ID   DEF1_CLITE              Reviewed;          49 AA.
AC   Q7M1F2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Defensin-like protein 1;
DE   AltName: Full=Cysteine-rich antimicrobial protein 1;
DE   AltName: Full=Defensin AMP1;
DE            Short=CtAMP1;
OS   Clitoria ternatea (Butterfly pea).
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; indigoferoid/millettioid clade; Phaseoleae; Clitoria.
OX   NCBI_TaxID=43366;
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=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; S66219; S66219.
DR   AlphaFoldDB; Q7M1F2; -.
DR   SMR; Q7M1F2; -.
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..49
FT                   /note="Defensin-like protein 1"
FT                   /id="PRO_0000366951"
FT   DISULFID        3..49
FT                   /evidence="ECO:0000250"
FT   DISULFID        14..35
FT                   /evidence="ECO:0000250"
FT   DISULFID        20..43
FT                   /evidence="ECO:0000250"
FT   DISULFID        24..45
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   49 AA;  5613 MW;  7958823CB255D2CE CRC64;
     NLCERASLTW TGNCGNTGHC DTQCRNWESA KHGACHKRGN WKCFCYFNC