MORO_PTEVL
ID MORO_PTEVL Reviewed; 66 AA.
AC P0DUJ5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 1.
DT 25-MAY-2022, entry version 3.
DE RecName: Full=Pteroicidin-alpha {ECO:0000303|PubMed:29108968};
DE Short=Alpha-Pte-CONH2 {ECO:0000303|PubMed:29108968};
DE Short=Alpha-Pte-COOH {ECO:0000303|PubMed:29108968};
DE AltName: Full=Piscidin-like peptide {ECO:0000303|PubMed:29108968};
DE Flags: Precursor;
OS Pterois volitans (Red lionfish) (Gasterosteus volitans).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Scorpaenoidei; Scorpaenidae; Pteroinae; Pterois.
OX NCBI_TaxID=185886;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-66, SUBCELLULAR
RP LOCATION, AMIDATION AT ARG-43, MASS SPECTROMETRY, AND SYNTHESIS OF 23-66.
RC TISSUE=Venom;
RX PubMed=29108968; DOI=10.1016/j.fsi.2017.11.003;
RA Houyvet B., Bouchon-Navaro Y., Bouchon C., Goux D., Bernay B., Corre E.,
RA Zatylny-Gaudin C.;
RT "Identification of a moronecidin-like antimicrobial peptide in the venomous
RT fish Pterois volitans: Functional and structural study of pteroicidin-
RT alpha.";
RL Fish Shellfish Immunol. 72:318-324(2018).
CC -!- FUNCTION: The amidated peptide is bactericidal on human pathogens like
CC S.aureus or E.coli, as well as on the fish pathogen A.salmonicida
CC (PubMed:29108968). May also be active against a variety of fungi (By
CC similarity). It can kill bacteria in less than 30 minutes (S.aureus)
CC and 120 minutes (V.vulnificus) (PubMed:29108968). It induces hemolysis
CC of erythrocytes from human and fishes (sea bass and lesser-spotted
CC dogfish) (PubMed:29108968). {ECO:0000250|UniProtKB:Q8UUG2,
CC ECO:0000269|PubMed:29108968}.
CC -!- FUNCTION: The non-amidated peptide only inhibits growth of human
CC pathogens like S.aureus or E.coli, and the fish pathogen A.salmonicida.
CC Induces hemolysis of erythrocytes from human and fishes (sea bass and
CC lesser-spotted dogfish). {ECO:0000269|PubMed:29108968}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29108968}.
CC -!- TISSUE SPECIFICITY: Expressed in gill, skin, intestine, spleen,
CC anterior kidney, and blood cells. {ECO:0000305|PubMed:29108968}.
CC -!- PTM: This peptide exists in N-terminally amidated and non-amidated
CC forms. The amidated form is more active and has a greater alpha-helix
CC content than the non-amidated form. {ECO:0000269|PubMed:29108968}.
CC -!- MASS SPECTROMETRY: Mass=2408.22; Method=MALDI; Note=Amidated form.;
CC Evidence={ECO:0000269|PubMed:29108968};
CC -!- MASS SPECTROMETRY: Mass=2409.09; Method=MALDI; Note=Non-amidated form.;
CC Evidence={ECO:0000269|PubMed:29108968};
CC -!- SIMILARITY: Belongs to the pleurocidin family. {ECO:0000305}.
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DR AlphaFoldDB; P0DUJ5; -.
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 InterPro; IPR012515; Antimicrobial12.
DR Pfam; PF08107; Antimicrobial12; 1.
PE 1: Evidence at protein level;
KW Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; Fungicide;
KW Immunity; Innate immunity; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:29108968"
FT PEPTIDE 23..43
FT /note="Pteroicidin-alpha"
FT /evidence="ECO:0000269|PubMed:29108968"
FT /id="PRO_0000452481"
FT PROPEP 44..66
FT /evidence="ECO:0000269|PubMed:29108968"
FT /id="PRO_0000452482"
FT MOD_RES 43
FT /note="Arginine amide; partial"
FT /evidence="ECO:0000303|PubMed:29108968"
SQ SEQUENCE 66 AA; 7508 MW; DC59E1D2936BFEA2 CRC64;
MKCIALFLVL SMVVLMAEPG EAFIHHIIGG LFHVGKSIHD LIRGKNRDMA EQQELERAFD
RERAFA