ID   ICID_SOLTU              Reviewed;         107 AA.
AC   P08454;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Wound-induced proteinase inhibitor 1;
DE   AltName: Full=Chymotrypsin inhibitor I, D subunit;
DE   AltName: Full=Wound-induced proteinase inhibitor I;
DE   Flags: Precursor;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Cleveland T.E., Thornburg R.W., Ryan C.A.;
RT   "Molecular characterization of a wound-inducible inhibitor I gene from
RT   potato and the processing of its mRNA and protein.";
RL   Plant Mol. Biol. 8:199-207(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 37-107 (SUBUNITS B; C AND D).
RC   STRAIN=cv. Ulster Prince;
RX   PubMed=4606338; DOI=10.1016/0014-5793(74)80798-2;
RA   Richardson M., Cossins L.;
RT   "Chymotryptic inhibitor I from potatoes: the amino acid sequences of
RT   subunits B, C, and D.";
RL   FEBS Lett. 45:11-13(1974).
RN   [3]
RP   ERRATUM OF PUBMED:4606338, AND SEQUENCE REVISION.
RA   Richardson M., Cossins L.;
RL   FEBS Lett. 52:161-161(1975).
CC   -!- FUNCTION: Inhibits both chymotrypsin and trypsin.
CC   -!- SUBUNIT: Heterogeneous tetramers of similar chains.
CC   -!- MISCELLANEOUS: Mechanical damage (i.e. insect chewing) to this plant
CC       results in the systemic release of a factor from the wound site. Within
CC       the leaves it induces the cytoplasmic synthesis of proteinase
CC       inhibitors I and II.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine
CC       protease inhibitor) family. {ECO:0000305}.
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DR   EMBL; M17108; AAA33816.1; -; Genomic_DNA.
DR   PIR; S06251; S06251.
DR   AlphaFoldDB; P08454; -.
DR   SMR; P08454; -.
DR   MEROPS; I13.006; -.
DR   PRIDE; P08454; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P08454; baseline and differential.
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   Serine protease inhibitor; Signal.
FT   SIGNAL          1..23
FT   PROPEP          24..36
FT                   /evidence="ECO:0000269|PubMed:4606338"
FT                   /id="PRO_0000025292"
FT   CHAIN           37..107
FT                   /note="Wound-induced proteinase inhibitor 1"
FT                   /id="PRO_0000025293"
FT   SITE            83..84
FT                   /note="Reactive bond"
FT   CONFLICT        45..46
FT                   /note="QR -> LQ (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="E -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="C -> S (in Ref. 1; AAA33816)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   107 AA;  12145 MW;  3964CF60D81D2349 CRC64;
     MESKFAHIIV FFLLATSFET LLARKESDGP EVIELQKEFE CNGKQRWPEL IGVPTKLAKG
     IIEKENSLIT NVQILLNGSP VTMDYRCNRV RLFDNILGDV VQIPRVA