ID   MORO_MORCH              Reviewed;          79 AA.
AC   Q8UUG2;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Moronecidin {ECO:0000303|PubMed:11739390};
DE   AltName: Full=Piscidin-2 {ECO:0000303|PubMed:15193922};
DE   Flags: Precursor;
OS   Morone chrysops (White bass) (Perca chrysops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Morone.
OX   NCBI_TaxID=46259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 23-41,
RP   FUNCTION, SYNTHESIS OF 23-44, AMIDATION AT GLY-44, MASS SPECTROMETRY, AND
RP   TISSUE SPECIFICITY.
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   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).
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 (PubMed:11739390). Rapidly inactivates both channel catfish
CC       herpesvirus (ED(50)=4 uM) and frog virus 3 (ED(50)=13 uM) over a wide
CC       temperature range (PubMed:15193922). Seems to disrupt the membranes by
CC       adopting an alpha helical conformation (PubMed:11739390).
CC       {ECO:0000269|PubMed:11739390, ECO:0000269|PubMed:15193922}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in gill, skin, intestine, spleen,
CC       anterior kidney, and blood cells. {ECO:0000269|PubMed:11739390}.
CC   -!- MASS SPECTROMETRY: Mass=2543; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11739390};
CC   -!- SIMILARITY: Belongs to the pleurocidin family. {ECO:0000305}.
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DR   EMBL; AF332621; AAL40409.1; -; mRNA.
DR   EMBL; AF394243; AAL57318.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8UUG2; -.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR012515; Antimicrobial12.
DR   Pfam; PF08107; Antimicrobial12; 1.
PE   1: Evidence at protein level;
KW   Amidation; Antibiotic; Antimicrobial; Antiviral protein;
KW   Direct protein sequencing; Fungicide; Immunity; Innate immunity; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:11739390"
FT   PEPTIDE         23..44
FT                   /note="Moronecidin"
FT                   /evidence="ECO:0000269|PubMed:11739390"
FT                   /id="PRO_0000000283"
FT   PROPEP          47..79
FT                   /id="PRO_0000000284"
FT   REGION          45..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         44
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:11739390"
SQ   SEQUENCE   79 AA;  9106 MW;  B6F32481C4200EEB CRC64;
     MKCATLSLVL SMVVLMAEPG DAFFHHIFRG IVHVGKTIHK LVTGGKAEQD QQDQQYQQDQ
     QDQQAQQYQR FNRERAAFD