IAAA_HORVU
ID IAAA_HORVU Reviewed; 145 AA.
AC P28041;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Alpha-amylase/trypsin inhibitor CMa;
DE AltName: Full=Chloroform/methanol-soluble protein CMa;
DE Flags: Precursor;
GN Name=IAT1;
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 [MRNA].
RC STRAIN=cv. Abyssinian; TISSUE=Endosperm;
RX PubMed=8219088; DOI=10.1007/bf00019301;
RA Medina-Alcazar J., Hueros G., Carbonero P.;
RT "Cloning of cDNA, expression, and chromosomal location of genes encoding
RT the three types of subunits of the barley tetrameric inhibitor of insect
RT alpha-amylase.";
RL Plant Mol. Biol. 23:535-542(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Bomi; TISSUE=Seed;
RX PubMed=1732002; DOI=10.1007/bf00034972;
RA Rasmussen S.K., Johansson A.;
RT "Nucleotide sequence of a cDNA coding for the barley seed protein CMa: an
RT inhibitor of insect alpha-amylase.";
RL Plant Mol. Biol. 18:423-427(1992).
RN [3]
RP PROTEIN SEQUENCE OF 26-47.
RX PubMed=3484638; DOI=10.1016/0167-4838(86)90318-3;
RA Barber D., Sanchez-Monge R., Mendez E., Lazaro A., Garcia-Olmedo F.,
RA Salcedo G.;
RT "New alpha-amylase and trypsin inhibitors among the CM-proteins of barley
RT (Hordeum vulgare).";
RL Biochim. Biophys. Acta 869:115-118(1986).
RN [4]
RP PROTEIN SEQUENCE OF 26-47.
RC STRAIN=cv. H354-295-2-5; TISSUE=Starchy endosperm;
RX PubMed=8125056; DOI=10.1002/elps.11501401169;
RA Flengsrud R.;
RT "Separation of acidic barley endosperm proteins by two-dimensional
RT electrophoresis.";
RL Electrophoresis 14:1060-1066(1993).
CC -!- FUNCTION: Alpha-amylase/trypsin inhibitor. It could be involved in
CC insect defense mechanisms.
CC -!- SUBUNIT: Heterotetramer of one CMa, one CMb and two CMd chains.
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 EMBL; X69937; CAA49555.1; -; mRNA.
DR EMBL; X59264; CAA41956.1; -; mRNA.
DR PIR; S39560; S39560.
DR AlphaFoldDB; P28041; -.
DR SMR; P28041; -.
DR MEROPS; I06.004; -.
DR ExpressionAtlas; P28041; 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:UniProtKB-KW.
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 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 Protease inhibitor; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:3484638,
FT ECO:0000269|PubMed:8125056"
FT CHAIN 26..145
FT /note="Alpha-amylase/trypsin inhibitor CMa"
FT /id="PRO_0000014350"
FT CONFLICT 24
FT /note="T -> A (in Ref. 2; CAA41956)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..89
FT /note="EA -> R (in Ref. 2; CAA41956)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="S -> R (in Ref. 2; CAA41956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 15500 MW; 0AAD9F62423F3600 CRC64;
MASKSSITPL LLAAVLASVF AAATATGQYC YAGMGLPSNP LEGCREYVAQ QTCGVTIAGS
PVSSEPGDTP KDRCCQELDE APQHCRCEAV RYFIGRRSHP DWSVLKDLPG CPKEPQRDFA
KVLVTPGQCN VLTVHNAPYC LGLDI