OCE3_LEPPU
ID OCE3_LEPPU Reviewed; 66 AA.
AC C0HJZ8;
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-PT3 {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 bacterium
CC E.coli ATCC 25922 (MIC=320 uM) but not against S.pneumoniae ATCC
CC 700603, S.choleraesuis ATCC 14028 or Gram-positive bacterium S.aureus
CC ATCC 29313. Shows no hemolytic activity and no cytotoxicity.
CC {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=2528.53; 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=02748";
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DR AlphaFoldDB; C0HJZ8; -.
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_0000436212"
FT PEPTIDE 42..66
FT /note="Ocellatin-PT3"
FT /evidence="ECO:0000269|PubMed:26107622"
FT /id="PRO_0000436213"
FT MOD_RES 66
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:26107622"
SQ SEQUENCE 66 AA; 7333 MW; 975B463670A6C82E CRC64;
MAFLKKSLFL VLFLGLVSLS ICDEEKRQDE DDDDDDDEEK RGVIDIIKGA GKDLIAHAIG
KLAEKV