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P80403

- IAAI_AMAHP

UniProt

P80403 - IAAI_AMAHP

Protein

Alpha-amylase inhibitor AAI

Gene

AAI

Organism
Amaranthus hypochondriacus (Prince-of-Wales feather)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Alpha-amylase inhibitor. It is active against alpha-amylases from Tribolium castaneum and Prostephanus truncatus larvae.

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Alpha-amylase inhibitor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-amylase inhibitor AAI
    Gene namesi
    Name:AAI
    OrganismiAmaranthus hypochondriacus (Prince-of-Wales feather)
    Taxonomic identifieri28502 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeAmaranthus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3232Alpha-amylase inhibitor AAIPRO_0000084123Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi1 ↔ 181 Publication
    Disulfide bondi8 ↔ 231 Publication
    Disulfide bondi17 ↔ 311 Publication

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Endosperm.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-106908.

    Structurei

    Secondary structure

    1
    32
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83
    Helixi10 – 134
    Beta strandi26 – 316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CLVX-ray2.00I1-32[»]
    1HTXNMR-A1-32[»]
    1QFDNMR-A1-32[»]
    ProteinModelPortaliP80403.
    SMRiP80403. Positions 1-32.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80403.

    Family & Domainsi

    Domaini

    The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.

    Keywords - Domaini

    Knottin

    Family and domain databases

    InterProiIPR011052. Proteinase_amylase_inhib_dom.
    [Graphical view]
    SUPFAMiSSF57027. SSF57027. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P80403-1 [UniParc]FASTAAdd to Basket

    « Hide

    CIPKWNRCGP KMDGVPCCEP YTCTSDYYGN CS                      32
    Length:32
    Mass (Da):3,592
    Last modified:February 1, 1995 - v1
    Checksum:i4B9B744B58C39BE3
    GO

    Sequence databases

    PIRiA54845.

    Cross-referencesi

    Sequence databases

    PIRi A54845.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CLV X-ray 2.00 I 1-32 [» ]
    1HTX NMR - A 1-32 [» ]
    1QFD NMR - A 1-32 [» ]
    ProteinModelPortali P80403.
    SMRi P80403. Positions 1-32.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-106908.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P80403.

    Family and domain databases

    InterProi IPR011052. Proteinase_amylase_inhib_dom.
    [Graphical view ]
    SUPFAMi SSF57027. SSF57027. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "A novel alpha-amylase inhibitor from amaranth (Amaranthus hypocondriacus) seeds."
      Chagolla-Lopez A., Blanco-Labra A., Patthy A., Sanchez R., Pongor S.
      J. Biol. Chem. 269:23675-23680(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, DISULFIDE BONDS.
      Tissue: Seed.
    2. "Solution structure of the major alpha-amylase inhibitor of the crop plant amaranth."
      Lu S., Deng P., Liu X., Luo J., Han R., Gu X., Liang S., Wang X., Li F., Lozanov V., Patthy A., Pongor S.
      J. Biol. Chem. 274:20473-20478(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR, REVISION OF DISULFIDE BONDS.
      Tissue: Seed.

    Entry informationi

    Entry nameiIAAI_AMAHP
    AccessioniPrimary (citable) accession number: P80403
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 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

    External Data

    Dasty 3