ID   ITI1_LAGSI              Reviewed;          30 AA.
AC   P26771;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Trypsin inhibitor 1;
DE   AltName: Full=LLDTI-I;
DE            Short=LLTI-I;
DE   AltName: Full=Trypsin inhibitor I;
DE   Contains:
DE     RecName: Full=Trypsin inhibitor 2;
DE     AltName: Full=LLDTI-II;
DE              Short=LLTI-II;
DE     AltName: Full=Trypsin inhibitor II;
OS   Lagenaria siceraria (Bottle gourd) (Lagenaria leucantha).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Lagenaria.
OX   NCBI_TaxID=3668;
RN   [1]
RP   PROTEIN SEQUENCE (LLDTI-I AND LLDTI-II), AND PYROGLUTAMATE FORMATION AT
RP   GLN-1.
RC   STRAIN=cv. Depressa Makino; TISSUE=Seed;
RX   PubMed=1562585; DOI=10.1016/0167-4838(92)90268-i;
RA   Matsuo M., Hamato N., Takano R., Kamei-Hayashi K., Yasuda-Kamatani Y.,
RA   Nomoto K., Hara S.;
RT   "Trypsin inhibitors from bottle gourd (Lagenaria leucantha Rusby var.
RT   Depressa Makino) seeds. Purification and amino acid sequences.";
RL   Biochim. Biophys. Acta 1120:187-192(1992).
RN   [2]
RP   PROTEIN SEQUENCE (LLTI-III).
RC   STRAIN=cv. Gourda Makino; TISSUE=Seed;
RX   PubMed=1368303; DOI=10.1271/bbb.56.275;
RA   Hamato N., Takano R., Kamei-Hayashi K., Hara S.;
RT   "Purification and characterization of serine proteinase inhibitors form
RT   gourd (Lagenaria leucantha Rusby var. Gourda Makino) seeds.";
RL   Biosci. Biotechnol. Biochem. 56:275-279(1992).
CC   -!- FUNCTION: Strong inhibitors of 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   -!- PTM: LLTI-III seems to differ from LLDTI-I by the absence of
CC       cyclization of Gln-1.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I7 (squash-type serine
CC       protease inhibitor) family. {ECO:0000305}.
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DR   PIR; S21743; S21743.
DR   AlphaFoldDB; P26771; -.
DR   SMR; P26771; -.
DR   MEROPS; I07.009; -.
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   Pyrrolidone carboxylic acid; Secreted; Serine protease inhibitor.
FT   PEPTIDE         1..30
FT                   /note="Trypsin inhibitor 1"
FT                   /id="PRO_0000033214"
FT   PEPTIDE         2..30
FT                   /note="Trypsin inhibitor 2"
FT                   /id="PRO_0000033215"
FT   SITE            6..7
FT                   /note="Reactive bond"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:1562585"
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;  3455 MW;  3852E6F1FA42CE5F CRC64;
     QRRCPRIYME CKHDSDCLAD CVCLEHGICG