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P01087

- IAAT_ELECO

UniProt

P01087 - IAAT_ELECO

Protein

Alpha-amylase/trypsin inhibitor

Gene
N/A
Organism
Eleusine coracana (Indian finger millet) (Ragi)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    May play a protective role against endo- and exogenous hydrolytic activities in the Ragi seeds.

    GO - Molecular functioni

    1. alpha-amylase inhibitor activity Source: UniProtKB-KW
    2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Alpha-amylase inhibitor, Protease inhibitor, Serine protease inhibitor

    Protein family/group databases

    MEROPSiI06.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylase/trypsin inhibitor
    Short name:
    RBI
    Alternative name(s):
    RATI
    OrganismiEleusine coracana (Indian finger millet) (Ragi)
    Taxonomic identifieri4511 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladeChloridoideaeCynodonteaeEleusininaeEleusine

    Organism-specific databases

    GrameneiP01087.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 122122Alpha-amylase/trypsin inhibitorPRO_0000070490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi6 ↔ 55
    Disulfide bondi20 ↔ 44
    Disulfide bondi29 ↔ 85
    Disulfide bondi45 ↔ 103
    Disulfide bondi57 ↔ 114

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Seeds.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-1537215.

    Structurei

    Secondary structure

    1
    122
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 54
    Turni9 – 113
    Turni16 – 183
    Helixi19 – 2911
    Beta strandi32 – 354
    Helixi37 – 5014
    Turni53 – 553
    Helixi56 – 649
    Helixi87 – 937
    Helixi94 – 963
    Turni100 – 1034
    Beta strandi110 – 1123
    Beta strandi115 – 1173

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B1UX-ray2.20A1-122[»]
    1BIPNMR-A1-122[»]
    1TMQX-ray2.50B1-117[»]
    ProteinModelPortaliP01087.
    SMRiP01087. Positions 3-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01087.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di1.10.120.10. 1 hit.
    InterProiIPR006106. Allergen/soft/tryp_amyl_inhib.
    IPR006105. Allergen/tryp_amyl_inhib_CS.
    IPR016140. Bifunc_inhib/LTP/seed_store.
    IPR013771. Trypsin/amylase_inhib.
    [Graphical view]
    PfamiPF00234. Tryp_alpha_amyl. 1 hit.
    [Graphical view]
    PRINTSiPR00808. AMLASEINHBTR.
    SMARTiSM00499. AAI. 1 hit.
    [Graphical view]
    SUPFAMiSSF47699. SSF47699. 1 hit.
    PROSITEiPS00426. CEREAL_TRYP_AMYL_INH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P01087-1 [UniParc]FASTAAdd to Basket

    « Hide

    SVGTSCIPGM AIPHNPLDSC RWYVSTRTCG VGPRLATQEM KARCCRQLEA    50
    IPAYCRCEAV RILMDGVVTP SGQHEGRLLQ DLPGCPRQVQ RAFAPKLVTE 100
    VECNLATIHG GPFCLSLLGA GE 122
    Length:122
    Mass (Da):13,138
    Last modified:July 15, 1998 - v2
    Checksum:iC8ED7A01CD470E17
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 262ST → AK.
    Natural varianti28 – 281T → A.
    Natural varianti70 – 701P → S.

    Sequence databases

    PIRiA01326. WIILAI.

    Cross-referencesi

    Sequence databases

    PIRi A01326. WIILAI.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B1U X-ray 2.20 A 1-122 [» ]
    1BIP NMR - A 1-122 [» ]
    1TMQ X-ray 2.50 B 1-117 [» ]
    ProteinModelPortali P01087.
    SMRi P01087. Positions 3-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1537215.

    Protein family/group databases

    MEROPSi I06.003.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Gramenei P01087.

    Miscellaneous databases

    EvolutionaryTracei P01087.

    Family and domain databases

    Gene3Di 1.10.120.10. 1 hit.
    InterProi IPR006106. Allergen/soft/tryp_amyl_inhib.
    IPR006105. Allergen/tryp_amyl_inhib_CS.
    IPR016140. Bifunc_inhib/LTP/seed_store.
    IPR013771. Trypsin/amylase_inhib.
    [Graphical view ]
    Pfami PF00234. Tryp_alpha_amyl. 1 hit.
    [Graphical view ]
    PRINTSi PR00808. AMLASEINHBTR.
    SMARTi SM00499. AAI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47699. SSF47699. 1 hit.
    PROSITEi PS00426. CEREAL_TRYP_AMYL_INH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete amino acid sequence of the bifunctional alpha-amylase/trypsin inhibitor from seeds of ragi (Indian finger millet, Eleusine coracana Gaertn.)."
      Campos F.A.P., Richardson M.
      FEBS Lett. 152:300-304(1983)
      Cited for: PROTEIN SEQUENCE.
      Tissue: Seed.
    2. "A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5-A resolution."
      Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Rueth F.-X., Glockshuber R.
      Structure 6:911-921(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
      Tissue: Seed.
    3. "Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.9-A resolution."
      Gourinath S., Srinivasan A., Singh T.P.
      Acta Crystallogr. D 55:25-30(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
      Tissue: Seed.
    4. "Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution."
      Gourinath S., Alam N., Srinivasan A., Betzel C., Singh T.P.
      Acta Crystallogr. D 56:287-293(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
      Tissue: Seed.
    5. "Determination of the three-dimensional structure of the bifunctional alpha-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy."
      Strobl S., Muehlhahn P., Bernstein R., Wiltscheck R., Maskos K., Wunderlich M., Huber R., Glockshuber R., Holak T.A.
      Biochemistry 34:8281-8293(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
      Tissue: Seed.

    Entry informationi

    Entry nameiIAAT_ELECO
    AccessioniPrimary (citable) accession number: P01087
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    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