ID   OCE1_LEPPE              Reviewed;          25 AA.
AC   P0DQJ7;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Ocellatin-P1 {ECO:0000305};
DE   AltName: Full=Pentadactylin {ECO:0000303|PubMed:16236555};
OS   Leptodactylus pentadactylus (Smokey jungle frog) (Rana pentadactyla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Leptodactylidae; Leptodactylinae;
OC   Leptodactylus.
OX   NCBI_TaxID=47564;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AMIDATION AT LEU-25, MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, AND SYNTHESIS.
RC   TISSUE=Skin secretion;
RX   PubMed=16236555; DOI=10.1016/j.cbpc.2005.09.002;
RA   King J.D., Al-Ghaferi N., Abraham B., Sonnevend A., Leprince J.,
RA   Nielsen P.F., Conlon J.M.;
RT   "Pentadactylin: an antimicrobial peptide from the skin secretions of the
RT   South American bullfrog Leptodactylus pentadactylus.";
RL   Comp. Biochem. Physiol. 141:393-397(2005).
CC   -!- FUNCTION: Antibacterial peptide that ihibits reference strains of both
CC       Gram-negative bacteria (E.coli, E.cloacae, K.pneumoniae, P.aeruginosa)
CC       and Gram-positive bacteria (S.aureus, S.epidermidis, E.faecalis,
CC       Streptococcus group B) with relatively low potencies (MIC=25-200 uM).
CC       The peptide shows very low hemolytic activity against human
CC       erythrocytes. Wheel projection demonstrates the amphipathicity of the
CC       alpha-helices is low which may explain the low antibacterial potency.
CC       {ECO:0000269|PubMed:16236555}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16236555}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:16236555}.
CC   -!- MASS SPECTROMETRY: Mass=2540.5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16236555};
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=00540";
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DR   AlphaFoldDB; P0DQJ7; -.
DR   SMR; P0DQJ7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..25
FT                   /note="Ocellatin-P1"
FT                   /id="PRO_0000449459"
FT   MOD_RES         25
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:16236555"
SQ   SEQUENCE   25 AA;  2543 MW;  C7E5528A5826859F CRC64;
     GLLDTLKGAA KNVVGSLASK VMEKL