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A1E295 (CATB_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin B

EC=3.4.22.1

Cleaved into the following 2 chains:

  1. Cathepsin B light chain
  2. Cathepsin B heavy chain
Gene names
Name:CTSB
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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

Interacts with SRPX2. 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. Secretedextracellular space Ref.2.

Tissue specificity

Expressed in heart (at protein level). Ref.2

Sequence similarities

Belongs to the peptidase C1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 7962Activation peptide By similarity
PRO_0000330885
Chain80 – 332253Cathepsin B
PRO_0000330886
Chain80 – 12647Cathepsin B light chain By similarity
PRO_0000330887
Chain129 – 332204Cathepsin B heavy chain By similarity
PRO_0000330888
Propeptide333 – 3353 By similarity
PRO_0000330889

Sites

Active site1081 By similarity
Active site2781 By similarity
Active site2981 By similarity

Amino acid modifications

Modified residue2201N6-acetyllysine By similarity
Glycosylation1921N-linked (GlcNAc...)
Disulfide bond93 ↔ 122 By similarity
Disulfide bond105 ↔ 150 By similarity
Disulfide bond141 ↔ 207 By similarity
Disulfide bond142 ↔ 146 By similarity
Disulfide bond179 ↔ 211 By similarity
Disulfide bond187 ↔ 198 By similarity
Disulfide bond227 ↔ 331 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1E295 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: D94E13E44822C19D

FASTA33536,901
        10         20         30         40         50         60 
MWRLLATLSC LVLLTSARES LHFQPLSDEL VNFINKQNTT WTAGHNFYNV DLSYVKKLCG 

        70         80         90        100        110        120 
TFLGGPKLPQ RAAFAADMIL PKSFDAREQW PNCPTIKEIR DQGSCGSCWA FGAVEAISDR 

       130        140        150        160        170        180 
ICIRSNGRVN VEVSAEDMLT CCGDECGDGC NGGFPSGAWN FWTKKGLVSG GLYDSHVGCR 

       190        200        210        220        230        240 
PYSIPPCEHH VNGSRPPCTG EGDTPKCSKI CEPGYTPSYK EDKHFGCSSY SISRNEKEIM 

       250        260        270        280        290        300 
AEIYKNGPVE GAFTVYSDFL QYKSGVYQHV TGDLMGGHAI RILGWGVENG TPYWLVGNSW 

       310        320        330 
NTDWGDNGFF KILRGQDHCG IESEIVAGIP CTPHF 

« Hide

References

[1]"Molecular cloning and polymorphism of cathepsin B (CTSB) gene in porcine."
Chen L., Li X.W., Zhu L., Li Q., Li M.Z.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Proteomics analysis of cardiac extracellular matrix remodeling in a porcine model of ischemia/reperfusion injury."
Barallobre-Barreiro J., Didangelos A., Schoendube F.A., Drozdov I., Yin X., Fernandez-Caggiano M., Willeit P., Puntmann V.O., Aldama-Lopez G., Shah A.M., Domenech N., Mayr M.
Circulation 125:789-802(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF095956 mRNA. Translation: ABK96810.1.
RefSeqNP_001090927.1. NM_001097458.1.
XP_005657323.1. XM_005657266.1.
XP_005657324.1. XM_005657267.1.
UniGeneSsc.53773.

3D structure databases

ProteinModelPortalA1E295.
SMRA1E295. Positions 18-332.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC01.060.

Proteomic databases

PRIDEA1E295.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000026923; ENSSSCP00000024395; ENSSSCG00000023666.
GeneID100037961.
KEGGssc:100037961.

Organism-specific databases

CTD1508.

Phylogenomic databases

GeneTreeENSGT00730000110701.
HOVERGENHBG003480.
KOK01363.
OMACTGEGDT.
OrthoDBEOG7034HR.
TreeFamTF314576.

Gene expression databases

ArrayExpressA1E295.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR015643. Peptidase_C1A_cathepsin-B.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF285. PTHR12411:SF285. 1 hit.
PfamPF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATB_PIG
AccessionPrimary (citable) accession number: A1E295
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries