ID   ITR3_CUCMC              Reviewed;          30 AA.
AC   P32041; Q9S748;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Trypsin inhibitor 3;
DE   AltName: Full=CMCTI-III;
DE   AltName: Full=Trypsin inhibitor III;
DE   Contains:
DE     RecName: Full=Trypsin inhibitor 2;
DE     AltName: Full=CMCT-II;
DE     AltName: Full=CMeTI-A;
DE     AltName: Full=Trypsin inhibitor II;
DE   Contains:
DE     RecName: Full=Trypsin inhibitor 1;
DE     AltName: Full=CMCTI-I;
DE     AltName: Full=Trypsin inhibitor I;
OS   Cucumis melo var. conomon (Oriental pickling melon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3657;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=1368838; DOI=10.1271/bbb.56.1241;
RA   Nishino J., Takano R., Kamei-Hayashi K., Minakata H., Nomoto K., Hara S.;
RT   "Amino acid sequences of trypsin inhibitors from oriental pickling melon
RT   (Cucumis melo L. var. Conomon Makino) seeds.";
RL   Biosci. Biotechnol. Biochem. 56:1241-1246(1992).
RN   [2]
RP   PROTEIN SEQUENCE (CMCT-II).
RC   TISSUE=Seed;
RX   PubMed=8537309; DOI=10.1093/oxfordjournals.jbchem.a124875;
RA   Lee C.F., Lin J.Y.;
RT   "Amino acid sequences of trypsin inhibitors from the melon Cucumis melo.";
RL   J. Biochem. 118:18-22(1995).
CC   -!- FUNCTION: Inhibits lysyl endopeptidase and 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   PIR; PC1113; PC1113.
DR   AlphaFoldDB; P32041; -.
DR   SMR; P32041; -.
DR   MEROPS; I07.013; -.
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 3"
FT                   /id="PRO_0000033201"
FT   PEPTIDE         2..30
FT                   /note="Trypsin inhibitor 2"
FT                   /id="PRO_0000033202"
FT   PEPTIDE         3..30
FT                   /note="Trypsin inhibitor 1"
FT                   /id="PRO_0000033203"
FT   SITE            6..7
FT                   /note="Reactive bond"
FT   DISULFID        4..21
FT                   /evidence="ECO:0000250"
FT   DISULFID        11..23
FT                   /evidence="ECO:0000250"
FT   DISULFID        17..29
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   30 AA;  3409 MW;  D5D1D1817255555E CRC64;
     QRMCPKILMK CKQDSDCLLD CVCLKEGFCG