ID   DEF2_PEA                Reviewed;          47 AA.
AC   P81930;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Defensin-2;
DE   AltName: Full=Antifungal protein Psd2;
DE   AltName: Full=Defense-related peptide 2;
OS   Pisum sativum (Garden pea).
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; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=cv. Mikado; TISSUE=Epidermis, and Seed endosperm;
RX   PubMed=10860545; DOI=10.1006/abbi.2000.1824;
RA   Almeida M.S., Cabral K.M., Zingali R.B., Kurtenbach E.;
RT   "Characterization of two novel defense peptides from pea (Pisum sativum)
RT   seeds.";
RL   Arch. Biochem. Biophys. 378:278-286(2000).
RN   [2]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   PubMed=31294889; DOI=10.1002/prot.25783;
RA   Pinheiro-Aguiar R., do Amaral V.S.G., Pereira I.B., Kurtenbach E.,
RA   Almeida F.C.L.;
RT   "Nuclear magnetic resonance solution structure of Pisum sativum defensin 2
RT   provides evidence for the presence of hydrophobic surface-clusters.";
RL   Proteins 88:242-246(2020).
CC   -!- FUNCTION: Possesses antifungal activity sensitive to inorganic cations.
CC   -!- TISSUE SPECIFICITY: Epidermis and vascular bundles of pods, stems,
CC       roots, leaves and wet or dry seeds.
CC   -!- DEVELOPMENTAL STAGE: Mature seed in dormancy.
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR   PDB; 6NOM; NMR; -; A=1-47.
DR   PDBsum; 6NOM; -.
DR   AlphaFoldDB; P81930; -.
DR   BMRB; P81930; -.
DR   SMR; P81930; -.
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   3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Plant defense.
FT   CHAIN           1..47
FT                   /note="Defensin-2"
FT                   /id="PRO_0000074243"
FT   DISULFID        3..47
FT                   /evidence="ECO:0000269|PubMed:31294889,
FT                   ECO:0007744|PDB:6NOM"
FT   DISULFID        14..35
FT                   /evidence="ECO:0000269|PubMed:31294889,
FT                   ECO:0007744|PDB:6NOM"
FT   DISULFID        20..41
FT                   /evidence="ECO:0000269|PubMed:31294889,
FT                   ECO:0007744|PDB:6NOM"
FT   DISULFID        24..43
FT                   /evidence="ECO:0000269|PubMed:31294889,
FT                   ECO:0007744|PDB:6NOM"
FT   STRAND          3..11
FT                   /evidence="ECO:0007829|PDB:6NOM"
FT   HELIX           20..26
FT                   /evidence="ECO:0007829|PDB:6NOM"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:6NOM"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:6NOM"
SQ   SEQUENCE   47 AA;  5404 MW;  5AB56FBD582EE717 CRC64;
     KTCENLSGTF KGPCIPDGNC NKHCRNNEHL LSGRCRDDFR CWCTNRC