ID   ITR1_MOMCH              Reviewed;          30 AA.
AC   P10294;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Trypsin inhibitor 1;
DE   AltName: Full=MCTI-I;
DE   AltName: Full=Trypsin inhibitor I;
OS   Momordica charantia (Bitter gourd) (Balsam pear).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Momordiceae; Momordica.
OX   NCBI_TaxID=3673;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=2738047; DOI=10.1093/oxfordjournals.jbchem.a122625;
RA   Hara S., Makino J., Ikenaka T.;
RT   "Amino acid sequences and disulfide bridges of serine proteinase inhibitors
RT   from bitter gourd (Momordica charantia LINN.) seeds.";
RL   J. Biochem. 105:88-92(1989).
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   PIR; JX0057; JX0057.
DR   AlphaFoldDB; P10294; -.
DR   SMR; P10294; -.
DR   MEROPS; I07.001; -.
DR   Proteomes; UP000504603; Unplaced.
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   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   Reference proteome; Secreted; Serine protease inhibitor.
FT   PEPTIDE         1..30
FT                   /note="Trypsin inhibitor 1"
FT                   /id="PRO_0000044386"
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;  3413 MW;  D5E1344365E34E9A CRC64;
     ERRCPRILKQ CKRDSDCPGE CICMAHGFCG