ID   DEF1_VIGUN              Reviewed;          47 AA.
AC   P83399;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Defensin-like protein 1;
DE   AltName: Full=Cp-thionin I;
DE   AltName: Full=Cp-thionin-1;
DE   AltName: Full=Gamma-thionin I;
OS   Vigna unguiculata (Cowpea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3917;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND 3D-STRUCTURE
RP   MODELING.
RC   STRAIN=cv. Epace-10 {ECO:0000269|PubMed:12112698};
RC   TISSUE=Cotyledon {ECO:0000269|PubMed:12112698};
RX   PubMed=12112698; DOI=10.1002/prot.10142;
RA   Melo F.R., Rigden D.J., Franco O.L., Mello L.V., Ary M.B.,
RA   Grossi de Sa M.F., Bloch C. Jr.;
RT   "Inhibition of trypsin by cowpea thionin: characterization, molecular
RT   modeling, and docking.";
RL   Proteins 48:311-319(2002).
CC   -!- FUNCTION: Inhibits trypsin but not chymotrypsin.
CC       {ECO:0000269|PubMed:12112698}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:12112698}.
CC   -!- MASS SPECTROMETRY: Mass=5229.03; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12112698};
CC   -!- SIMILARITY: Belongs to the DEFL family. Protease inhibitor I18
CC       (RTI/MTI-2) subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was initially thought to be a thionin.
CC       {ECO:0000305|PubMed:12112698}.
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DR   AlphaFoldDB; P83399; -.
DR   SMR; P83399; -.
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   CDD; cd00107; Knot1; 1.
DR   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR008176; Defensin_plant.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   PRINTS; PR00288; PUROTHIONIN.
DR   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
DR   PROSITE; PS00940; GAMMA_THIONIN; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW   Plant defense.
FT   CHAIN           1..47
FT                   /note="Defensin-like protein 1"
FT                   /id="PRO_0000074260"
FT   SITE            11
FT                   /note="Interaction with trypsin"
FT                   /evidence="ECO:0000269|PubMed:12112698"
FT   DISULFID        3..47
FT                   /evidence="ECO:0000250|UniProtKB:P21925"
FT   DISULFID        14..34
FT                   /evidence="ECO:0000250|UniProtKB:P21925"
FT   DISULFID        20..41
FT                   /evidence="ECO:0000250|UniProtKB:P21925"
FT   DISULFID        24..43
FT                   /evidence="ECO:0000250|UniProtKB:P21925"
SQ   SEQUENCE   47 AA;  5173 MW;  AEDCC05B89660D82 CRC64;
     RVCESQSHGF KGACTGDHNC ALVCRNEGFS GGNCRGFRRR CFCTLKC