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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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