ID   OCE4_LEPPU              Reviewed;          66 AA.
AC   C0HJZ9;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Ocellatin-PT4 {ECO:0000303|PubMed:26107622};
DE   Flags: Precursor;
OS   Leptodactylus pustulatus (Ceara white-lipped frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Leptodactylidae; Leptodactylinae;
OC   Leptodactylus.
OX   NCBI_TaxID=1349691;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-66, FUNCTION,
RP   SUBCELLULAR LOCATION, MASS SPECTROMETRY, AMIDATION AT VAL-66, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:26107622};
RX   PubMed=26107622; DOI=10.1021/np500907t;
RA   Marani M.M., Dourado F.S., Quelemes P.V., de Araujo A.R., Perfeito M.L.,
RA   Barbosa E.A., Veras L.M., Coelho A.L., Andrade E.B., Eaton P., Longo J.P.,
RA   Azevedo R.B., Delerue-Matos C., Leite J.R.;
RT   "Characterization and biological activities of ocellatin peptides from the
RT   skin secretion of the frog Leptodactylus pustulatus.";
RL   J. Nat. Prod. 78:1495-1504(2015).
CC   -!- FUNCTION: Has antibacterial activity against Gram-negative bacteria
CC       E.coli ATCC 25922 (MIC=80 uM), K.pneumoniae ATCC 700603 (MIC=310 uM)
CC       and S.choleraesuis ATCC 14028 (MIC=310 uM). Shows no hemolytic activity
CC       and no cytotoxicity. {ECO:0000269|PubMed:26107622}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26107622}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:26107622}.
CC   -!- MASS SPECTROMETRY: Mass=2593.46; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:26107622};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Ocellatin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=02598";
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DR   AlphaFoldDB; C0HJZ9; -.
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:0019836; P:hemolysis by symbiont of host erythrocytes; IEA:InterPro.
DR   InterPro; IPR012518; Antimicrobial15.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
DR   Pfam; PF08110; Antimicrobial15; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..39
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436214"
FT   PEPTIDE         42..66
FT                   /note="Ocellatin-PT4"
FT                   /evidence="ECO:0000269|PubMed:26107622"
FT                   /id="PRO_0000436215"
FT   MOD_RES         66
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:26107622"
SQ   SEQUENCE   66 AA;  7398 MW;  8C5B463677C6C2F3 CRC64;
     MAFLKKSLFL VLFLGLVSLS ICDEEKRQDE DDDDDDDEEK RGVFDIIKGA GKQLIAHAMG
     KIAEKV