ID   MORO_MORSA              Reviewed;          79 AA.
AC   Q8UUG0;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Moronecidin {ECO:0000303|PubMed:11739390};
DE   AltName: Full=Piscidin-1 {ECO:0000303|PubMed:11713517, ECO:0000303|PubMed:17253775};
DE   Flags: Precursor;
OS   Morone saxatilis (Striped bass) (Perca saxatilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Morone.
OX   NCBI_TaxID=34816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 23-41, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Gill, and Skin;
RX   PubMed=11739390; DOI=10.1074/jbc.m109173200;
RA   Lauth X., Shike H., Burns J.C., Westerman M.E., Ostland V.E.,
RA   Carlberg J.M., Van Olst J.C., Nizet V., Taylor S.W., Shimizu C., Bulet P.;
RT   "Discovery and characterization of two isoforms of moronecidin, a novel
RT   antimicrobial peptide from hybrid striped bass.";
RL   J. Biol. Chem. 277:5030-5039(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-44, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=11713517; DOI=10.1038/35104690;
RA   Silphaduang U., Noga E.J.;
RT   "Peptide antibiotics in mast cells of fish.";
RL   Nature 414:268-269(2001).
RN   [3]
RP   ERRATUM.
RA   Silphaduang U., Noga E.J.;
RL   Nature 414:710-710(2001).
RN   [4]
RP   FUNCTION AS ANTIVIRAL PEPTIDE.
RX   PubMed=15193922; DOI=10.1016/j.virol.2004.02.029;
RA   Chinchar V.G., Bryan L., Silphadaung U., Noga E., Wade D.,
RA   Rollins-Smith L.;
RT   "Inactivation of viruses infecting ectothermic animals by amphibian and
RT   piscine antimicrobial peptides.";
RL   Virology 323:268-275(2004).
RN   [5]
RP   STRUCTURE BY NMR OF 23-44, AMIDATION AT GLY-44, AND FUNCTION.
RX   PubMed=17253775; DOI=10.1021/bi0620297;
RA   Campagna S., Saint N., Molle G., Aumelas A.;
RT   "Structure and mechanism of action of the antimicrobial peptide piscidin.";
RL   Biochemistry 46:1771-1778(2007).
CC   -!- FUNCTION: Antimicrobial peptide with broad-spectrum activity against
CC       Gram-positive and Gram-negative bacteria as well as against a variety
CC       of fungi. Rapidly inactivates channel catfish herpesvirus (ED(50)=4 uM)
CC       and frog virus 3 (ED(50)=13 uM) over a wide temperature range
CC       (PubMed:15193922). Seems to disrupt the membranes by adopting an alpha
CC       helical conformation and forming toroidal pores. Has hemolytic
CC       activity. {ECO:0000269|PubMed:11713517, ECO:0000269|PubMed:15193922,
CC       ECO:0000269|PubMed:17253775}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11713517}.
CC   -!- TISSUE SPECIFICITY: Expressed in mast cells in gill, skin and gut, and
CC       in lining blood vessels in the viscera. Also in intestine, spleen,
CC       anterior kidney, and blood cells. {ECO:0000269|PubMed:11713517}.
CC   -!- MASS SPECTROMETRY: Mass=2571; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11739390};
CC   -!- SIMILARITY: Belongs to the pleurocidin family. {ECO:0000305}.
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DR   EMBL; AF385583; AAL49496.1; -; mRNA.
DR   EMBL; AF394244; AAL57319.1; -; Genomic_DNA.
DR   PDB; 2JOS; NMR; -; A=23-44.
DR   PDB; 2MCU; NMR; -; A=23-44.
DR   PDB; 2MCV; NMR; -; A=23-44.
DR   PDB; 2OJM; NMR; -; A=23-44.
DR   PDB; 6PF0; NMR; -; A=23-44.
DR   PDBsum; 2JOS; -.
DR   PDBsum; 2MCU; -.
DR   PDBsum; 2MCV; -.
DR   PDBsum; 2OJM; -.
DR   PDBsum; 6PF0; -.
DR   AlphaFoldDB; Q8UUG0; -.
DR   BMRB; Q8UUG0; -.
DR   SMR; Q8UUG0; -.
DR   EvolutionaryTrace; Q8UUG0; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR012515; Antimicrobial12.
DR   Pfam; PF08107; Antimicrobial12; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Fungicide; Hemolysis; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:11713517,
FT                   ECO:0000269|PubMed:11739390"
FT   PEPTIDE         23..44
FT                   /note="Moronecidin"
FT                   /evidence="ECO:0000269|PubMed:11713517"
FT                   /id="PRO_0000000285"
FT   PROPEP          47..79
FT                   /evidence="ECO:0000269|PubMed:11713517"
FT                   /id="PRO_0000000286"
FT   REGION          45..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         44
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:17253775"
FT   STRAND          25..30
FT                   /evidence="ECO:0007829|PDB:2JOS"
FT   HELIX           31..41
FT                   /evidence="ECO:0007829|PDB:2JOS"
SQ   SEQUENCE   79 AA;  9222 MW;  C9DF13E1D4FA7EFD CRC64;
     MKCATLFLVL SMVVLMAEPG DAFFHHIFRG IVHVGKTIHR LVTGGKAEQD QQDQQYQQEQ
     QEQQAQQYQR FNRERAAFD