ID   DEF_LENCC               Reviewed;          74 AA.
AC   B3F051; P85530;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=Defensin Lc-def {ECO:0000303|PubMed:18468512, ECO:0000312|EMBL:ABP04037.1};
DE   Flags: Precursor;
OS   Lens culinaris subsp. culinaris (Cultivated lentil) (Lens esculenta).
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; Lens.
OX   NCBI_TaxID=362247;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ABP04037.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-74, FUNCTION, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Seedling {ECO:0000269|PubMed:18468512};
RX   PubMed=18468512; DOI=10.1016/j.bbrc.2008.04.161;
RA   Finkina E.I., Shramova E.I., Tagaev A.A., Ovchinnikova T.V.;
RT   "A novel defensin from the lentil Lens culinaris seeds.";
RL   Biochem. Biophys. Res. Commun. 371:860-865(2008).
CC   -!- FUNCTION: Has antifungal activity against the phytopathogenic fungus
CC       A.niger VKM F-2259, but not against A.alternata VKM F-3047. Does not
CC       inhibit trypsin or chymotrypsin. {ECO:0000269|PubMed:18468512}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=5440.41; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18468512};
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF194158; ABP04037.1; -; mRNA.
DR   PDB; 2LJ7; NMR; -; A=28-74.
DR   PDBsum; 2LJ7; -.
DR   AlphaFoldDB; B3F051; -.
DR   BMRB; B3F051; -.
DR   SMR; B3F051; -.
DR   TCDB; 1.C.45.1.4; the plant defensin (plant defensin) family.
DR   GO; GO:0005576; C:extracellular region; 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   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.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:18468512"
FT   CHAIN           28..74
FT                   /note="Defensin Lc-def"
FT                   /evidence="ECO:0000269|PubMed:18468512"
FT                   /id="PRO_5000375684"
FT   DISULFID        30..74
FT                   /evidence="ECO:0000250|UniProtKB:P81929"
FT   DISULFID        41..62
FT                   /evidence="ECO:0000250|UniProtKB:P81929"
FT   DISULFID        47..68
FT                   /evidence="ECO:0000250|UniProtKB:P81929"
FT   DISULFID        51..70
FT                   /evidence="ECO:0000250|UniProtKB:P81929"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:2LJ7"
FT   HELIX           47..53
FT                   /evidence="ECO:0007829|PDB:2LJ7"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:2LJ7"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:2LJ7"
SQ   SEQUENCE   74 AA;  8401 MW;  86D60E44F22CD04F CRC64;
     MEKKTVAALS FLFIVLFVAQ EIAVTEAKTC ENLSDSFKGP CIPDGNCNKH CKEKEHLLSG
     RCRDDFRCWC TRNC