ID   IAAT_MAIZE              Reviewed;         206 AA.
AC   P13867;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Alpha-amylase/trypsin inhibitor;
DE   AltName: Full=Antifungal protein;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Richardson M., Valdes-Rodriguez S., Blanco-Labra A.;
RT   "A possible function for thaumatin and a TMV-induced protein suggested by
RT   homology to a maize inhibitor.";
RL   Nature 327:432-434(1987).
RN   [2]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=1731773; DOI=10.1016/s0006-291x(05)80103-2;
RA   Huynh Q.K., Borgmeyer J.R., Zobel J.F.;
RT   "Isolation and characterization of a 22 kDa protein with antifungal
RT   properties from maize seeds.";
RL   Biochem. Biophys. Res. Commun. 182:1-5(1992).
CC   -!- FUNCTION: Inhibits both trypsin and alpha-amylase. Inhibits the growth
CC       of some plant fungal pathogens.
CC   -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00699}.
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DR   PIR; A29581; A29581.
DR   AlphaFoldDB; P13867; -.
DR   SMR; P13867; -.
DR   PRIDE; P13867; -.
DR   MaizeGDB; 69169; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P13867; baseline and differential.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.110.10; -; 1.
DR   InterPro; IPR037176; Osmotin/thaumatin-like_sf.
DR   InterPro; IPR001938; Thaumatin.
DR   InterPro; IPR017949; Thaumatin_CS.
DR   PANTHER; PTHR31048; PTHR31048; 1.
DR   Pfam; PF00314; Thaumatin; 1.
DR   PIRSF; PIRSF002703; Thaumatin; 1.
DR   PRINTS; PR00347; THAUMATIN.
DR   SMART; SM00205; THN; 1.
DR   SUPFAM; SSF49870; SSF49870; 1.
DR   PROSITE; PS00316; THAUMATIN_1; 1.
DR   PROSITE; PS51367; THAUMATIN_2; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW   Plant defense; Protease inhibitor; Reference proteome;
KW   Serine protease inhibitor.
FT   CHAIN           1..206
FT                   /note="Alpha-amylase/trypsin inhibitor"
FT                   /id="PRO_0000096234"
FT   DISULFID        9..205
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        51..61
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        66..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        118..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        124..177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        132..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        146..155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        156..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   CONFLICT        108
FT                   /note="Y -> M (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   206 AA;  22075 MW;  6C73E1BACAE090DE CRC64;
     AVFTVVNQCP FTVWAASVPV GGGRQLNRGE SWRITAPAGT TAARIWARTG CQFDASGRGS
     CRTGDCGGVV QCTGYGRAPN TLAEYALKQF NNLDFFDISI LDGFNVPYSF LPDGGSGCSR
     GPRCAVDVNA RCPAELRQDG VCNNACPVFK KDEYCCVGSA ANNCHPTNYS RYFKGQCPDA
     YSYPKDDATS TFTCPAGTNY KVVFCP