ID   ITR5_LUFAE              Reviewed;          63 AA.
AC   P34950;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Trypsin inhibitor 5;
DE   AltName: Full=TGT-II;
DE   AltName: Full=Trypsin inhibitor II;
DE   Flags: Precursor;
OS   Luffa aegyptiaca (Sponge gourd) (Luffa cylindrica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Luffa.
OX   NCBI_TaxID=3670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8419358; DOI=10.1016/s0021-9258(18)54006-0;
RA   Ling M.-H., Qi H.-Y., Chi C.-W.;
RT   "Protein, cDNA, and genomic DNA sequences of the towel gourd trypsin
RT   inhibitor. A squash family inhibitor.";
RL   J. Biol. Chem. 268:810-814(1993).
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   EMBL; M98055; AAA33407.1; -; mRNA.
DR   PIR; A45041; A45041.
DR   AlphaFoldDB; P34950; -.
DR   SMR; P34950; -.
DR   MEROPS; I07.011; -.
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   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..34
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033208"
FT   PEPTIDE         35..63
FT                   /note="Trypsin inhibitor 5"
FT                   /id="PRO_0000033209"
FT   SITE            39..40
FT                   /note="Reactive bond"
FT   DISULFID        37..54
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..56
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..62
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   63 AA;  6691 MW;  88E656B70A287CF6 CRC64;
     MASVAESSGV VEVIELISDG GNDLPRKIMS GRHGGICPRI LMPCKTDDDC MLDCRCLSNG
     YCG