ID   DEF_NICAL               Reviewed;         105 AA.
AC   Q8GTM0;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Flower-specific defensin;
DE   AltName: Full=NaD1;
DE   Flags: Precursor;
GN   Name=D1;
OS   Nicotiana alata (Winged tobacco) (Persian tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND PROTEIN SEQUENCE OF
RP   26-33.
RX   PubMed=12644678; DOI=10.1104/pp.102.016626;
RA   Lay F.T., Brugliera F., Anderson M.A.;
RT   "Isolation and properties of floral defensins from ornamental tobacco and
RT   petunia.";
RL   Plant Physiol. 131:1283-1293(2003).
RN   [2]
RP   STRUCTURE BY NMR OF 26-72.
RX   PubMed=12473460; DOI=10.1016/s0022-2836(02)01103-8;
RA   Lay F.T., Schirra H.J., Scanlon M.J., Anderson M.A., Craik D.J.;
RT   "The three-dimensional solution structure of NaD1, a new floral defensin
RT   from Nicotiana alata and its application to a homology model of the crop
RT   defense protein alfAFP.";
RL   J. Mol. Biol. 325:175-188(2003).
CC   -!- FUNCTION: Plant defense peptide with antifungal activity against
CC       F.oxysporum and B.cinerea. Retards the growth of the Lepidopteran
CC       insect pests H.armigera and H.punctigera.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Stable under extremes of pH.;
CC       Temperature dependence:
CC         Stable under extremes of temperature.;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Vacuole
CC       {ECO:0000269|PubMed:12644678}.
CC   -!- TISSUE SPECIFICITY: Most abundant in the epidermal cell layers of the
CC       petals and sepals, within the connective cells of the anthers, and the
CC       cortical cells of the style. Not detected in the tapetum, pollen mother
CC       cells, the transmitting tissue, the vascular bundles of the anther and
CC       style or in leaves. Expressed also in ovaries, but barley detectable in
CC       roots.
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR   EMBL; AF509566; AAN70999.1; -; mRNA.
DR   PDB; 4AAZ; X-ray; 1.40 A; A/B=26-72.
DR   PDB; 4AB0; X-ray; 1.64 A; A/B=26-72.
DR   PDB; 4CQK; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=26-72.
DR   PDB; 6B55; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=25-72.
DR   PDBsum; 4AAZ; -.
DR   PDBsum; 4AB0; -.
DR   PDBsum; 4CQK; -.
DR   PDBsum; 6B55; -.
DR   AlphaFoldDB; Q8GTM0; -.
DR   SMR; Q8GTM0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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   3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Plant defense; Secreted; Signal; Vacuole.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:12644678"
FT   CHAIN           26..72
FT                   /note="Flower-specific defensin"
FT                   /id="PRO_0000007042"
FT   PROPEP          73..105
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000007043"
FT   DISULFID        28..72
FT   DISULFID        39..59
FT   DISULFID        45..66
FT   DISULFID        49..68
FT   STRAND          27..31
FT                   /evidence="ECO:0007829|PDB:4AAZ"
FT   HELIX           42..51
FT                   /evidence="ECO:0007829|PDB:4AAZ"
FT   STRAND          55..59
FT                   /evidence="ECO:0007829|PDB:4AAZ"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:4AAZ"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:4AAZ"
SQ   SEQUENCE   105 AA;  11722 MW;  DA7F41736CEE6AC3 CRC64;
     MARSLCFMAF AILAMMLFVA YEVQARECKT ESNTFPGICI TKPPCRKACI SEKFTDGHCS
     KILRRCLCTK PCVFDEKMTK TGAEILAEEA KTLAAALLEE EIMDN