ID   DEF1_PINSY              Reviewed;          83 AA.
AC   A4L7R7;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Defensin-1;
DE   Flags: Precursor;
GN   Name=Def1 {ECO:0000312|EMBL:ABO61348.1};
OS   Pinus sylvestris (Scotch pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=3349;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABO61348.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Root {ECO:0000312|EMBL:ABO61348.1};
RX   PubMed=19683554; DOI=10.1016/j.peptides.2009.08.007;
RA   Kovaleva V., Kiyamova R., Cramer R., Krynytskyy H., Gout I., Filonenko V.,
RA   Gout R.;
RT   "Purification and molecular cloning of antimicrobial peptides from Scots
RT   pine seedlings.";
RL   Peptides 30:2136-2143(2009).
CC   -!- FUNCTION: Plant defense peptide. Has antifungal activity against
CC       B.cinera, F.oxysporum, F.solani and H.annosum with IC(50) values of 0.4
CC       ug/ml, 2.9 ug/ml, 0.9 ug/ml and 1.4 ug/ml, respectively. Has modest
CC       antifungal activity against C.albicans and T.reesei. Causes thickening
CC       of F.oxysporum hyphae and an increase in their branching. Lacks
CC       antibacterial activity against the Gram-negative bacteria E.coli and
CC       E.carotovora. {ECO:0000269|PubMed:19683554}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O65740}.
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000255}.
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DR   EMBL; EF455616; ABO61348.1; -; mRNA.
DR   PDB; 5NCE; NMR; -; A=34-83.
DR   PDBsum; 5NCE; -.
DR   AlphaFoldDB; A4L7R7; -.
DR   BMRB; A4L7R7; -.
DR   SMR; A4L7R7; -.
DR   PRIDE; A4L7R7; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
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; Disulfide bond; Fungicide; Plant defense;
KW   Secreted; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..83
FT                   /note="Defensin-1"
FT                   /id="PRO_0000392921"
FT   DISULFID        36..82
FT                   /evidence="ECO:0000250|UniProtKB:P32026"
FT   DISULFID        47..67
FT                   /evidence="ECO:0000250|UniProtKB:P32026"
FT   DISULFID        53..76
FT                   /evidence="ECO:0000250|UniProtKB:P32026"
FT   DISULFID        57..78
FT                   /evidence="ECO:0000250|UniProtKB:P32026"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:5NCE"
FT   HELIX           50..60
FT                   /evidence="ECO:0007829|PDB:5NCE"
FT   STRAND          63..68
FT                   /evidence="ECO:0007829|PDB:5NCE"
FT   STRAND          70..73
FT                   /evidence="ECO:0007829|PDB:5NCE"
FT   STRAND          75..81
FT                   /evidence="ECO:0007829|PDB:5NCE"
SQ   SEQUENCE   83 AA;  9017 MW;  2B0399E825C3A0E2 CRC64;
     MAGKGVGSRL STLFLLVLLV ITIGMMQVQV AEGRMCKTPS GKFKGYCVNN TNCKNVCRTE
     GFPTGSCDFH VAGRKCYCYK PCP