ID   AFP1_TRANT              Reviewed;          11 AA.
AC   B3EWE8;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Antifungal peptide 1 {ECO:0000303|PubMed:21736910};
DE            Short=Tn-AFP1 {ECO:0000303|PubMed:21736910};
OS   Trapa natans (Water chestnut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Trapa.
OX   NCBI_TaxID=22666;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=Fruit flesh {ECO:0000269|PubMed:21736910};
RX   PubMed=21736910; DOI=10.1016/j.peptides.2011.06.020;
RA   Mandal S.M., Migliolo L., Franco O.L., Ghosh A.K.;
RT   "Identification of an antifungal peptide from Trapa natans fruits with
RT   inhibitory effects on Candida tropicalis biofilm formation.";
RL   Peptides 32:1741-1747(2011).
CC   -!- FUNCTION: Has antifungal activity against C.tropicalis (MIC=32 ug/ml)
CC       including the inhibition of biofilm formation. Has virtually no
CC       hemolytic activity against mouse erythrocytes.
CC       {ECO:0000269|PubMed:21736910}.
CC   -!- MASS SPECTROMETRY: Mass=1230.237; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21736910};
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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.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Fungicide.
FT   PEPTIDE         1..11
FT                   /note="Antifungal peptide 1"
FT                   /evidence="ECO:0000269|PubMed:21736910"
FT                   /id="PRO_0000415957"
SQ   SEQUENCE   11 AA;  1233 MW;  8285D9C6A73761F1 CRC64;
     LMCTHPLDCS N