ID   AFP1_PASAL              Reviewed;          31 AA.
AC   B3EWF0;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Antifungal protein 1 {ECO:0000303|PubMed:20955745};
DE            Short=Pa-AFP1 {ECO:0000303|PubMed:20955745};
DE   Flags: Fragment;
OS   Passiflora alata (Winged-stem passion flower) (Fragrant granadilla).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Passifloraceae; Passiflora.
OX   NCBI_TaxID=159422;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, DISULFIDE BONDS, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000269|PubMed:20955745};
RX   PubMed=20955745; DOI=10.1016/j.peptides.2010.10.011;
RA   Ribeiro S.M., Almeida R.G., Pereira C.A., Moreira J.S., Pinto M.F.,
RA   Oliveira A.C., Vasconcelos I.M., Oliveira J.T., Santos M.O., Dias S.C.,
RA   Franco O.L.;
RT   "Identification of a Passiflora alata Curtis dimeric peptide showing
RT   identity with 2S albumins.";
RL   Peptides 32:868-874(2011).
CC   -!- FUNCTION: Has antifungal activity against C.gloeosporioides but not
CC       against B.cinerea and Fusarium sp. or against various yeasts. Has no
CC       antibacterial activity. {ECO:0000269|PubMed:20955745}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. {ECO:0000269|PubMed:20955745}.
CC   -!- PTM: Disulfide bonds. {ECO:0000269|PubMed:20955745}.
CC   -!- MASS SPECTROMETRY: Mass=11569.76; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20955745};
CC   -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; B3EWF0; -.
DR   SMR; B3EWF0; -.
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; Disulfide bond; Fungicide;
KW   Plant defense.
FT   CHAIN           1..>31
FT                   /note="Antifungal protein 1"
FT                   /id="PRO_0000415954"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         31
FT                   /evidence="ECO:0000303|PubMed:20955745"
SQ   SEQUENCE   31 AA;  3584 MW;  3811652C98C3E079 CRC64;
     PGAGSQEERM QGQMEGQDFS HEERFLSMVR E