DEF1_HEUSA
ID DEF1_HEUSA Reviewed; 54 AA.
AC P0C8Y5; Q7M1F4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Defensin-like protein 1;
DE AltName: Full=Cysteine-rich antifungal protein 1;
DE AltName: Full=Defensin AFP1;
DE Short=HsAFP1;
OS Heuchera sanguinea (Coralbells).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Saxifragales; Saxifragaceae; Heuchera.
OX NCBI_TaxID=43368;
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=9405418; DOI=10.1074/jbc.272.51.32176;
RA Thevissen K., Osborn R.W., Acland D.P., Broekaert W.F.;
RT "Specific, high affinity binding sites for an antifungal plant defensin on
RT Neurospora crassa hyphae and microsomal membranes.";
RL J. Biol. Chem. 272:32176-32181(1997).
RN [3]
RP FUNCTION.
RX PubMed=16284838; DOI=10.1023/a:1007018423603;
RA De Lucca A.J., Jacks T.J., Broekaert W.J.;
RT "Fungicidal and binding properties of three plant peptides.";
RL Mycopathologia 144:87-91(1998).
CC -!- FUNCTION: Possesses antifungal activity insensitive to inorganic
CC cations. Causes germ tubes and hyphae to swell and form multiple hyphal
CC buds. Binds to the plasma membrane of the fungus. Has no inhibitory
CC effect on insect gut alpha-amylase. {ECO:0000269|PubMed:16284838,
CC ECO:0000269|PubMed:7628617, ECO:0000269|PubMed:9405418}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEFL family. {ECO:0000305}.
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DR PIR; S66220; S66220.
DR PDB; 2N2Q; NMR; -; A=1-54.
DR PDBsum; 2N2Q; -.
DR AlphaFoldDB; P0C8Y5; -.
DR SMR; P0C8Y5; -.
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; 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.
FT CHAIN 1..54
FT /note="Defensin-like protein 1"
FT /id="PRO_0000366953"
FT DISULFID 6..54
FT /evidence="ECO:0000250"
FT DISULFID 17..39
FT /evidence="ECO:0000250"
FT DISULFID 23..48
FT /evidence="ECO:0000250"
FT DISULFID 27..50
FT /evidence="ECO:0000250"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2N2Q"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:2N2Q"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:2N2Q"
FT STRAND 43..53
FT /evidence="ECO:0007829|PDB:2N2Q"
SQ SEQUENCE 54 AA; 5949 MW; 67FA1CCFBB92A7C9 CRC64;
DGVKLCDVPS GTWSGHCGSS SKCSQQCKDR EHFAYGGACH YQFPSVKCFC KRQC
