DEF1_PEA
ID DEF1_PEA Reviewed; 46 AA.
AC P81929;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Defensin-1;
DE AltName: Full=Antifungal protein Psd1;
DE AltName: Full=Defense-related peptide 1;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=cv. Mikado; TISSUE=Epidermis, and Seed endosperm;
RX PubMed=10860545; DOI=10.1006/abbi.2000.1824;
RA Almeida M.S., Cabral K.M., Zingali R.B., Kurtenbach E.;
RT "Characterization of two novel defense peptides from pea (Pisum sativum)
RT seeds.";
RL Arch. Biochem. Biophys. 378:278-286(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-23, AND DISULFIDE BONDS.
RX PubMed=11697857; DOI=10.1006/abbi.2001.2564;
RA Almeida M.S., Cabral K.S., de Medeiros L.N., Valente A.P., Almeida F.C.,
RA Kurtenbach E.;
RT "cDNA cloning and heterologous expression of functional cysteine-rich
RT antifungal protein Psd1 in the yeast Pichia pastoris.";
RL Arch. Biochem. Biophys. 395:199-207(2001).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=11812144; DOI=10.1006/jmbi.2001.5252;
RA Almeida M.S., Cabral K.M., Kurtenbach E., Almeida F.C., Valente A.P.;
RT "Solution structure of Pisum sativum defensin 1 by high resolution NMR:
RT plant defensins, identical backbone with different mechanisms of action.";
RL J. Mol. Biol. 315:749-757(2002).
CC -!- FUNCTION: Possesses antifungal activity sensitive to inorganic cations.
CC -!- TISSUE SPECIFICITY: Epidermis and vascular bundles of pods, stems,
CC roots, leaves and wet or dry seeds.
CC -!- DEVELOPMENTAL STAGE: Mature seed in dormancy.
CC -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR PDB; 1JKZ; NMR; -; A=1-46.
DR PDBsum; 1JKZ; -.
DR AlphaFoldDB; P81929; -.
DR SMR; P81929; -.
DR EvolutionaryTrace; P81929; -.
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; 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 3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Fungicide; Plant defense.
FT CHAIN 1..46
FT /note="Defensin-1"
FT /id="PRO_0000074242"
FT DISULFID 3..46
FT /evidence="ECO:0000269|PubMed:11697857"
FT DISULFID 14..35
FT /evidence="ECO:0000269|PubMed:11697857"
FT DISULFID 20..40
FT /evidence="ECO:0000269|PubMed:11697857"
FT DISULFID 24..42
FT /evidence="ECO:0000269|PubMed:11697857"
FT CONFLICT 43
FT /note="T -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1JKZ"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1JKZ"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:1JKZ"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1JKZ"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1JKZ"
SQ SEQUENCE 46 AA; 5209 MW; 12B4ABCF0A6701FC CRC64;
KTCEHLADTY RGVCFTNASC DDHCKNKAHL ISGTCHNWKC FCTQNC
