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P00767

- CTRB_BOVIN

UniProt

P00767 - CTRB_BOVIN

Protein

Chymotrypsinogen B

Gene
N/A
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    • Comment

    Functioni

    Catalytic activityi

    Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei57 – 571Charge relay system1 Publication
    Active sitei102 – 1021Charge relay system1 Publication
    Active sitei195 – 1951Charge relay system1 Publication

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. digestion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Digestion

    Protein family/group databases

    MEROPSiS01.152.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chymotrypsinogen B (EC:3.4.21.1)
    Cleaved into the following 3 chains:
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1313Chymotrypsin B chain APRO_0000027629Add
    BLAST
    Propeptidei14 – 152PRO_0000027630
    Chaini16 – 146131Chymotrypsin B chain BPRO_0000027631Add
    BLAST
    Propeptidei147 – 1482PRO_0000027632
    Chaini149 – 24597Chymotrypsin B chain CPRO_0000027633Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi1 ↔ 1221 PublicationPROSITE-ProRule annotation
    Disulfide bondi42 ↔ 581 PublicationPROSITE-ProRule annotation
    Disulfide bondi136 ↔ 2011 PublicationPROSITE-ProRule annotation
    Disulfide bondi168 ↔ 1821 PublicationPROSITE-ProRule annotation
    Disulfide bondi191 ↔ 2201 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PRIDEiP00767.

    Interactioni

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CBWX-ray2.60A/F1-13[»]
    1HJAX-ray2.30A1-13[»]
    3BG4X-ray2.50A1-13[»]
    ProteinModelPortaliP00767.
    SMRiP00767. Positions 1-245.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00767.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 243228Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5640.
    HOVERGENiHBG013304.
    InParanoidiP00767.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00767-1 [UniParc]FASTAAdd to Basket

    « Hide

    CGVPAIQPVL SGLARIVNGE DAVPGSWPWQ VSLQDSTGFH FCGGSLISED    50
    WVVTAAHCGV TTSDVVVAGE FDQGLETEDT QVLKIGKVFK NPKFSILTVR 100
    NDITLLKLAT PAQFSETVSA VCLPSADEDF PAGMLCATTG WGKTKYNALK 150
    TPDKLQQATL PIVSNTDCRK YWGSRVTDVM ICAGASGVSS CMGDSGGPLV 200
    CQKNGAWTLA GIVSWGSSTC STSTPAVYAR VTALMPWVQE TLAAN 245
    Length:245
    Mass (Da):25,755
    Last modified:July 21, 1986 - v1
    Checksum:i678016446FF5FEB5
    GO

    Sequence databases

    PIRiA00953. KYBOB.
    UniGeneiBt.107724.

    Cross-referencesi

    Web resourcesi

    Worthington enzyme manual

    Sequence databases

    PIRi A00953. KYBOB.
    UniGenei Bt.107724.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CBW X-ray 2.60 A/F 1-13 [» ]
    1HJA X-ray 2.30 A 1-13 [» ]
    3BG4 X-ray 2.50 A 1-13 [» ]
    ProteinModelPortali P00767.
    SMRi P00767. Positions 1-245.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P00767.
    ChEMBLi CHEMBL3063.

    Protein family/group databases

    MEROPSi S01.152.

    Proteomic databases

    PRIDEi P00767.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG013304.
    InParanoidi P00767.

    Miscellaneous databases

    EvolutionaryTracei P00767.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of chymotrypsinogen B compared with chymotrypsinogen A and trypsinogen."
      Smillie L.B., Furka A., Nagabhushan N., Stevenson K.J., Parkes C.O.
      Nature 218:343-346(1968) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS, ACTIVE SITE.

    Entry informationi

    Entry nameiCTRB_BOVIN
    AccessioniPrimary (citable) accession number: P00767
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 113 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3