DEF1_PETHY
ID DEF1_PETHY Reviewed; 103 AA.
AC Q8H6Q1;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Floral defensin-like protein 1;
DE AltName: Full=PhD1;
DE Flags: Precursor;
GN Name=D1;
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).
RN [2]
RP STRUCTURE BY NMR OF 26-72.
RX PubMed=12846570; DOI=10.1021/bi034379o;
RA Janssen B.-J., Schirra H.J., Lay F.T., Anderson M.A., Craik D.J.;
RT "Structure of Petunia hybrida defensin 1, a novel plant defensin with five
RT disulfide bonds.";
RL Biochemistry 42:8214-8222(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.
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; AF507975; AAN64750.1; -; mRNA.
DR PDB; 1N4N; NMR; -; A=26-72.
DR PDBsum; 1N4N; -.
DR AlphaFoldDB; Q8H6Q1; -.
DR SMR; Q8H6Q1; -.
DR EvolutionaryTrace; Q8H6Q1; -.
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; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR SUPFAM; SSF57095; SSF57095; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Fungicide; Knottin; Plant defense; Secreted; Signal; Vacuole.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:12644678"
FT CHAIN 26..72
FT /note="Floral defensin-like protein 1"
FT /id="PRO_0000007047"
FT PROPEP 73..103
FT /note="Removed in mature form"
FT /id="PRO_0000007048"
FT DISULFID 28..72
FT DISULFID 32..48
FT DISULFID 39..59
FT DISULFID 45..66
FT DISULFID 49..68
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1N4N"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:1N4N"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1N4N"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1N4N"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1N4N"
SQ SEQUENCE 103 AA; 11361 MW; A8B629A3E06A0D01 CRC64;
MARSICFFAV AILALMLFAA YDAEAATCKA ECPTWDSVCI NKKPCVACCK KAKFSDGHCS
KILRRCLCTK ECVFEKTEAT QTETFTKDVN TLAEALLEAD MMV
