IAA2_WHEAT
ID IAA2_WHEAT Reviewed; 153 AA.
AC P01083; O49956; Q99300;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 3.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Alpha-amylase inhibitor 0.28;
DE AltName: Full=CIII;
DE AltName: Full=WMAI-1;
DE Flags: Precursor;
GN Name=IMA1;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Chinese Spring; TISSUE=Endosperm;
RA Carbonero P.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 31-153.
RA Kashlan N., Richardson M.;
RT "The complete amino acid sequence of a major wheat protein inhibitor of
RT alpha-amylase.";
RL Phytochemistry 20:1781-1784(1981).
RN [3]
RP PROTEIN SEQUENCE OF 31-153, AND DISULFIDE BONDS.
RC STRAIN=cv. Pastore;
RX PubMed=1868845; DOI=10.1111/j.1432-1033.1991.tb16159.x;
RA Poerio E., Caporale C., Carrano L., Pucci P., Buonocore V.;
RT "Assignment of the five disulfide bridges in an alpha-amylase inhibitor
RT from wheat kernel by fast-atom-bombardment mass spectrometry and Edman
RT degradation.";
RL Eur. J. Biochem. 199:595-600(1991).
RN [4]
RP PROTEIN SEQUENCE OF 31-153.
RX PubMed=1717975;
RA Caporale C., Carrano L., Nitti G., Poerio E., Pucci P., Buonocore V.;
RT "Determination of the primary structure of an alpha-amylase inhibitor from
RT wheat kernel by Edman degradation and fast atom bombardment mass
RT spectrometry.";
RL Protein Seq. Data Anal. 4:3-8(1991).
RN [5]
RP PROTEIN SEQUENCE OF 31-54.
RX PubMed=938475; DOI=10.1042/bj1550193;
RA Redman D.G.;
RT "N-terminal amino acid sequence of wheat proteins that lack phenylalanine
RT and histidine residues.";
RL Biochem. J. 155:193-195(1976).
RN [6]
RP MUTAGENESIS OF SER-31; TRP-34; GLY-61; GLU-66; ASP-88 AND 99-GLU-LEU-100.
RX PubMed=1932677; DOI=10.1007/bf00037140;
RA Garcia-Maroto F., Carbonero P., Garcia-Olmedo F.;
RT "Site-directed mutagenesis and expression in Escherichia coli of WMAI-1, a
RT wheat monomeric inhibitor of insect alpha-amylase.";
RL Plant Mol. Biol. 17:1005-1011(1991).
CC -!- FUNCTION: Alpha-amylase inhibitor.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Endosperm.
CC -!- PTM: The disulfide bonds are essential 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 EMBL; AJ223492; CAA11410.1; -; mRNA.
DR PIR; A01322; WIWTA.
DR PIR; S16920; S16920.
DR PIR; T06517; T06517.
DR AlphaFoldDB; P01083; -.
DR SMR; P01083; -.
DR Allergome; 8725; Tri a 15.
DR PRIDE; P01083; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P01083; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0015066; F:alpha-amylase inhibitor activity; 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 Alpha-amylase inhibitor; Direct protein sequencing; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:1717975,
FT ECO:0000269|PubMed:1868845, ECO:0000269|PubMed:938475,
FT ECO:0000269|Ref.2"
FT CHAIN 31..153
FT /note="Alpha-amylase inhibitor 0.28"
FT /id="PRO_0000070485"
FT DISULFID 37..84
FT /evidence="ECO:0000269|PubMed:1868845"
FT DISULFID 51..72
FT /evidence="ECO:0000269|PubMed:1868845"
FT DISULFID 59..112
FT /evidence="ECO:0000269|PubMed:1868845"
FT DISULFID 73..128
FT /evidence="ECO:0000269|PubMed:1868845"
FT DISULFID 86..143
FT /evidence="ECO:0000269|PubMed:1868845"
FT VARIANT 95
FT /note="S -> A (in 50% of the molecules)"
FT VARIANT 97
FT /note="Y -> A (in very small amount)"
FT VARIANT 128..129
FT /note="CK -> GP (in very small amount)"
FT MUTAGEN 31
FT /note="S->ARIRAR: Increases preincubation time required for
FT maximum activity."
FT /evidence="ECO:0000269|PubMed:1932677"
FT MUTAGEN 34
FT /note="W->WEPRAPW: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:1932677"
FT MUTAGEN 34
FT /note="W->WGPRLPW: Increases preincubation time required
FT for maximum activity."
FT /evidence="ECO:0000269|PubMed:1932677"
FT MUTAGEN 61
FT /note="G->GIGPRL,GIGPPL,GIGPLL: Little effect on activity."
FT /evidence="ECO:0000269|PubMed:1932677"
FT MUTAGEN 66
FT /note="E->EGPRLPE,EEPRAPE: Little effect on activity."
FT /evidence="ECO:0000269|PubMed:1932677"
FT MUTAGEN 88
FT /note="D->EGPRL,DDGP,DD: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:1932677"
FT MUTAGEN 99..100
FT /note="EL->GASGPSLG,GASGP: Little effect on activity."
FT /evidence="ECO:0000269|PubMed:1932677"
FT CONFLICT 38
FT /note="N -> D (in Ref. 1; CAA11410 and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="Y -> W (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 145..146
FT /note="Missing (in Ref. 1; CAA11410)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="A -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 16800 MW; 05A680B728FC8377 CRC64;
MWMKTVFWGL LVFMLVATTM AVEYGARSHN SGPWSWCNPA TGYKVSALTG CRAMVKLQCV
GSQVPEAVLR DCCQQLADIN NEWCRCGDLS SMLRSVYQEL GVREGKEVLP GCRKEVMKLT
AASVPEVCKV PIPNPSGDRA GVCYGDWAAY PDV
