ITR1_MIRJA
ID ITR1_MIRJA Reviewed; 37 AA.
AC P84778;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Trypsin inhibitor 1;
DE AltName: Full=MJTI I;
DE AltName: Full=Trypsin inhibitor I;
OS Mirabilis jalapa (Garden four-o'clock).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Nyctaginaceae; Mirabilis.
OX NCBI_TaxID=3538;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND DISULFIDE BONDS.
RC TISSUE=Seed {ECO:0000269|PubMed:17481678};
RX PubMed=17481678; DOI=10.1016/j.phytochem.2007.03.012;
RA Kowalska J., Pszczola K., Wilimowska-Pelc A., Lorenc-Kubis I., Zuziak E.,
RA Lugowski M., Legowska A., Kwiatkowska A., Sleszynska M., Lesner A.,
RA Walewska A., Zablotna E., Rolka K., Wilusz T.;
RT "Trypsin inhibitors from the garden four o'clock (Mirabilis jalapa) and
RT spinach (Spinacia oleracea) seeds: isolation, characterization and chemical
RT synthesis.";
RL Phytochemistry 68:1487-1496(2007).
CC -!- FUNCTION: Trypsin inhibitor. {ECO:0000269|PubMed:17481678}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC -!- MASS SPECTROMETRY: Mass=4060.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17481678};
CC -!- MASS SPECTROMETRY: Mass=4061.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17481678};
CC -!- SIMILARITY: Belongs to the Mirabilis serine proteinase inhibitor
CC family. {ECO:0000269|PubMed:17481678}.
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DR AlphaFoldDB; P84778; -.
DR SMR; P84778; -.
DR MEROPS; I90.001; -.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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..37
FT /note="Trypsin inhibitor 1"
FT /id="PRO_0000292936"
FT SITE 32..33
FT /note="Reactive bond for trypsin"
FT /evidence="ECO:0000250|UniProtKB:P84779"
FT DISULFID 5..21
FT /evidence="ECO:0000269|PubMed:17481678"
FT DISULFID 12..25
FT /evidence="ECO:0000269|PubMed:17481678"
FT DISULFID 20..36
FT /evidence="ECO:0000269|PubMed:17481678"
SQ SEQUENCE 37 AA; 4068 MW; AD627C0E7C12E6BB CRC64;
EDEECAKTDQ ICPPNAPNYC CSGSCVPHPR LRIFVCA