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IAAC3_WHEAT
ID   IAAC3_WHEAT             Reviewed;         168 AA.
AC   P17314;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Alpha-amylase/trypsin inhibitor CM3;
DE   AltName: Full=Chloroform/methanol-soluble protein CM3;
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. 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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Agathe; TISSUE=Seed;
RA   Gautier M.-F., Alary R., Lullien V., Joudrier P.;
RL   Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 26-60.
RC   STRAIN=cv. Turgidum; TISSUE=Endosperm;
RA   Shewry P.R., Lafiandra D., Salcedo G., Aragoncillo C., Garcia-Olmedo F.,
RA   Lew E.J.-L., Dietler M.D., Kasarda D.D.;
RT   "N-terminal amino acid sequence of chloroform/methanol-soluble proteins and
RT   albumins from endosperm of wheat, barley and related species.";
RL   FEBS Lett. 175:359-363(1984).
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; X17574; CAA35597.1; -; mRNA.
DR   EMBL; X61032; CAA43367.1; -; mRNA.
DR   PIR; S10029; S10029.
DR   AlphaFoldDB; P17314; -.
DR   SMR; P17314; -.
DR   Allergome; 1051; Tri a 30.
DR   Allergome; 8191; Tri a 30.0101.
DR   MEROPS; I06.004; -.
DR   PRIDE; P17314; -.
DR   EnsemblPlants; TraesCAD_scaffold_059374_01G000200.1; TraesCAD_scaffold_059374_01G000200.1; TraesCAD_scaffold_059374_01G000200.
DR   EnsemblPlants; TraesCLE_scaffold_030329_01G000100.1; TraesCLE_scaffold_030329_01G000100.1; TraesCLE_scaffold_030329_01G000100.
DR   EnsemblPlants; TraesCS4B02G328100.1; TraesCS4B02G328100.1.cds1; TraesCS4B02G328100.
DR   EnsemblPlants; TraesPAR_scaffold_030854_01G000500.1; TraesPAR_scaffold_030854_01G000500.1; TraesPAR_scaffold_030854_01G000500.
DR   EnsemblPlants; TraesROB_scaffold_059406_01G000100.1; TraesROB_scaffold_059406_01G000100.1; TraesROB_scaffold_059406_01G000100.
DR   EnsemblPlants; TraesWEE_scaffold_013736_01G000500.1; TraesWEE_scaffold_013736_01G000500.1; TraesWEE_scaffold_013736_01G000500.
DR   Gramene; TraesCAD_scaffold_059374_01G000200.1; TraesCAD_scaffold_059374_01G000200.1; TraesCAD_scaffold_059374_01G000200.
DR   Gramene; TraesCLE_scaffold_030329_01G000100.1; TraesCLE_scaffold_030329_01G000100.1; TraesCLE_scaffold_030329_01G000100.
DR   Gramene; TraesCS4B02G328100.1; TraesCS4B02G328100.1.cds1; TraesCS4B02G328100.
DR   Gramene; TraesPAR_scaffold_030854_01G000500.1; TraesPAR_scaffold_030854_01G000500.1; TraesPAR_scaffold_030854_01G000500.
DR   Gramene; TraesROB_scaffold_059406_01G000100.1; TraesROB_scaffold_059406_01G000100.1; TraesROB_scaffold_059406_01G000100.
DR   Gramene; TraesWEE_scaffold_013736_01G000500.1; TraesWEE_scaffold_013736_01G000500.1; TraesWEE_scaffold_013736_01G000500.
DR   HOGENOM; CLU_113497_1_1_1; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P17314; baseline and differential.
DR   Genevisible; P17314; 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..25
FT                   /evidence="ECO:0000269|Ref.3"
FT   CHAIN           26..168
FT                   /note="Alpha-amylase/trypsin inhibitor CM3"
FT                   /id="PRO_0000014346"
SQ   SEQUENCE   168 AA;  18221 MW;  A950FF272E90D23C CRC64;
     MACKSSCSLL LLAAVLLSVL AAASASGSCV PGVAFRTNLL PHCRDYVLQQ TCGTFTPGSK
     LPEWMTSASI YSPGKPYLAK LYCCQELAEI SQQCRCEALR YFIALPVPSQ PVDPRSGNVG
     ESGLIDLPGC PREMQWDFVR LLVAPGQCNL ATIHNVRYCP AVEQPLWI
 
 
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