DEF1_AESHI
ID DEF1_AESHI Reviewed; 50 AA.
AC Q7M1F3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Defensin-like protein 1;
DE AltName: Full=Cysteine-rich antimicrobial protein 1;
DE AltName: Full=Defensin AMP1;
DE Short=AhAMP1;
OS Aesculus hippocastanum (Horse chestnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Sapindaceae; Hippocastanoideae;
OC Hippocastaneae; Aesculus.
OX NCBI_TaxID=43364;
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 STRUCTURE BY NMR.
RX PubMed=10591099;
RX DOI=10.1002/(sici)1097-0134(19991115)37:3<388::aid-prot7>3.3.co;2-6;
RA Fant F., Vranken W.F., Borremans F.A.M.;
RT "The three-dimensional solution structure of Aesculus hippocastanum
RT antimicrobial protein 1 determined by 1H nuclear magnetic resonance.";
RL Proteins 37:388-403(1999).
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).
CC -!- FUNCTION: Possesses antimicrobial activity sensitive to inorganic
CC cations. Binds specifically to the fungal plasma membrane. Has no
CC inhibitory effect on insect gut alpha-amylase.
CC {ECO:0000269|PubMed:10656585, ECO:0000269|PubMed:7628617}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR PIR; S66218; S66218.
DR PDB; 1BK8; NMR; -; A=1-50.
DR PDBsum; 1BK8; -.
DR AlphaFoldDB; Q7M1F3; -.
DR BMRB; Q7M1F3; -.
DR SMR; Q7M1F3; -.
DR EvolutionaryTrace; Q7M1F3; -.
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 3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Fungicide; Plant defense; Secreted.
FT CHAIN 1..50
FT /note="Defensin-like protein 1"
FT /id="PRO_0000366950"
FT DISULFID 2..50
FT DISULFID 14..35
FT DISULFID 20..44
FT DISULFID 24..46
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1BK8"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1BK8"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:1BK8"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1BK8"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:1BK8"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1BK8"
SQ SEQUENCE 50 AA; 5863 MW; A87D5BF8752BB560 CRC64;
LCNERPSQTW SGNCGNTAHC DKQCQDWEKA SHGACHKREN HWKCFCYFNC
