ID   AMP1_MIRJA              Reviewed;          61 AA.
AC   P25403;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 4.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Antimicrobial peptide 1;
DE   AltName: Full=MJ-AMP1;
DE            Short=AMP1;
DE   Flags: Precursor; Fragment;
GN   Name=AMP1;
OS   Mirabilis jalapa (Garden four-o'clock).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Nyctaginaceae; Mirabilis.
OX   NCBI_TaxID=3538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=7647302; DOI=10.1007/bf00021195;
RA   de Bolle M.F., Eggermont K., Duncan R.E., Osborn R.W., Terras F.R.G.,
RA   Broekaert W.F.;
RT   "Cloning and characterization of two cDNA clones encoding seed-specific
RT   antimicrobial peptides from Mirabilis jalapa L.";
RL   Plant Mol. Biol. 28:713-721(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-61, AND PYROGLUTAMATE FORMATION AT GLN-25.
RC   TISSUE=Seed;
RX   PubMed=1733929; DOI=10.1016/s0021-9258(18)45866-8;
RA   Cammue B.P.A., de Bolle M.F.C., Terras F.R.G., Proost P., van Damme J.,
RA   Rees S.B., Vanderleyden J., Broekaert W.F.;
RT   "Isolation and characterization of a novel class of plant antimicrobial
RT   peptides from Mirabilis jalapa L. seeds.";
RL   J. Biol. Chem. 267:2228-2233(1992).
CC   -!- FUNCTION: Possesses antifungal activity and is also active on two
CC       tested Gram-positive bacteria but is non-toxic for Gram-negative
CC       bacteria and cultured human cells.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Found only in seeds.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- PTM: Three disulfide bonds are present.
CC   -!- SIMILARITY: Belongs to the AMP family. {ECO:0000305}.
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DR   EMBL; U15538; AAA80484.1; -; mRNA.
DR   PIR; S57815; S57815.
DR   AlphaFoldDB; P25403; -.
DR   SMR; P25403; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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   InterPro; IPR013006; Antimicrobial_C6_CS.
DR   InterPro; IPR009101; Gurmarin/antifun_pep.
DR   InterPro; IPR024206; Gurmarin/antimicrobial_peptd.
DR   Pfam; PF11410; Antifungal_pept; 1.
DR   SUPFAM; SSF57048; SSF57048; 1.
DR   PROSITE; PS60011; PLANT_C6_AMP; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Knottin; Plant defense; Pyrrolidone carboxylic acid; Secreted;
KW   Signal.
FT   SIGNAL          <1..24
FT                   /evidence="ECO:0000269|PubMed:1733929"
FT   CHAIN           25..61
FT                   /note="Antimicrobial peptide 1"
FT                   /id="PRO_0000001310"
FT   MOD_RES         25
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:1733929"
FT   DISULFID        26..43
FT                   /evidence="ECO:0000250"
FT   DISULFID        33..47
FT                   /evidence="ECO:0000250"
FT   DISULFID        42..58
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   61 AA;  6605 MW;  1957BF5FC2FE75C2 CRC64;
     LPVAFLKFAI VLILFIAMSA MIEAQCIGNG GRCNENVGPP YCCSGFCLRQ PGQGYGYCKN
     R