ID   PLE1_PSEAM              Reviewed;          68 AA.
AC   P81941; P81619; Q9PRJ9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 2.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Pleurocidin;
DE   Flags: Precursor;
GN   Name=ple1;
OS   Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC   Pseudopleuronectes.
OX   NCBI_TaxID=8265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Skin, and Small intestine;
RX   PubMed=10898673; DOI=10.1128/aac.44.8.2039-2045.2000;
RA   Cole A.M., Darouiche R.O., Legarda D., Connell N., Diamond G.;
RT   "Characterization of a fish antimicrobial peptide: gene expression,
RT   subcellular localization, and spectrum of activity.";
RL   Antimicrob. Agents Chemother. 44:2039-2045(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   PubMed=11113283; DOI=10.1016/s0145-305x(00)00052-5;
RA   Douglas S.E., Gallant J.W., Gong Z., Hew C.-L.;
RT   "Cloning and developmental expression of a family of pleurocidin-like
RT   antimicrobial peptides from winter flounder, Pleuronectes americanus
RT   (Walbaum).";
RL   Dev. Comp. Immunol. 25:137-147(2001).
RN   [3]
RP   PROTEIN SEQUENCE OF 23-47, AND CHARACTERIZATION.
RC   TISSUE=Epidermis, and Skin mucus;
RX   PubMed=9115266; DOI=10.1074/jbc.272.18.12008;
RA   Cole A.M., Weis P., Diamond G.;
RT   "Isolation and characterization of pleurocidin, an antimicrobial peptide in
RT   the skin secretions of winter flounder.";
RL   J. Biol. Chem. 272:12008-12013(1997).
RN   [4]
RP   STRUCTURE BY NMR OF 23-47, LIPID-BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=15882067; DOI=10.1021/bi0504005;
RA   Syvitski R.T., Burton I., Mattatall N.R., Douglas S.E., Jakeman D.L.;
RT   "Structural characterization of the antimicrobial peptide pleurocidin from
RT   winter flounder.";
RL   Biochemistry 44:7282-7293(2005).
CC   -!- FUNCTION: Antimicrobial peptide with potent activity against Gram-
CC       positive and Gram-negative bacteria. Activity against E.coli and
CC       B.subtilis. Weaker activity against L.mucor, s.marcescens and
CC       P.aeruginosa. May play a role in innate host defense.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15882067}. Membrane
CC       {ECO:0000269|PubMed:15882067}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:15882067}. Note=Associates with phospholipid
CC       membranes via its amphipathic helix and can insert into the lipid
CC       bilayer.
CC   -!- TISSUE SPECIFICITY: Goblet cells.
CC   -!- MISCELLANEOUS: The peptide is disordered in aqueous solution.
CC       {ECO:0000305|PubMed:15882067}.
CC   -!- SIMILARITY: Belongs to the pleurocidin family. {ECO:0000305}.
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DR   EMBL; AF210241; AAF17252.1; -; Genomic_DNA.
DR   EMBL; AF210242; AAF17253.1; -; mRNA.
DR   EMBL; AF184223; AAG10397.1; -; mRNA.
DR   PDB; 1Z64; NMR; -; A=23-47.
DR   PDB; 2LS9; NMR; -; A=23-47.
DR   PDB; 6RSG; NMR; -; A=23-47.
DR   PDBsum; 1Z64; -.
DR   PDBsum; 2LS9; -.
DR   PDBsum; 6RSG; -.
DR   AlphaFoldDB; P81941; -.
DR   BMRB; P81941; -.
DR   SMR; P81941; -.
DR   EvolutionaryTrace; P81941; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR012515; Antimicrobial12.
DR   Pfam; PF08107; Antimicrobial12; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Lipid-binding; Membrane; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:9115266"
FT   PEPTIDE         23..47
FT                   /note="Pleurocidin"
FT                   /id="PRO_0000000273"
FT   PROPEP          48..68
FT                   /id="PRO_0000000274"
FT   CONFLICT        44..45
FT                   /note="TH -> HT (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           25..42
FT                   /evidence="ECO:0007829|PDB:1Z64"
FT   TURN            43..46
FT                   /evidence="ECO:0007829|PDB:1Z64"
SQ   SEQUENCE   68 AA;  7601 MW;  0601CBAA55C2E59D CRC64;
     MKFTATFLMM AIFVLMVEPG ECGWGSFFKK AAHVGKHVGK AALTHYLGDK QELNKRAVDE
     DPNVIVFE