ID   IAA2_HORVU              Reviewed;         152 AA.
AC   P13691;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Alpha-amylase inhibitor BDAI-1;
DE   Flags: Precursor;
GN   Name=IAD1;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 31-53.
RC   STRAIN=cv. Bomi;
RX   PubMed=3257914; DOI=10.1111/j.1432-1033.1988.tb13864.x;
RA   Lazaro A., Sanchez-Monge R., Salcedo G., Paz-Ares J., Carbonero P.,
RA   Garcia-Olmedo F.;
RT   "A dimeric inhibitor or insect alpha-amylase from barley. Cloning of the
RT   cDNA and identification of the protein.";
RL   Eur. J. Biochem. 172:129-134(1988).
CC   -!- FUNCTION: Could be involved in insect defense mechanisms. Inhibits
CC       insect-type alpha-amylase.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Endosperm.
CC   -!- PTM: Five disulfide bonds are present (Probable), which are essential
CC       for the inhibitor activity.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha-
CC       amylase inhibitor) family. {ECO:0000305}.
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DR   PIR; S00332; S00332.
DR   AlphaFoldDB; P13691; -.
DR   SMR; P13691; -.
DR   Allergome; 8778; Hor v BDAI.
DR   EnsemblPlants; HORVU.MOREX.r2.6HG0448020.1; HORVU.MOREX.r2.6HG0448020.1.CDS.1; HORVU.MOREX.r2.6HG0448020.
DR   EnsemblPlants; HORVU.MOREX.r2.6HG0448020.1.mrna1; HORVU.MOREX.r2.6HG0448020.1.mrna1.cds1; HORVU.MOREX.r2.6HG0448020.1.
DR   Gramene; HORVU.MOREX.r2.6HG0448020.1; HORVU.MOREX.r2.6HG0448020.1.CDS.1; HORVU.MOREX.r2.6HG0448020.
DR   Gramene; HORVU.MOREX.r2.6HG0448020.1.mrna1; HORVU.MOREX.r2.6HG0448020.1.mrna1.cds1; HORVU.MOREX.r2.6HG0448020.1.
DR   ExpressionAtlas; P13691; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0015066; F:alpha-amylase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd00261; AAI_SS; 1.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR044723; AAI_SS_dom.
DR   InterPro; IPR002411; Allergen/amylase_inhib_rice.
DR   InterPro; IPR006106; Allergen/soft/tryp_amyl_inhib.
DR   InterPro; IPR006105; Allergen/tryp_amyl_inhib_CS.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PIRSF; PIRSF001657; Allergen/amylase_inhib; 1.
DR   PRINTS; PR00808; AMLASEINHBTR.
DR   PRINTS; PR00809; RAGALLERGEN.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
DR   PROSITE; PS00426; CEREAL_TRYP_AMYL_INH; 1.
PE   1: Evidence at protein level;
KW   Alpha-amylase inhibitor; Direct protein sequencing; Disulfide bond;
KW   Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000269|PubMed:3257914"
FT   CHAIN           31..152
FT                   /note="Alpha-amylase inhibitor BDAI-1"
FT                   /id="PRO_0000014356"
SQ   SEQUENCE   152 AA;  16429 MW;  6D7271A1EAE07761 CRC64;
     MGAMWMKSML LVLLLCMLMV TPMTGARSDN SGPWMWCDPE MGHKVSPLTR CRALVKLECV
     GNRVPEDVLR DCCQEVANIS NEWCRCGDLG SMLRSVYAAL GVGGGPEEVF PGCQKDVMKL
     LVAGVPALCN VPIPNEAAGT RGVCYWSAST DT