ID   DEF1_DAHME              Reviewed;          50 AA.
AC   P0C8Y4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Defensin-like protein 1;
DE   AltName: Full=Cysteine-rich antimicrobial protein 1;
DE   AltName: Full=Defensin AMP1;
DE            Short=DmAMP1;
OS   Dahlia merckii (Bedding dahlia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Coreopsideae; Dahlia.
OX   NCBI_TaxID=43367;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Seed;
RX   PubMed=7628617; DOI=10.1016/0014-5793(95)00666-w;
RA   Osborn R.W., De Samblanx G.W., Thevissen K., Goderis I., Torrekens S.,
RA   Van Leuven F., Attenborough S., Rees S.B., Broekaert W.F.;
RT   "Isolation and characterisation of plant defensins from seeds of
RT   Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae.";
RL   FEBS Lett. 368:257-262(1995).
RN   [2]
RP   FUNCTION.
RX   PubMed=8663029; DOI=10.1074/jbc.271.25.15018;
RA   Thevissen K., Ghazi A., De Samblanx G.W., Brownlee C., Osborn R.W.,
RA   Broekaert W.F.;
RT   "Fungal membrane responses induced by plant defensins and thionins.";
RL   J. Biol. Chem. 271:15018-15025(1996).
RN   [3]
RP   FUNCTION.
RX   PubMed=10656585; DOI=10.1094/mpmi.2000.13.1.54;
RA   Thevissen K., Osborn R.W., Acland D.P., Broekaert W.F.;
RT   "Specific binding sites for an antifungal plant defensin from Dahlia
RT   (Dahlia merckii) on fungal cells are required for antifungal activity.";
RL   Mol. Plant Microbe Interact. 13:54-61(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=13129623; DOI=10.1016/s0378-1097(03)00590-1;
RA   Thevissen K., Francois I.E.J.A., Takemoto J.Y., Ferket K.K.A.,
RA   Meert E.M.K., Cammue B.P.A.;
RT   "DmAMP1, an antifungal plant defensin from dahlia (Dahlia merckii),
RT   interacts with sphingolipids from Saccharomyces cerevisiae.";
RL   FEMS Microbiol. Lett. 226:169-173(2003).
RN   [5]
RP   BIOTECHNOLOGY.
RX   PubMed=17216480; DOI=10.1007/s00425-006-0471-1;
RA   Zhu Y.J., Agbayani R., Moore P.H.;
RT   "Ectopic expression of Dahlia merckii defensin DmAMP1 improves papaya
RT   resistance to Phytophthora palmivora by reducing pathogen vigor.";
RL   Planta 226:87-97(2007).
RN   [6]
RP   BIOTECHNOLOGY.
RX   PubMed=18618285; DOI=10.1007/s11248-008-9196-1;
RA   Jha S., Tank H.G., Prasad B.D., Chattoo B.B.;
RT   "Expression of Dm-AMP1 in rice confers resistance to Magnaporthe oryzae and
RT   Rhizoctonia solani.";
RL   Transgenic Res. 18:59-69(2009).
CC   -!- FUNCTION: Possesses antimicrobial activity sensitive to inorganic
CC       cations. Has no inhibitory effect on insect gut alpha-amylase. Induces
CC       potential changes in fungal membranes and increased K+ efflux and
CC       Ca(2+) uptake. Interacts with sphingolipids and ergosterols found in
CC       fungal plasma membranes. {ECO:0000269|PubMed:10656585,
CC       ECO:0000269|PubMed:13129623, ECO:0000269|PubMed:7628617,
CC       ECO:0000269|PubMed:8663029}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- BIOTECHNOLOGY: DmAMP1 expression in heterologous plants such as rice or
CC       papaya may provide a broad-spectrum disease resistance.
CC       {ECO:0000269|PubMed:17216480, ECO:0000269|PubMed:18618285}.
CC   -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR   AlphaFoldDB; P0C8Y4; -.
DR   SMR; P0C8Y4; -.
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   Gene3D; 3.30.30.10; -; 1.
DR   InterPro; IPR003614; Scorpion_toxin-like.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   SMART; SM00505; Knot1; 1.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW   Plant defense; Secreted.
FT   CHAIN           1..50
FT                   /note="Defensin-like protein 1"
FT                   /id="PRO_0000366952"
FT   DISULFID        3..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..35
FT                   /evidence="ECO:0000250"
FT   DISULFID        20..44
FT                   /evidence="ECO:0000250"
FT   DISULFID        24..46
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   50 AA;  5525 MW;  05B98EF2AEF1A452 CRC64;
     ELCEKASKTW SGNCGNTGHC DNQCKSWEGA AHGACHVRNG KHMCFCYFNC