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P01062

- IBB_VIGRR

UniProt

P01062 - IBB_VIGRR

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Protein
Bowman-Birk type trypsin inhibitor
Gene
N/A
Organism
Vigna radiata var. radiata (Mung bean) (Phaseolus aureus)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei20 – 212Reactive bond for trypsin
Sitei47 – 482Reactive bond for trypsin

GO - Molecular functioni

  1. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Protein family/group databases

    MEROPSiI12.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bowman-Birk type trypsin inhibitor
    OrganismiVigna radiata var. radiata (Mung bean) (Phaseolus aureus)
    Taxonomic identifieri3916 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeVigna

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: InterPro
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7272Bowman-Birk type trypsin inhibitor
    PRO_0000105849Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi12 ↔ 66 By similarity
    Disulfide bondi13 ↔ 28 By similarity
    Disulfide bondi16 ↔ 62 By similarity
    Disulfide bondi18 ↔ 26
    Disulfide bondi36 ↔ 43 By similarity
    Disulfide bondi40 ↔ 55 By similarity
    Disulfide bondi45 ↔ 53 By similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 237
    Beta strandi26 – 283
    Beta strandi32 – 343
    Beta strandi43 – 508
    Beta strandi52 – 554
    Beta strandi59 – 613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G9IX-ray2.20I10-31[»]
    1SBWX-ray1.80I8-69[»]
    1SMFX-ray2.10I10-31[»]
    3MYWX-ray2.50I1-72[»]
    ProteinModelPortaliP01062.
    SMRiP01062. Positions 1-71.

    Miscellaneous databases

    EvolutionaryTraceiP01062.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di2.10.69.10. 1 hit.
    InterProiIPR000877. Prot_inh_BBI.
    [Graphical view]
    PfamiPF00228. Bowman-Birk_leg. 2 hits.
    [Graphical view]
    SMARTiSM00269. BowB. 1 hit.
    [Graphical view]
    SUPFAMiSSF57247. SSF57247. 1 hit.
    PROSITEiPS00281. BOWMAN_BIRK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P01062-1 [UniParc]FASTAAdd to Basket

    « Hide

    SHDEPSESSE PCCDSCDCTK SIPPECHCAN IRLNSCHSAC KSCICTRSMP   50
    GKCRCLDTDD FCYKPCESMD KD 72
    Length:72
    Mass (Da):7,959
    Last modified:February 1, 1995 - v2
    Checksum:i8359DE1A8E61E4F8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1 – 22Missing in 2nd and 3rd isoinhibitor.
    Natural varianti2 – 21H → D in 1st isoinhibitor.
    Natural varianti3 – 31D → K in 3rd isoinhibitor.

    Sequence databases

    PIRiA01301. TIMB.

    Cross-referencesi

    Sequence databases

    PIRi A01301. TIMB.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G9I X-ray 2.20 I 10-31 [» ]
    1SBW X-ray 1.80 I 8-69 [» ]
    1SMF X-ray 2.10 I 10-31 [» ]
    3MYW X-ray 2.50 I 1-72 [» ]
    ProteinModelPortali P01062.
    SMRi P01062. Positions 1-71.
    ModBasei Search...

    Protein family/group databases

    MEROPSi I12.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P01062.

    Family and domain databases

    Gene3Di 2.10.69.10. 1 hit.
    InterProi IPR000877. Prot_inh_BBI.
    [Graphical view ]
    Pfami PF00228. Bowman-Birk_leg. 2 hits.
    [Graphical view ]
    SMARTi SM00269. BowB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57247. SSF57247. 1 hit.
    PROSITEi PS00281. BOWMAN_BIRK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete amino acid sequence of mung bean trypsin inhibitor."
      Zhang Y., Luo S., Tan F., Qi Z., Xu L., Zhang A.
      Sci. Sin., Ser. B Chem. Biol. Agric. Med. Earth Sci. 25:268-277(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    2. "Studies on an artificial trypsin inhibitor peptide derived from the mung bean trypsin inhibitor: chemical synthesis, refolding, and crystallographic analysis of its complex with trypsin."
      Li Y., Huang Q., Zhang S., Liu S., Qi C., Tang Y.
      J. Biochem. 116:18-25(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 10-31, SEQUENCE REVISION.

    Entry informationi

    Entry nameiIBB_VIGRR
    AccessioniPrimary (citable) accession number: P01062
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: February 1, 1995
    Last modified: July 9, 2014
    This is version 80 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Functionally this inhibitor is unusual in that it stoichiometrically inhibits trypsin in a molar ratio of 1:2.
    The specificities and functions of this superfamily of inhibitors depend not only on the active sites within the domains, but also upon the amino acid composition, and resulting molecular conformation, surrounding these regions.
    Three isoinhibitors are also found whose amino ends differ slightly from that shown.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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