IAA1_WHEAT
ID IAA1_WHEAT Reviewed; 124 AA.
AC P01085;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Alpha-amylase inhibitor 0.19;
DE AltName: Full=0.19 alpha-AI;
DE Short=0.19 AI;
DE AltName: Allergen=Tri a 28;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3872681; DOI=10.1016/0167-4838(85)90299-7;
RA Maeda K., Wakabayashi S., Matsubara H.;
RT "Complete amino acid sequence of an alpha-amylase inhibitor in wheat kernel
RT (0.19-inhibitor).";
RL Biochim. Biophys. Acta 828:213-221(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kernel;
RX PubMed=9443806; DOI=10.1093/oxfordjournals.jbchem.a021853;
RA Okuda M., Satoh T., Sakurai N., Shibuya K., Kaji H., Samejima T.;
RT "Overexpression in Escherichia coli of chemically synthesized gene for
RT active 0.19 alpha-amylase inhibitor from wheat kernel.";
RL J. Biochem. 122:918-926(1997).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ALLERGEN.
RX PubMed=21623965; DOI=10.1111/j.1365-2222.2011.03766.x;
RA Sotkovsky P., Sklenar J., Halada P., Cinova J., Setinova I., Kainarova A.,
RA Golias J., Pavlaskova K., Honzova S., Tuckova L.;
RT "A new approach to the isolation and characterization of wheat flour
RT allergens.";
RL Clin. Exp. Allergy 41:1031-1043(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=9354618; DOI=10.1021/bi971307m;
RA Oda Y., Matsunaga T., Fukuyama K., Miyazaki T., Morimoto T.;
RT "Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from
RT wheat kernel determined by X-ray analysis at 2.06-A resolution.";
RL Biochemistry 36:13503-13511(1997).
CC -!- FUNCTION: Alpha-amylase inhibitor.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Endosperm.
CC -!- PTM: The disulfide bonds are essential for the inhibitor activity.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:21623965}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha-
CC amylase inhibitor) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB003682; BAA20139.1; -; mRNA.
DR PIR; A01324; WIWTA1.
DR PDB; 1HSS; X-ray; 2.06 A; A/B/C/D=1-124.
DR PDBsum; 1HSS; -.
DR AlphaFoldDB; P01085; -.
DR SMR; P01085; -.
DR Allergome; 8186; Tri a 28.
DR PRIDE; P01085; -.
DR EvolutionaryTrace; P01085; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P01085; baseline.
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:0019863; F:IgE binding; IDA:UniProtKB.
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; 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 SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
DR PROSITE; PS00426; CEREAL_TRYP_AMYL_INH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Alpha-amylase inhibitor; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted.
FT CHAIN 1..124
FT /note="Alpha-amylase inhibitor 0.19"
FT /id="PRO_0000070484"
FT DISULFID 6..52
FT /evidence="ECO:0000269|PubMed:9354618,
FT ECO:0007744|PDB:1HSS"
FT DISULFID 20..41
FT /evidence="ECO:0000269|PubMed:9354618,
FT ECO:0007744|PDB:1HSS"
FT DISULFID 28..83
FT /evidence="ECO:0000269|PubMed:9354618,
FT ECO:0007744|PDB:1HSS"
FT DISULFID 42..99
FT /evidence="ECO:0000269|PubMed:9354618,
FT ECO:0007744|PDB:1HSS"
FT DISULFID 54..115
FT /evidence="ECO:0000269|PubMed:9354618,
FT ECO:0007744|PDB:1HSS"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:1HSS"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:1HSS"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1HSS"
FT HELIX 35..46
FT /evidence="ECO:0007829|PDB:1HSS"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1HSS"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:1HSS"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:1HSS"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:1HSS"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1HSS"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1HSS"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:1HSS"
SQ SEQUENCE 124 AA; 13337 MW; 97A8FB07D5A7788B CRC64;
SGPWMCYPGQ AFQVPALPAC RPLLRLQCNG SQVPEAVLRD CCQQLAHISE WCRCGALYSM
LDSMYKEHGA QEGQAGTGAF PRCRREVVKL TAASITAVCR LPIVVDASGD GAYVCKDVAA
YPDA
