IAC16_WHEAT
ID IAC16_WHEAT Reviewed; 143 AA.
AC P16159;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Alpha-amylase/trypsin inhibitor CM16;
DE AltName: Full=Chloroform/methanol-soluble protein CM16;
DE Flags: Precursor;
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. Agathe; TISSUE=Seed;
RX PubMed=2102817; DOI=10.1007/bf00028768;
RA Gautier M.-F., Alary R., Joudrier P.;
RT "Cloning and characterization of a cDNA encoding the wheat (Triticum durum
RT Desf.) CM16 protein.";
RL Plant Mol. Biol. 14:313-322(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Chinese Spring; TISSUE=Endosperm;
RX PubMed=2102861; DOI=10.1007/bf00016517;
RA Garcia-Maroto F., Marana C., Mena M., Garcia-Olmedo F., Carbonero P.;
RT "Cloning of cDNA and chromosomal location of genes encoding the three types
RT of subunits of the wheat tetrameric inhibitor of insect alpha-amylase.";
RL Plant Mol. Biol. 14:845-853(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Timgalen; TISSUE=Seed;
RX PubMed=1893108; DOI=10.1007/bf00020573;
RA Lullien V., Alary R., Joudrier P., Gautier M.-F.;
RT "Characterization of a cDNA clone encoding the Triticum aestivum L. CM16
RT protein: homology with the Triticum durum Desf. sequence.";
RL Plant Mol. Biol. 16:373-374(1991).
RN [4]
RP PROTEIN SEQUENCE OF 25-53.
RA Barber D., Sanchez-Monge R., Garcia-Olmedo F., Salcedo G., Mendez E.;
RT "Evolutionary implications of sequential homologies among members of the
RT trypsin / alpha-amylase inhibitor family (CM-proteins) in wheat and
RT barley.";
RL Biochim. Biophys. Acta 873:147-151(1986).
CC -!- FUNCTION: Alpha-amylase/trypsin inhibitor. It could be involved in
CC insect defense mechanisms.
CC -!- SUBUNIT: Subunit of the tetrameric inhibitor.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Developing endosperm.
CC -!- PTM: Five disulfide bonds are present (Probable), which are essential
CC for the inhibitor activity.
CC -!- MISCELLANEOUS: CM proteins would be involved in the cooking quality of
CC pasta.
CC -!- SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha-
CC amylase inhibitor) family. {ECO:0000305}.
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DR EMBL; X16733; CAA34709.1; -; mRNA.
DR EMBL; X17573; CAA35596.1; -; mRNA.
DR EMBL; X55455; CAA39100.1; -; mRNA.
DR PIR; C25310; C25310.
DR PIR; S13384; S13384.
DR AlphaFoldDB; P16159; -.
DR SMR; P16159; -.
DR Allergome; 8777; Tri a 40.
DR MEROPS; I06.004; -.
DR PRIDE; P16159; -.
DR EnsemblPlants; TraesCAD_scaffold_059374_01G000100.1; TraesCAD_scaffold_059374_01G000100.1; TraesCAD_scaffold_059374_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_030329_01G000200.1; TraesCLE_scaffold_030329_01G000200.1; TraesCLE_scaffold_030329_01G000200.
DR EnsemblPlants; TraesCS4B02G328000.1; TraesCS4B02G328000.1.cds1; TraesCS4B02G328000.
DR EnsemblPlants; TraesPAR_scaffold_030854_01G000400.1; TraesPAR_scaffold_030854_01G000400.1; TraesPAR_scaffold_030854_01G000400.
DR EnsemblPlants; TraesROB_scaffold_059406_01G000200.1; TraesROB_scaffold_059406_01G000200.1; TraesROB_scaffold_059406_01G000200.
DR EnsemblPlants; TraesWEE_scaffold_013736_01G000400.1; TraesWEE_scaffold_013736_01G000400.1; TraesWEE_scaffold_013736_01G000400.
DR Gramene; TraesCAD_scaffold_059374_01G000100.1; TraesCAD_scaffold_059374_01G000100.1; TraesCAD_scaffold_059374_01G000100.
DR Gramene; TraesCLE_scaffold_030329_01G000200.1; TraesCLE_scaffold_030329_01G000200.1; TraesCLE_scaffold_030329_01G000200.
DR Gramene; TraesCS4B02G328000.1; TraesCS4B02G328000.1.cds1; TraesCS4B02G328000.
DR Gramene; TraesPAR_scaffold_030854_01G000400.1; TraesPAR_scaffold_030854_01G000400.1; TraesPAR_scaffold_030854_01G000400.
DR Gramene; TraesROB_scaffold_059406_01G000200.1; TraesROB_scaffold_059406_01G000200.1; TraesROB_scaffold_059406_01G000200.
DR Gramene; TraesWEE_scaffold_013736_01G000400.1; TraesWEE_scaffold_013736_01G000400.1; TraesWEE_scaffold_013736_01G000400.
DR HOGENOM; CLU_113497_1_1_1; -.
DR OMA; CCGELAN; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P16159; baseline.
DR Genevisible; P16159; TA.
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; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 25..143
FT /note="Alpha-amylase/trypsin inhibitor CM16"
FT /id="PRO_0000014347"
SQ SEQUENCE 143 AA; 15782 MW; DEB33F376D85ECCA CRC64;
MASKSNCVLL LAAVLVSIFA AVAAIGNEDC TPWMSTLITP LPSCRDYVEQ QACRIETPGS
PYLAKQQCCG ELANIPQQCR CQALRYFMGP KSRPDQSGLM ELPGCPREVQ MDFVRILVTP
GYCNLTTVHN TPYCLAMEES QWS
