ID   DEF2_PETHY              Reviewed;         101 AA.
AC   Q8H6Q0;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Floral defensin-like protein 2;
DE   AltName: Full=PhD2;
DE   Flags: Precursor;
GN   Name=D2;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 26-33.
RC   STRAIN=cv. Old Glory Blue;
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).
CC   -!- FUNCTION: Plant defense peptide with antifungal activity against
CC       F.oxysporum and B.cinerea.
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 {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Petals.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- PTM: When compared to other plant defensins, the petunia defensins have
CC       an additional fifth disulfide bond.
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR   EMBL; AF507976; AAN64751.1; -; mRNA.
DR   AlphaFoldDB; Q8H6Q0; -.
DR   SMR; Q8H6Q0; -.
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   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW   Knottin; Plant defense; Secreted; Signal; Vacuole.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:12644678"
FT   CHAIN           26..74
FT                   /note="Floral defensin-like protein 2"
FT                   /id="PRO_0000007049"
FT   PROPEP          75..101
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000007050"
FT   DISULFID        28..74
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..48
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..61
FT                   /evidence="ECO:0000250"
FT   DISULFID        45..68
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..70
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   101 AA;  11049 MW;  8E5AFE2BD4052D0B CRC64;
     MARSICFFAV AILALMLFAA YETEAGTCKA ECPTWEGICI NKAPCVKCCK AQPEKFTDGH
     CSKILRRCLC TKPCATEEAT ATLANEVKTM AEALVEEDMM E