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A1E295

- CATB_PIG

UniProt

A1E295 - CATB_PIG

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Protein

Cathepsin B

Gene

CTSB

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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

  1. cysteine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. cellular response to thyroid hormone stimulus Source: Ensembl
  2. collagen catabolic process Source: Ensembl
  3. decidualization Source: Ensembl
  4. epithelial cell differentiation Source: Ensembl
  5. proteolysis involved in cellular protein catabolic process Source: Ensembl
  6. regulation of catalytic activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

ReactomeiREACT_215103. Assembly of collagen fibrils and other multimeric structures.
REACT_215953. Trafficking and processing of endosomal TLR.
REACT_223608. Collagen degradation.

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Chromosome 14

Subcellular locationi

Lysosome By similarity. Melanosome By similarity. Secretedextracellular space 1 Publication

GO - Cellular componenti

  1. extracellular space Source: BHF-UCL
  2. extracellular vesicular exosome Source: Ensembl
  3. lysosome Source: UniProtKB-KW
  4. mitochondrion Source: Ensembl
  5. nucleolus Source: Ensembl
  6. perinuclear region of cytoplasm Source: Ensembl
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_0000330885Add
BLAST
Chaini80 – 332253Cathepsin BPRO_0000330886Add
BLAST
Chaini80 – 12647Cathepsin B light chainBy similarityPRO_0000330887Add
BLAST
Chaini129 – 332204Cathepsin B heavy chainBy similarityPRO_0000330888Add
BLAST
Propeptidei333 – 3353By similarityPRO_0000330889

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...)
Modified residuei220 – 2201N6-acetyllysineBy similarity
Disulfide bondi227 ↔ 331By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiA1E295.

Expressioni

Tissue specificityi

Expressed in heart (at protein level).1 Publication

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiA1E295. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliA1E295.
SMRiA1E295. Positions 18-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00760000118871.
HOVERGENiHBG003480.
InParanoidiA1E295.
KOiK01363.
OMAiCTGEGDT.
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.
IPR015643. Peptidase_C1A_cathepsin-B.
IPR012599. Propeptide_C1A.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PTHR12411:SF285. PTHR12411:SF285. 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.

A1E295-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWRLLATLSC LVLLTSARES LHFQPLSDEL VNFINKQNTT WTAGHNFYNV
60 70 80 90 100
DLSYVKKLCG TFLGGPKLPQ RAAFAADMIL PKSFDAREQW PNCPTIKEIR
110 120 130 140 150
DQGSCGSCWA FGAVEAISDR ICIRSNGRVN VEVSAEDMLT CCGDECGDGC
160 170 180 190 200
NGGFPSGAWN FWTKKGLVSG GLYDSHVGCR PYSIPPCEHH VNGSRPPCTG
210 220 230 240 250
EGDTPKCSKI CEPGYTPSYK EDKHFGCSSY SISRNEKEIM AEIYKNGPVE
260 270 280 290 300
GAFTVYSDFL QYKSGVYQHV TGDLMGGHAI RILGWGVENG TPYWLVGNSW
310 320 330
NTDWGDNGFF KILRGQDHCG IESEIVAGIP CTPHF
Length:335
Mass (Da):36,901
Last modified:January 23, 2007 - v1
Checksum:iD94E13E44822C19D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF095956 mRNA. Translation: ABK96810.1.
RefSeqiNP_001090927.1. NM_001097458.1.
XP_005657323.1. XM_005657266.1.
XP_005657324.1. XM_005657267.1.
UniGeneiSsc.53773.

Genome annotation databases

EnsembliENSSSCT00000026923; ENSSSCP00000024395; ENSSSCG00000023666.
GeneIDi100037961.
KEGGissc:100037961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF095956 mRNA. Translation: ABK96810.1 .
RefSeqi NP_001090927.1. NM_001097458.1.
XP_005657323.1. XM_005657266.1.
XP_005657324.1. XM_005657267.1.
UniGenei Ssc.53773.

3D structure databases

ProteinModelPortali A1E295.
SMRi A1E295. Positions 18-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi A1E295. 2 interactions.

Protein family/group databases

MEROPSi C01.060.

Proteomic databases

PRIDEi A1E295.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSSSCT00000026923 ; ENSSSCP00000024395 ; ENSSSCG00000023666 .
GeneIDi 100037961.
KEGGi ssc:100037961.

Organism-specific databases

CTDi 1508.

Phylogenomic databases

GeneTreei ENSGT00760000118871.
HOVERGENi HBG003480.
InParanoidi A1E295.
KOi K01363.
OMAi CTGEGDT.
OrthoDBi EOG7034HR.
TreeFami TF314576.

Enzyme and pathway databases

Reactomei REACT_215103. Assembly of collagen fibrils and other multimeric structures.
REACT_215953. Trafficking and processing of endosomal TLR.
REACT_223608. Collagen degradation.

Family and domain databases

InterProi IPR025661. 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 ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
PTHR12411:SF285. PTHR12411:SF285. 1 hit.
Pfami PF00112. Peptidase_C1. 1 hit.
PF08127. Propeptide_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiCATB_PIG
AccessioniPrimary (citable) accession number: A1E295
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 50 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

External Data

Dasty 3