ID   DEF2_SINAL              Reviewed;          99 AA.
AC   P26780;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Defensin-like protein 2;
DE   AltName: Full=MTI-2;
DE   AltName: Full=Trypsin inhibitor 2;
DE   Flags: Precursor;
OS   Sinapis alba (White mustard) (Brassica hirta).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Sinapis.
OX   NCBI_TaxID=3728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Albatros; TISSUE=Seed;
RX   PubMed=7750566; DOI=10.1016/0014-5793(95)00386-n;
RA   Ceci L.R., Spoto N., de Virgilio M., Gallerani R.;
RT   "The gene coding for the mustard trypsin inhibitor-2 is discontinuous and
RT   wound-inducible.";
RL   FEBS Lett. 364:179-181(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 31-93.
RC   STRAIN=cv. Albatros; TISSUE=Seed;
RX   PubMed=1451776; DOI=10.1016/0014-5793(92)80199-q;
RA   Menegatti E., Tedeschi G., Ronchi S., Bortolotti F., Ascenzi P.,
RA   Thomas R.M., Bolognesi M., Palmieri S.;
RT   "Purification, inhibitory properties and amino acid sequence of a new
RT   serine proteinase inhibitor from white mustard (Sinapis alba L.) seed.";
RL   FEBS Lett. 301:10-14(1992).
CC   -!- FUNCTION: Inhibits bovine beta-trypsin and alpha-chymotrypsin on a 1:1
CC       molar basis.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the DEFL family. Protease inhibitor I18
CC       (RTI/MTI-2) subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was initially thought (PubMed:7750566 and PubMed:1451776) to
CC       be a protease inhibitor. {ECO:0000305}.
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DR   EMBL; X84208; CAA58994.1; -; Genomic_DNA.
DR   PIR; S65661; S65661.
DR   AlphaFoldDB; P26780; -.
DR   SMR; P26780; -.
DR   MEROPS; I18.001; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   InterPro; IPR002061; Scorpion_toxinL/defensin.
DR   Pfam; PF00537; Toxin_3; 1.
DR   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW   Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000269|PubMed:1451776"
FT   CHAIN           31..93
FT                   /note="Defensin-like protein 2"
FT                   /id="PRO_0000031097"
FT   PROPEP          94..99
FT                   /id="PRO_0000031098"
FT   SITE            50..51
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..86
FT                   /evidence="ECO:0000250"
FT   DISULFID        47..71
FT                   /evidence="ECO:0000250"
FT   DISULFID        56..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..83
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   99 AA;  10982 MW;  5E96C788968EEA9F CRC64;
     MAMAKKSVSS FTLIFILVLV IFEVPEIKAQ DSECLKEYGG DVGFPFCAPR IFPTICYTRC
     RENKGAKGGR CIWGEGTNVK CLCDYCNDSP FDQILRGGI