ID   DEF1_RAPSA              Reviewed;          80 AA.
AC   P69241; P30225; Q41163;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Defensin-like protein 1;
DE   AltName: Full=Cysteine-rich antifungal protein 1;
DE            Short=AFP1;
DE   Flags: Precursor;
GN   Name=AFP1;
OS   Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus.
OX   NCBI_TaxID=3726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Ronde Rode Kleine Witpunt; TISSUE=Seed;
RX   PubMed=7780308; DOI=10.2307/3870116;
RA   Terras F.R.G., Eggermont K., Kovaleva V., Raikhel N.V., Osborn R.W.,
RA   Kester A., Rees S.B., Torrekens S., van Leuven F., Vanderleyden J.,
RA   Cammue B.P.A., Broekaert W.F.;
RT   "Small cysteine-rich antifungal proteins from radish: their role in host
RT   defense.";
RL   Plant Cell 7:573-588(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 30-73.
RC   TISSUE=Seed;
RX   PubMed=1639777; DOI=10.1016/s0021-9258(19)49534-3;
RA   Terras F.R.G., Schoofs H.M.E., de Bolle M.F.C., van Leuven F., Rees S.B.,
RA   Vanderleyden J., Cammue B.P.A., Broekaert W.F.;
RT   "Analysis of two novel classes of plant antifungal proteins from radish
RT   (Raphanus sativus L.) seeds.";
RL   J. Biol. Chem. 267:15301-15309(1992).
RN   [3]
RP   STRUCTURE BY NMR OF 30-80, AND DISULFIDE BONDS.
RX   PubMed=9636715; DOI=10.1006/jmbi.1998.1767;
RA   Fant F., Vranken W.F., Broekaert W.F., Borremans F.A.M.;
RT   "Determination of the three-dimensional solution structure of Raphanus
RT   sativus antifungal protein 1 by 1H NMR.";
RL   J. Mol. Biol. 279:257-270(1998).
CC   -!- FUNCTION: Possesses antifungal activity sensitive to inorganic cations.
CC   -!- SUBUNIT: Forms oligomers in its native state.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR   EMBL; U18557; AAA69541.1; -; mRNA.
DR   PIR; T10176; T10176.
DR   RefSeq; XP_018469135.1; XM_018613633.1.
DR   PDB; 1AYJ; NMR; -; A=31-80.
DR   PDBsum; 1AYJ; -.
DR   AlphaFoldDB; P69241; -.
DR   BMRB; P69241; -.
DR   SMR; P69241; -.
DR   TCDB; 1.C.45.1.1; the plant defensin (plant defensin) family.
DR   GeneID; 108840814; -.
DR   KEGG; rsz:108840814; -.
DR   OrthoDB; 1565340at2759; -.
DR   EvolutionaryTrace; P69241; -.
DR   Proteomes; UP000504610; Unplaced.
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; Pyrrolidone carboxylic acid; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:1639777"
FT   CHAIN           30..80
FT                   /note="Defensin-like protein 1"
FT                   /id="PRO_0000007034"
FT   MOD_RES         30
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P30231"
FT   DISULFID        33..80
FT                   /evidence="ECO:0000269|PubMed:9636715,
FT                   ECO:0007744|PDB:1AYJ"
FT   DISULFID        44..65
FT                   /evidence="ECO:0000269|PubMed:9636715,
FT                   ECO:0007744|PDB:1AYJ"
FT   DISULFID        50..74
FT                   /evidence="ECO:0000269|PubMed:9636715,
FT                   ECO:0007744|PDB:1AYJ"
FT   DISULFID        54..76
FT                   /evidence="ECO:0000269|PubMed:9636715,
FT                   ECO:0007744|PDB:1AYJ"
FT   STRAND          33..36
FT                   /evidence="ECO:0007829|PDB:1AYJ"
FT   HELIX           47..57
FT                   /evidence="ECO:0007829|PDB:1AYJ"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:1AYJ"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:1AYJ"
FT   STRAND          73..78
FT                   /evidence="ECO:0007829|PDB:1AYJ"
SQ   SEQUENCE   80 AA;  8734 MW;  05B90FAAC8DA6C2B CRC64;
     MAKFASIIAL LFAALVLFAA FEAPTMVEAQ KLCERPSGTW SGVCGNNNAC KNQCINLEKA
     RHGSCNYVFP AHKCICYFPC