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AMP1_MACIN
ID   AMP1_MACIN              Reviewed;         102 AA.
AC   P80915; O04396;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Antimicrobial peptide 1;
DE            Short=AMP1;
DE   AltName: Full=MiAMP1;
DE   Flags: Precursor;
OS   Macadamia integrifolia (Macadamia nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Proteales; Proteaceae; Macadamia.
OX   NCBI_TaxID=60698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 27-96.
RC   TISSUE=Seed;
RX   PubMed=9108242; DOI=10.1111/j.1432-1033.1997.00743.x;
RA   Marcus J.P., Green J.L., Goulter K.C., Harrison S.J., Manners J.M.;
RT   "Purification, characterisation and cDNA cloning of an antimicrobial
RT   peptide from Macadamia integrifolia.";
RL   Eur. J. Biochem. 244:743-749(1997).
RN   [2]
RP   STRUCTURE BY NMR OF 27-102.
RX   PubMed=10543955; DOI=10.1006/jmbi.1999.3163;
RA   McManus A.M., Nielsen K.J., Marcus J.P., Harrison S.J., Green J.L.,
RA   Manners J.M., Craik D.J.;
RT   "MiAMP1, a novel protein from Macadamia integrifolia adopts a Greek key
RT   beta-barrel fold unique amongst plant antimicrobial proteins.";
RL   J. Mol. Biol. 293:629-638(1999).
CC   -!- FUNCTION: Antimicrobial peptide which inhibits the growth of a variety
CC       of fungi, oomycetes, Gram-positive bacterial phytopatogenes and
CC       S.cerevisiae in vitro. No activity against E.coli.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Its antimicrobial activity is diminished by calcium and
CC       potassium chloride salts.
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DR   EMBL; Y10903; CAA71842.1; -; mRNA.
DR   PDB; 1C01; NMR; -; A=27-102.
DR   PDBsum; 1C01; -.
DR   AlphaFoldDB; P80915; -.
DR   SMR; P80915; -.
DR   EvolutionaryTrace; P80915; -.
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   GO; GO:0045926; P:negative regulation of growth; IEA:InterPro.
DR   Gene3D; 2.60.20.30; -; 1.
DR   InterPro; IPR015791; Antimic/Inh_G_crystallin-like.
DR   InterPro; IPR015201; Antimicrobial_MiAMP1.
DR   InterPro; IPR011024; G_crystallin-like.
DR   Pfam; PF09117; MiAMP1; 1.
DR   SUPFAM; SSF49695; SSF49695; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Plant defense; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:9108242"
FT   CHAIN           27..102
FT                   /note="Antimicrobial peptide 1"
FT                   /id="PRO_0000020709"
FT   DISULFID        37..90
FT   DISULFID        47..102
FT   DISULFID        49..75
FT   STRAND          28..31
FT                   /evidence="ECO:0007829|PDB:1C01"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:1C01"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:1C01"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:1C01"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:1C01"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:1C01"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:1C01"
FT   STRAND          79..85
FT                   /evidence="ECO:0007829|PDB:1C01"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:1C01"
SQ   SEQUENCE   102 AA;  10944 MW;  9FB79954454B9311 CRC64;
     MASTKLFFSV ITVMMLIAMA SEMVNGSAFT VWSGPGCNNR AERYSKCGCS AIHQKGGYDF
     SYTGQTAALY NQAGCSGVAH TRFGSSARAC NPFGWKSIFI QC
 
 
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