ID   ITR4_CUCSA              Reviewed;          30 AA.
AC   P10292;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Trypsin inhibitor 4;
DE   AltName: Full=CSTI-IV;
DE   AltName: Full=Trypsin inhibitor IV;
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=3977882; DOI=10.1016/0006-291x(85)90233-5;
RA   Wieczorek M., Otlewski J., Cook J., Parks K., Leluk J., Wilimowska-Pelc A.,
RA   Polanowski A., Wilusz T., Laskowski M. Jr.;
RT   "The squash family of serine proteinase inhibitors. Amino acid sequences
RT   and association equilibrium constants of inhibitors from squash, summer
RT   squash, zucchini, and cucumber seeds.";
RL   Biochem. Biophys. Res. Commun. 126:646-652(1985).
CC   -!- FUNCTION: Inhibits trypsin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I7 (squash-type serine
CC       protease inhibitor) family. {ECO:0000305}.
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DR   AlphaFoldDB; P10292; -.
DR   SMR; P10292; -.
DR   MEROPS; I07.015; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00150; PlantTI; 1.
DR   InterPro; IPR000737; Prot_inh_squash.
DR   InterPro; IPR011052; Proteinase_amylase_inhib_sf.
DR   Pfam; PF00299; Squash; 1.
DR   PRINTS; PR00293; SQUASHINHBTR.
DR   SUPFAM; SSF57027; SSF57027; 1.
DR   PROSITE; PS00286; SQUASH_INHIBITOR; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Protease inhibitor;
KW   Secreted; Serine protease inhibitor.
FT   PEPTIDE         1..30
FT                   /note="Trypsin inhibitor 4"
FT                   /id="PRO_0000044377"
FT   SITE            5..6
FT                   /note="Reactive bond"
FT   DISULFID        3..20
FT                   /evidence="ECO:0000250"
FT   DISULFID        10..22
FT                   /evidence="ECO:0000250"
FT   DISULFID        16..29
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   30 AA;  3429 MW;  7A4B870E7D2A088F CRC64;
     MMCPRILMKC KHDSDCLPGC VCLEHIEYCG