ID   IAAD_HORVU              Reviewed;         171 AA.
AC   P11643;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Alpha-amylase/trypsin inhibitor CMd;
DE   AltName: Full=Chloroform/methanol-soluble protein CMd;
DE   Flags: Precursor;
GN   Name=IAT3; Synonyms=CMD2;
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 [GENOMIC DNA].
RC   STRAIN=cv. NK 1558;
RX   PubMed=9207849; DOI=10.1023/a:1005811111719;
RA   Grosset J., Alary R., Gautier M.-F., Menossi M., Martinez-Izquierdo J.A.,
RA   Joudrier P.;
RT   "Characterization of a barley gene coding for an alpha-amylase inhibitor
RT   subunit (CMd protein) and analysis of its promoter in transgenic tobacco
RT   plants and in maize kernels by microprojectile bombardment.";
RL   Plant Mol. Biol. 34:331-338(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 11-171.
RC   STRAIN=cv. Hiproly; TISSUE=Endosperm;
RX   PubMed=3167062; DOI=10.1016/0167-4781(88)90141-8;
RA   Halford N.G., Morris N.A., Urwin P., Williamson M.S., Kasarda D.D.,
RA   Lew E.J.-L., Kreis M., Shewry P.R.;
RT   "Molecular cloning of the barley seed protein CMd: a variant member of the
RT   alpha-amylase/trypsin inhibitor family of cereals.";
RL   Biochim. Biophys. Acta 950:435-440(1988).
RN   [4]
RP   PROTEIN SEQUENCE OF 25-30.
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: Part of a complex with inhibitory activity, but CMd is
CC       inactive as a separate subunit.
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; X69939; CAA49557.1; -; mRNA.
DR   EMBL; U47641; AAB63441.1; -; Genomic_DNA.
DR   EMBL; X13198; CAA31585.1; -; mRNA.
DR   PIR; S78525; S78525.
DR   AlphaFoldDB; P11643; -.
DR   SMR; P11643; -.
DR   MEROPS; I06.004; -.
DR   PRIDE; P11643; -.
DR   EnsemblPlants; HORVU.MOREX.r2.4HG0341150.1; HORVU.MOREX.r2.4HG0341150.1.CDS.1; HORVU.MOREX.r2.4HG0341150.
DR   EnsemblPlants; HORVU.MOREX.r2.4HG0341150.1.mrna1; HORVU.MOREX.r2.4HG0341150.1.mrna1.cds1; HORVU.MOREX.r2.4HG0341150.1.
DR   Gramene; HORVU.MOREX.r2.4HG0341150.1; HORVU.MOREX.r2.4HG0341150.1.CDS.1; HORVU.MOREX.r2.4HG0341150.
DR   Gramene; HORVU.MOREX.r2.4HG0341150.1.mrna1; HORVU.MOREX.r2.4HG0341150.1.mrna1.cds1; HORVU.MOREX.r2.4HG0341150.1.
DR   OMA; PQQCRCE; -.
DR   ExpressionAtlas; P11643; 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..24
FT                   /evidence="ECO:0000269|PubMed:8125056"
FT   CHAIN           25..171
FT                   /note="Alpha-amylase/trypsin inhibitor CMd"
FT                   /id="PRO_0000014352"
SQ   SEQUENCE   171 AA;  18526 MW;  8D8934FED808FED4 CRC64;
     MACKSSRSLL LLATVMVSVF AAAAAAAAAT DCSPGVAFPT NLLGHCRDYV LQQTCAVFTP
     GSKLPEWMTS AELNYPGQPY LAKLYCCQEL AEIPQQCRCE ALRYFMALPV PSQPVDPSTG
     NVGQSGLMDL PGCPREMQRD FVRLLVAPGQ CNLATIHNVR YCPAVEQPLW I