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A1E295

- CATB_PIG

UniProt

A1E295 - CATB_PIG

Protein

Cathepsin B

Gene

CTSB

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      Previous versions | rss
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    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. regulation of catalytic activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Enzyme and pathway databases

    ReactomeiREACT_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. lysosome Source: UniProtKB-SubCell
    3. melanosome Source: UniProtKB-SubCell
    4. mitochondrion Source: Ensembl
    5. nucleolus Source: Ensembl
    6. perinuclear region of cytoplasm Source: Ensembl

    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

    Gene expression databases

    ArrayExpressiA1E295.

    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

    GeneTreeiENSGT00730000110701.
    HOVERGENiHBG003480.
    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

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    MWRLLATLSC LVLLTSARES LHFQPLSDEL VNFINKQNTT WTAGHNFYNV    50
    DLSYVKKLCG TFLGGPKLPQ RAAFAADMIL PKSFDAREQW PNCPTIKEIR 100
    DQGSCGSCWA FGAVEAISDR ICIRSNGRVN VEVSAEDMLT CCGDECGDGC 150
    NGGFPSGAWN FWTKKGLVSG GLYDSHVGCR PYSIPPCEHH VNGSRPPCTG 200
    EGDTPKCSKI CEPGYTPSYK EDKHFGCSSY SISRNEKEIM AEIYKNGPVE 250
    GAFTVYSDFL QYKSGVYQHV TGDLMGGHAI RILGWGVENG TPYWLVGNSW 300
    NTDWGDNGFF KILRGQDHCG IESEIVAGIP CTPHF 335
    Length:335
    Mass (Da):36,901
    Last modified:January 23, 2007 - v1
    Checksum:iD94E13E44822C19D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 ENSGT00730000110701.
    HOVERGENi HBG003480.
    KOi K01363.
    OMAi CTGEGDT.
    OrthoDBi EOG7034HR.
    TreeFami TF314576.

    Enzyme and pathway databases

    Reactomei REACT_215953. Trafficking and processing of endosomal TLR.
    REACT_223608. Collagen degradation.

    Gene expression databases

    ArrayExpressi A1E295.

    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: October 1, 2014
    This is version 48 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