IAAB_HORVU
ID IAAB_HORVU Reviewed; 149 AA.
AC P32936;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Alpha-amylase/trypsin inhibitor CMb;
DE AltName: Full=Chloroform/methanol-soluble protein CMb;
DE Flags: Precursor;
GN Name=IAT2;
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 PROTEIN SEQUENCE OF 25-53.
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 [3]
RP PROTEIN SEQUENCE OF 25-33.
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 CMb 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 -!- PTM: Exists both in a glycosylated and in an unglycosylated form. The
CC glycosylated form is a potent allergen.
CC -!- ALLERGEN: Causes an allergic reaction in human. Involved in baker's
CC asthma.
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; X69938; CAA49556.1; -; mRNA.
DR PIR; S78524; S78524.
DR AlphaFoldDB; P32936; -.
DR SMR; P32936; -.
DR Allergome; 418; Hor v 15.
DR MEROPS; I06.004; -.
DR EnsemblPlants; HORVU.MOREX.r2.4HG0341180.1; HORVU.MOREX.r2.4HG0341180.1.CDS.1; HORVU.MOREX.r2.4HG0341180.
DR EnsemblPlants; HORVU.MOREX.r2.4HG0341180.1.mrna1; HORVU.MOREX.r2.4HG0341180.1.mrna1.cds1; HORVU.MOREX.r2.4HG0341180.1.
DR Gramene; HORVU.MOREX.r2.4HG0341180.1; HORVU.MOREX.r2.4HG0341180.1.CDS.1; HORVU.MOREX.r2.4HG0341180.
DR Gramene; HORVU.MOREX.r2.4HG0341180.1.mrna1; HORVU.MOREX.r2.4HG0341180.1.mrna1.cds1; HORVU.MOREX.r2.4HG0341180.1.
DR ExpressionAtlas; P32936; 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 Allergen; Alpha-amylase inhibitor; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Protease inhibitor; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:3484638,
FT ECO:0000269|PubMed:8125056"
FT CHAIN 25..149
FT /note="Alpha-amylase/trypsin inhibitor CMb"
FT /id="PRO_0000014351"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 30
FT /note="C -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="W -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 149 AA; 16526 MW; A33E42B146A42847 CRC64;
MASKSSCDLL LAAVLVSIFA AVAAVGSEDC TPWTATPITP LPSCRDYVEQ QACRIETPGP
PYLAKQQCCG ELANIPQQCR CQALRFFMGR KSRPDQSGLM ELPGCPREVQ MDFVRILVTP
GFCNLTTVHN TPYCLAMDEW QWNRQFCSS