ID   DEF2A_SINAL             Reviewed;          51 AA.
AC   P30232;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Defensin-like protein 2A;
DE   AltName: Full=Cysteine-rich antifungal protein 2A;
DE            Short=AFP2A;
DE   AltName: Full=M2A;
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   PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-8, AND MASS SPECTROMETRY.
RC   TISSUE=Seed;
RX   PubMed=8836771; DOI=10.1111/j.1399-3011.1996.tb01094.x;
RA   Neumann G.M., Condron R., Polya G.M.;
RT   "Purification and mass spectrometry-based sequencing of yellow mustard
RT   (Sinapis alba L.) 6 kDa proteins. Identification as antifungal proteins.";
RL   Int. J. Pept. Protein Res. 47:437-446(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-26, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC   TISSUE=Seed;
RX   PubMed=8422949; DOI=10.1016/0014-5793(93)81299-f;
RA   Terras F.R.G., Torrekens S., van Leuven F., Osborn R.W., Vanderleyden J.,
RA   Cammue B.P.A., Broekaert W.F.;
RT   "A new family of basic cysteine-rich plant antifungal proteins from
RT   Brassicaceae species.";
RL   FEBS Lett. 316:233-240(1993).
CC   -!- FUNCTION: Possesses antifungal activity sensitive to inorganic cations.
CC   -!- SUBUNIT: Forms oligomers in its native state.
CC   -!- MASS SPECTROMETRY: Mass=5705; Mass_error=0.8; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8836771};
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; S28994; S28994.
DR   AlphaFoldDB; P30232; -.
DR   SMR; P30232; -.
DR   iPTMnet; P30232; -.
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; IPR008176; Defensin_plant.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
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   Phosphoprotein; Pyrrolidone carboxylic acid.
FT   CHAIN           1..51
FT                   /note="Defensin-like protein 2A"
FT                   /id="PRO_0000074244"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:8422949"
FT   MOD_RES         8
FT                   /note="Phosphoserine; by CPK"
FT                   /evidence="ECO:0000269|PubMed:8836771"
FT   DISULFID        4..51
FT                   /evidence="ECO:0000250"
FT   DISULFID        15..36
FT                   /evidence="ECO:0000250"
FT   DISULFID        21..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..47
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   51 AA;  5722 MW;  1C7F50E72DC945B1 CRC64;
     QKLCQRPSGT WSGVCGNNNA CRNQCINLEK ARHGSCNYVF PAHKCICYFP C