ID   DEF1_ARAHY              Reviewed;          71 AA.
AC   B3EWP3;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2016, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Defensin 1 {ECO:0000303|PubMed:26037551};
DE   AltName: Allergen=Ara h 12 {ECO:0000305|PubMed:26037551};
DE   Flags: Precursor; Fragment;
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yin H., Cai N.B., Huang X.W., Luo B.M., Li W.X., Zhuang W.J.;
RT   "Isolation of peanut seed-specific genes by analysis of expressed
RT   sequence.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 26-71, PROBABLE FUNCTION, PROBABLE DIMERIZATION, LACK
RP   OF GLYCOSYLATION, PRESENCE OF DISULFIDE BONDS, MASS SPECTROMETRY, ALLERGEN,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=26037551; DOI=10.1016/j.jaci.2015.04.010;
RA   Petersen A., Kull S., Rennert S., Becker W.M., Krause S., Ernst M.,
RA   Gutsmann T., Bauer J., Lindner B., Jappe U.;
RT   "Peanut defensins: Novel allergens isolated from lipophilic peanut
RT   extract.";
RL   J. Allergy Clin. Immunol. 136:1295-1301(2015).
CC   -!- FUNCTION: Probably has antifungal activity.
CC       {ECO:0000269|PubMed:26037551}.
CC   -!- SUBUNIT: May form dimers. {ECO:0000269|PubMed:26037551}.
CC   -!- PTM: Not glycosylated. {ECO:0000269|PubMed:26037551}.
CC   -!- PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:26037551}.
CC   -!- PTM: Met-61 and Met-63 might be oxidized in some molecules.
CC       {ECO:0000269|PubMed:26037551}.
CC   -!- MASS SPECTROMETRY: Mass=5184.1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:26037551};
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:26037551}.
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR   EMBL; EY396089; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3EWP3; -.
DR   SMR; B3EWP3; -.
DR   Allergome; 10187; Ara h 12.
DR   Allergome; 10188; Ara h 12.0101.
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.
PE   1: Evidence at protein level;
KW   Allergen; Antimicrobial; Defensin; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Oxidation; Plant defense; Signal.
FT   SIGNAL          <1..25
FT                   /evidence="ECO:0000269|PubMed:26037551"
FT   CHAIN           26..71
FT                   /note="Defensin 1"
FT                   /evidence="ECO:0000269|PubMed:26037551"
FT                   /id="PRO_0000435958"
FT   DISULFID        28..71
FT                   /evidence="ECO:0000250|UniProtKB:P81929"
FT   DISULFID        39..60
FT                   /evidence="ECO:0000250|UniProtKB:P81929"
FT   DISULFID        45..65
FT                   /evidence="ECO:0000250|UniProtKB:P81929"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   71 AA;  7909 MW;  3DD1F7F12E930E22 CRC64;
     KTVAGFCIFF LVLFLAQEGV VKTEAKLCNH LADTYRGPCF TNASCDDHCK NKEHFVSGTC
     MKMACWCAHN C