH92685.1.
RefSeqiNP_001126573.1. NM_001133101.1.

3D structure databases

ProteinModelPortaliQ5R6D1.
SMRiQ5R6D1. Positions 18-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000020558.

Protein family/group databases

MEROPSiC01.060.

Proteomic databases

PRIDEiQ5R6D1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSPPYT00000021385; ENSPPYP00000020558; ENSPPYG00000018345.
GeneIDi100173564.
KEGGipon:100173564.

Organism-specific databases

CTDi1508.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00780000121937.
HOGENOMiHOG000241341.
HOVERGENiHBG003480.
InParanoidiQ5R6D1.
KOiK01363.
OMAiEDMLTCC.
OrthoDBiEOG7034HR.
TreeFamiTF314576.

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...

Publicationsi

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

Entry informationi

Entry nameiCATB_PONAB
AccessioniPrimary (citable) accession number: Q5R6D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 21, 2004
Last modified: May 11, 2016
This is version 74 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.