PAFP_PHYAM
ID PAFP_PHYAM Reviewed; 65 AA.
AC P81418; O82728;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Antimicrobial peptide 1;
DE AltName: Full=AFPS-1;
DE AltName: Full=Anti-fungal protein 1;
DE AltName: Full=PAFP-S;
DE AltName: Full=Pa-AMP-1;
DE Short=AMP1;
DE Flags: Precursor;
OS Phytolacca americana (American pokeweed) (Phytolacca decandra).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Phytolaccaceae; Phytolacca.
OX NCBI_TaxID=3527;
RN [1]
RP NUCLEOTIDE SEQUENCE, PROTEIN SEQUENCE OF 28-65, AND TISSUE SPECIFICITY.
RC TISSUE=Seed;
RX PubMed=10759497; DOI=10.1104/pp.122.4.1015;
RA Liu Y., Luo J., Xu C., Ren F., Peng C., Wu G., Zhao J.;
RT "Purification, characterization, and molecular cloning of the gene of a
RT seed-specific antimicrobial protein from pokeweed.";
RL Plant Physiol. 122:1015-1024(2000).
RN [2]
RP PROTEIN SEQUENCE OF 28-65.
RC TISSUE=Seed;
RA Feng S.;
RL Submitted (JUN-1998) to UniProtKB.
RN [3]
RP STRUCTURE BY NMR OF 28-65.
RX PubMed=11551192; DOI=10.1021/bi010167k;
RA Gao G.-H., Liu W., Dai J.-X., Wang J.-F., Hu Z., Zhang Y., Wang D.-C.;
RT "Solution structure of PAFP-S: a new knottin-type antifungal peptide from
RT the seeds of Phytolacca americana.";
RL Biochemistry 40:10973-10978(2001).
CC -!- FUNCTION: Possesses antifungal activity.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Seed specific. {ECO:0000269|PubMed:10759497}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC -!- SIMILARITY: Belongs to the AMP family. {ECO:0000305}.
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DR EMBL; AF048745; AAC05129.1; -; mRNA.
DR EMBL; AF105062; AAD17942.1; -; Genomic_DNA.
DR PDB; 1DKC; NMR; -; A=28-65.
DR PDBsum; 1DKC; -.
DR AlphaFoldDB; P81418; -.
DR SMR; P81418; -.
DR EvolutionaryTrace; P81418; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 3D-structure; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Fungicide; Knottin; Plant defense; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:10759497, ECO:0000269|Ref.2"
FT CHAIN 28..65
FT /note="Antimicrobial peptide 1"
FT /id="PRO_0000001312"
FT DISULFID 30..47
FT DISULFID 37..51
FT DISULFID 46..62
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1DKC"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1DKC"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:1DKC"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1DKC"
SQ SEQUENCE 65 AA; 6804 MW; 0073DE3ABBDC5B5C CRC64;
MAKVSSAYLK FALVMILLLS VISAVMSAGC IKNGGRCNAS AGPPYCCSSY CFQIAGQSYG
VCKNR
