ID   DEF2_NIGSA              Reviewed;          50 AA.
AC   P86973;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Defensin D2 {ECO:0000303|PubMed:21144761};
DE            Short=Ns-D2 {ECO:0000303|PubMed:21144761};
OS   Nigella sativa (Black cumin).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Ranunculoideae;
OC   Nigelleae; Nigella.
OX   NCBI_TaxID=555479;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, DISULFIDE BONDS, AND MASS SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000269|PubMed:21144761};
RX   PubMed=21144761; DOI=10.1016/j.plaphy.2010.10.008;
RA   Rogozhin E.A., Oshchepkova Y.I., Odintsova T.I., Khadeeva N.V.,
RA   Veshkurova O.N., Egorov T.A., Grishin E.V., Salikhov S.I.;
RT   "Novel antifungal defensins from Nigella sativa L. seeds.";
RL   Plant Physiol. Biochem. 49:131-137(2011).
CC   -!- FUNCTION: Antimicrobial peptide active against fungi, Gram-positive and
CC       Gram-negative bacteria. Inhibits growth of hyphae in the fungi A.niger
CC       (IC(50)=3.5 ug/ml), B.sorokiniana (IC(50)=1.8 ug/ml), F.oxysporum
CC       (IC(50)=5.3 ug/ml), F.graminearum (IC(50)=6.9 ug/ml), F.culmorum
CC       (IC(50)=6.9 ug/ml) and B.cinerea (IC(50)=13.7 ug/ml). Has no effect on
CC       spore germination. Destroys spores in germinated conidia by disruption
CC       of cell walls and membranes in A.niger and B.sorokiniana. Causes
CC       vacuolization of germinated macro- and microconidia in F.oxysporum,
CC       F.graminearum and F.culmorum. Strongly inhibits growth of P.infestans
CC       on potato tubers above concentrations of 3.4 ug/ml. Inhibits growth of
CC       Gram-positive bacteria C.michiganensis and B.subtilis and of Gram-
CC       negative bacteria P.syringae, E.carotovora and E.coli.
CC       {ECO:0000269|PubMed:21144761}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P69241}.
CC   -!- PTM: Contains 4 disulfide bonds. {ECO:0000269|PubMed:21144761}.
CC   -!- MASS SPECTROMETRY: Mass=5492.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21144761};
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000255}.
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DR   AlphaFoldDB; P86973; -.
DR   SMR; P86973; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
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   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Plant defense; Secreted.
FT   CHAIN           1..50
FT                   /note="Defensin D2"
FT                   /id="PRO_0000412715"
FT   DISULFID        3..50
FT                   /evidence="ECO:0000250|UniProtKB:P69241"
FT   DISULFID        14..35
FT                   /evidence="ECO:0000250|UniProtKB:P69241"
FT   DISULFID        20..44
FT                   /evidence="ECO:0000250|UniProtKB:P69241"
FT   DISULFID        24..46
FT                   /evidence="ECO:0000250|UniProtKB:P69241"
SQ   SEQUENCE   50 AA;  5503 MW;  CE7C0EF50E086702 CRC64;
     KFCEKPSGTW SGVCGNSGAC KDQCIRLEGA KHGSCNYKLP AHRCICYYEC