ID   ICIW2_WHEAT             Reviewed;         119 AA.
AC   P83207; P83208;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Chymotrypsin inhibitor WCI;
DE   AltName: Full=Chloroform/methanol-soluble protein WCI;
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] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND VARIANT DES-(THR1)-WCI
RP   THR-1 DEL.
RC   STRAIN=cv. San Pastore {ECO:0000303|PubMed:21617989};
RC   TISSUE=Endosperm {ECO:0000303|PubMed:21617989};
RX   PubMed=21617989; DOI=10.1007/s00425-011-1437-5;
RA   Di Maro A., Farisei F., Panichi D., Severino V., Bruni N., Ficca A.G.,
RA   Ferranti P., Capuzzi V., Tedeschi F., Poerio E.;
RT   "WCI, a novel wheat chymotrypsin inhibitor: purification, primary
RT   structure, inhibitory properties and heterologous expression.";
RL   Planta 234:723-735(2011).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. San Pastore; TISSUE=Immature kernel;
RA   Verghini R., Di Gennaro S., Poerio E.;
RT   "RT-PCR cloning of the wheat gene wci coding for a chymotrypsin inhibitor
RT   belonging to the cereal chloroform/methanol soluble proteins.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Inhibits bovine, insect and wheat chymotrypsins. Inhibits
CC       bovine chymotrypsin with Ki of 0.6 nM. Does not inhibit human or wheat
CC       alpha-amylases, bovine pancreatic trypsin, or trypsin-like activity
CC       isolated from wheat. {ECO:0000269|PubMed:21617989}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH range is 7.0-9.0. {ECO:0000269|PubMed:21617989};
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius.
CC         {ECO:0000269|PubMed:21617989};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01087}.
CC   -!- MASS SPECTROMETRY: Mass=12933.40; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:21617989};
CC   -!- SIMILARITY: Belongs to the protease inhibitor I6 (cereal trypsin/alpha-
CC       amylase inhibitor) family. {ECO:0000305}.
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DR   EMBL; AJ422078; CAD19440.1; -; mRNA.
DR   AlphaFoldDB; P83207; -.
DR   SMR; P83207; -.
DR   MEROPS; I06.004; -.
DR   PRIDE; P83207; -.
DR   EnsemblPlants; TraesCAD_scaffold_112379_01G000100.1; TraesCAD_scaffold_112379_01G000100.1; TraesCAD_scaffold_112379_01G000100.
DR   EnsemblPlants; TraesCLE_scaffold_111143_01G000200.1; TraesCLE_scaffold_111143_01G000200.1; TraesCLE_scaffold_111143_01G000200.
DR   EnsemblPlants; TraesPAR_scaffold_110449_01G000100.1; TraesPAR_scaffold_110449_01G000100.1; TraesPAR_scaffold_110449_01G000100.
DR   EnsemblPlants; TraesROB_scaffold_097431_01G000100.1; TraesROB_scaffold_097431_01G000100.1; TraesROB_scaffold_097431_01G000100.
DR   EnsemblPlants; TraesWEE_scaffold_135394_01G000100.1; TraesWEE_scaffold_135394_01G000100.1; TraesWEE_scaffold_135394_01G000100.
DR   Gramene; TraesCAD_scaffold_112379_01G000100.1; TraesCAD_scaffold_112379_01G000100.1; TraesCAD_scaffold_112379_01G000100.
DR   Gramene; TraesCLE_scaffold_111143_01G000200.1; TraesCLE_scaffold_111143_01G000200.1; TraesCLE_scaffold_111143_01G000200.
DR   Gramene; TraesPAR_scaffold_110449_01G000100.1; TraesPAR_scaffold_110449_01G000100.1; TraesPAR_scaffold_110449_01G000100.
DR   Gramene; TraesROB_scaffold_097431_01G000100.1; TraesROB_scaffold_097431_01G000100.1; TraesROB_scaffold_097431_01G000100.
DR   Gramene; TraesWEE_scaffold_135394_01G000100.1; TraesWEE_scaffold_135394_01G000100.1; TraesWEE_scaffold_135394_01G000100.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P83207; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
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   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor.
FT   CHAIN           1..119
FT                   /note="Chymotrypsin inhibitor WCI"
FT                   /id="PRO_0000271234"
FT   DISULFID        6..55
FT                   /evidence="ECO:0000250|UniProtKB:P01087"
FT   DISULFID        20..44
FT                   /evidence="ECO:0000250|UniProtKB:P01087"
FT   DISULFID        29..87
FT                   /evidence="ECO:0000250|UniProtKB:P01087"
FT   DISULFID        45..105
FT                   /evidence="ECO:0000250|UniProtKB:P01087"
FT   DISULFID        57..116
FT                   /evidence="ECO:0000250|UniProtKB:P01087"
FT   VARIANT         1
FT                   /note="Missing (in des-(Thr1)-WCI form)"
FT                   /evidence="ECO:0000269|PubMed:21617989"
SQ   SEQUENCE   119 AA;  12944 MW;  258331C8FDCF316B CRC64;
     TSIYTCYEGV GLPVDPLQGC HYYVTSQTCG FVPLLPIEVM KDRCCRELAA ISSNCRCEGL
     RVFIDRAFPP SQSQGGGPPQ PPLAPRCPTE VKRDFARTLA LPGQCNLPTI HGGPYCVFP