ID   ICIW_WHEAT              Reviewed;          84 AA.
AC   P82977; Q4TZQ0; Q546I0;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Subtilisin-chymotrypsin inhibitor WSCI;
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].
RA   Grassau B., Frenzel K., Baur X., Yu F.;
RT   "Bacterial expression of the WSCI gene and characterization of the
RT   recombinant product.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 13-84, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, MASS SPECTROMETRY, AND REACTIVE SITE.
RC   STRAIN=cv. San Pastore; TISSUE=Endosperm;
RX   PubMed=12675523; DOI=10.1515/bc.2003.033;
RA   Poerio E., Di Gennaro S., Di Maro A., Farisei F., Ferranti P., Parente A.;
RT   "Primary structure and reactive site of a novel wheat proteinase inhibitor
RT   of subtilisin and chymotrypsin.";
RL   Biol. Chem. 384:295-304(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-84, AND FUNCTION.
RC   STRAIN=cv. San Pastore; TISSUE=Immature kernel;
RX   PubMed=15899701; DOI=10.1515/bc.2005.046;
RA   Di Gennaro S., Ficca A., Panichi D., Poerio E.;
RT   "cDNA cloning and heterologous expression of a wheat proteinase inhibitor
RT   of subtilisin and chymotrypsin (WSCI) that interferes with digestive
RT   enzymes of insect pests.";
RL   Biol. Chem. 386:383-389(2005).
CC   -!- FUNCTION: Inhibits B.lichenoformis subtilisin, B.subtilis subtilisin,
CC       bovine pancreatic alpha-chymotrypsin and porcine alpha-chymotrypsin
CC       with Ki of 3.92 nM, 5.70 nM, 7.24 nM and 9.35 nM respectively.
CC       B.lichenoformis subtilisin is inhibited with a molar ratio of 1:0.87.
CC       Also inhibits chymotrypsin-like activities from the digestive tracts of
CC       the insect larvae T.molitor, P.interpunctella and H.armigera. Does not
CC       inhibit bovine pancreatic trypsin, porcine pancreatic elastase, or
CC       human leukocyte elastase. {ECO:0000269|PubMed:12675523,
CC       ECO:0000269|PubMed:15899701}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 25 degrees Celsius when incubation is carried
CC         out at pH 7.0-9.0. {ECO:0000269|PubMed:12675523};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12675523}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=8126.3; Mass_error=0.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:12675523};
CC   -!- SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine
CC       protease inhibitor) family. {ECO:0000305}.
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DR   EMBL; DQ025758; AAY45744.1; -; mRNA.
DR   EMBL; AJ422055; CAD19324.1; -; mRNA.
DR   AlphaFoldDB; P82977; -.
DR   SMR; P82977; -.
DR   Allergome; 10784; Tri a 39.0101.
DR   Allergome; 4075; Tri a 39.
DR   MEROPS; I13.012; -.
DR   PRIDE; P82977; -.
DR   eggNOG; ENOG502R3R2; Eukaryota.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; P82977; baseline.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009611; P:response to wounding; IEA:InterPro.
DR   InterPro; IPR000864; Prot_inh_pot1.
DR   InterPro; IPR036354; Prot_inh_pot1_sf.
DR   PANTHER; PTHR33091; PTHR33091; 1.
DR   Pfam; PF00280; potato_inhibit; 1.
DR   PRINTS; PR00292; POTATOINHBTR.
DR   SUPFAM; SSF54654; SSF54654; 1.
DR   PROSITE; PS00285; POTATO_INHIBITOR; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..12
FT                   /evidence="ECO:0000269|PubMed:12675523"
FT   CHAIN           13..84
FT                   /note="Subtilisin-chymotrypsin inhibitor WSCI"
FT                   /id="PRO_0000217651"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            60..61
FT                   /note="Reactive bond"
FT   CONFLICT        51
FT                   /note="V -> I (in Ref. 1; AAY45744)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="R -> C (in Ref. 1; AAY45744)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   84 AA;  9326 MW;  E59B2374D25375C8 CRC64;
     MSSVVKKPLG GNTDTGDHHN QKTEWPELVG KSVEEAKKVI LQDKSEAQIV VLPVGTIVTM
     EYRIDRVRLF VDSLDKIAQV PRVG