ID   DEF2_VIGUN              Reviewed;          46 AA.
AC   P84920;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Defensin-like protein 2;
DE   AltName: Full=Cp-thionin II;
DE   AltName: Full=Cp-thionin-2;
DE   AltName: Full=Gamma-thionin II;
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, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND MASS SPECTROMETRY.
RC   STRAIN=cv. Epace-10 {ECO:0000269|PubMed:16824043};
RC   TISSUE=Seed {ECO:0000269|PubMed:16824043};
RX   PubMed=16824043; DOI=10.1111/j.1742-4658.2006.05349.x;
RA   Franco O.L., Murad A.M., Leite J.R., Mendes P.A.M., Prates M.V.,
RA   Bloch C. Jr.;
RT   "Identification of a cowpea gamma-thionin with bactericidal activity.";
RL   FEBS J. 273:3489-3497(2006).
CC   -!- FUNCTION: Has antibacterial activity against the Gram-positive
CC       bacterium S.aureus and the Gram-negative bacteria E.coli and
CC       P.syringae. Does not have antibacterial activity against the
CC       phytopathogenic bacteria R.solanacearum, Rhataybacter sp and Erwinia
CC       sp. Does not inhibit trypsin, chymotrypsin or alpha-amylases.
CC       {ECO:0000269|PubMed:16824043}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16824043}.
CC   -!- TISSUE SPECIFICITY: Present in seeds, cotyledons and leaves. Not found
CC       in roots or stems. {ECO:0000269|PubMed:16824043}.
CC   -!- DEVELOPMENTAL STAGE: Present in seeds and seedlings, levels decrease
CC       with seedling age. Light increases the rate of degradation. Present
CC       until 9 days in seedlings kept in the dark, not found after 6 days in
CC       seedlings kept in the light. {ECO:0000269|PubMed:16824043}.
CC   -!- MASS SPECTROMETRY: Mass=5235.04; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16824043};
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:16824043}.
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DR   AlphaFoldDB; P84920; -.
DR   SMR; P84920; -.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Plant defense.
FT   CHAIN           1..46
FT                   /note="Defensin-like protein 2"
FT                   /id="PRO_0000248510"
FT   DISULFID        3..46
FT                   /evidence="ECO:0000250|UniProtKB:P20158"
FT   DISULFID        13..33
FT                   /evidence="ECO:0000250|UniProtKB:P20158"
FT   DISULFID        19..40
FT                   /evidence="ECO:0000250|UniProtKB:P20158"
FT   DISULFID        23..42
FT                   /evidence="ECO:0000250|UniProtKB:P20158"
SQ   SEQUENCE   46 AA;  5242 MW;  5FB07A2D1235954B CRC64;
     KTCMTKKEGW GRCLIDTTCA HSCRKYGYMG GKCQGITRRC YCLLNC