ID   DEFD2_SPIOL             Reviewed;          52 AA.
AC   P81571;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Defensin D2;
DE   AltName: Full=Antimicrobial peptide D2;
DE   AltName: Full=So-D2;
DE   Flags: Fragment;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   STRAIN=cv. Matador; TISSUE=Leaf;
RX   PubMed=9762899; DOI=10.1016/s0014-5793(98)01060-6;
RA   Segura A., Moreno M., Molina A., Garcia-Olmedo F.;
RT   "Novel defensin subfamily from spinach (Spinacia oleracea).";
RL   FEBS Lett. 435:159-162(1998).
CC   -!- FUNCTION: Antimicrobial peptide. Active against Fusarium spp., Gram-
CC       positive and Gram-negative bacterial pathogens.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Distributed in the epidermal cell layer of leaves
CC       and in the subepidermal layer region of stems. Not in roots.
CC   -!- DEVELOPMENTAL STAGE: Present throughout the life of the leaf.
CC   -!- MASS SPECTROMETRY: Mass=5804; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9762899};
CC   -!- SIMILARITY: Belongs to the DEFL family. Group IV subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P81571; -.
DR   SMR; P81571; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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   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   Antibiotic; Antimicrobial; Cell wall; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Plant defense; Secreted.
FT   CHAIN           1..>52
FT                   /note="Defensin D2"
FT                   /id="PRO_0000074252"
FT   DISULFID        8..52
FT                   /evidence="ECO:0000250"
FT   DISULFID        19..39
FT                   /evidence="ECO:0000250"
FT   DISULFID        25..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        29..48
FT                   /evidence="ECO:0000250"
FT   NON_TER         52
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   52 AA;  5804 MW;  F2F736E3ADF8FEBB CRC64;
     GIFSSRKCKT PSKTFKGICT RDSNCDTSCR YEGYPAGDCK GIRRRCMCSK PC