ID   ITR1_BETVV              Reviewed;          33 AA.
AC   C0HLV1;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   02-JUN-2021, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Trypsin inhibitor 1 {ECO:0000305|PubMed:33118348};
DE   AltName: Full=BevuTI-I {ECO:0000303|PubMed:33118348};
DE   AltName: Full=Trypsin inhibitor I {ECO:0000303|PubMed:33118348};
OS   Beta vulgaris subsp. vulgaris (Beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=3555 {ECO:0000303|PubMed:33118348};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SYNTHESIS, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Fruit flesh {ECO:0000303|PubMed:33118348};
RX   PubMed=33118348; DOI=10.1021/acs.jnatprod.0c00648;
RA   Retzl B., Hellinger R., Muratspahic E., Pinto M.E.F., Bolzani V.S.,
RA   Gruber C.W.;
RT   "Discovery of a Beetroot Protease Inhibitor to Identify and Classify Plant-
RT   Derived Cystine Knot Peptides.";
RL   J. Nat. Prod. 83:3305-3314(2020).
CC   -!- FUNCTION: Inhibits trypsin (IC(50)=471 nM).
CC       {ECO:0000269|PubMed:33118348}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves and fruit flesh (at protein
CC       level). {ECO:0000269|PubMed:33118348}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin.
CC       {ECO:0000305|PubMed:33118348}.
CC   -!- MASS SPECTROMETRY: Mass=3560; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:33118348};
CC   -!- SIMILARITY: Belongs to the Mirabilis serine proteinase inhibitor
CC       family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HLV1; -.
DR   SMR; C0HLV1; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
DR   InterPro; IPR040875; Tryp_inh.
DR   Pfam; PF17983; Tryp_inh; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Protease inhibitor;
KW   Serine protease inhibitor.
FT   PEPTIDE         1..33
FT                   /note="Trypsin inhibitor 1"
FT                   /id="PRO_0000452750"
FT   SITE            28..29
FT                   /note="Reactive bond for trypsin"
FT                   /evidence="ECO:0000250|UniProtKB:P84779"
FT   DISULFID        1..17
FT                   /evidence="ECO:0000269|PubMed:33118348"
FT   DISULFID        8..21
FT                   /evidence="ECO:0000269|PubMed:33118348"
FT   DISULFID        16..32
FT                   /evidence="ECO:0000269|PubMed:33118348"
FT   UNSURE          7
FT                   /note="I or L"
FT                   /evidence="ECO:0000269|PubMed:33118348"
FT   UNSURE          29
FT                   /note="I or L"
FT                   /evidence="ECO:0000269|PubMed:33118348"
SQ   SEQUENCE   33 AA;  3568 MW;  62F19DADB217A4C5 CRC64;
     CTPSGTICSP EAPEQCCSNS CVPHQWLRIF VCA