ID   OCE1_LEPLD              Reviewed;          25 AA.
AC   P0DQL0;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Ocellatin-L1 {ECO:0000303|PubMed:19428765};
OS   Leptodactylus laticeps (Santa Fe frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Leptodactylidae; Leptodactylinae;
OC   Leptodactylus.
OX   NCBI_TaxID=1615745;
RN   [1]
RP   FUNCTION, SUBCELLULAR LOCATION, AND AMIDATION AT LEU-25.
RX   PubMed=16712520; DOI=10.2174/092986606775974410;
RA   Conlon J.M., Al-Ghaferi N., Abraham B., Sonnevend A., King J.D.,
RA   Nielsen P.F.;
RT   "Purification and properties of laticeptin, an antimicrobial peptide from
RT   skin secretions of the South American frog Leptodactylus laticeps.";
RL   Protein Pept. Lett. 13:411-415(2006).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=19428765; DOI=10.1016/j.peptides.2009.01.008;
RA   Conlon J.M., Abdel-Wahab Y.H., Flatt P.R., Leprince J., Vaudry H.,
RA   Jouenne T., Condamine E.;
RT   "A glycine-leucine-rich peptide structurally related to the plasticins from
RT   skin secretions of the frog Leptodactylus laticeps (Leptodactylidae).";
RL   Peptides 30:888-892(2009).
CC   -!- FUNCTION: Antimicrobial peptide with activity against Gram-negative
CC       bacteria but without activity against Gram-positive bacteria
CC       (PubMed:16712520). Shows a low activity in stimulating insulin release
CC       from rat BRIN-BD11 beta cells, and acts without loss of integrity of
CC       the plasma membrane (By similarity). Has very low hemolytic activity
CC       (PubMed:16712520). Shows weak amphipathicity in its alpha-helical
CC       conformation (PubMed:16712520). {ECO:0000250|UniProtKB:P0DQL1,
CC       ECO:0000269|PubMed:16712520}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16712520}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:16712520}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Ocellatin subfamily. {ECO:0000305}.
CC   -!- CAUTION: Ocellatin-L1 may be Ocellatin-L2 without a Asn-23 deamination.
CC       Since both peptides do not have the same antibacterial activity, they
CC       are kept in two separate entries. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=01409";
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DR   AlphaFoldDB; P0DQL0; -.
DR   SMR; P0DQL0; -.
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   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR012518; Antimicrobial15.
DR   Pfam; PF08110; Antimicrobial15; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Immunity;
KW   Innate immunity; Secreted.
FT   PEPTIDE         1..25
FT                   /note="Ocellatin-L1"
FT                   /evidence="ECO:0000269|PubMed:16712520"
FT                   /id="PRO_0000449665"
FT   MOD_RES         25
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:16712520"
SQ   SEQUENCE   25 AA;  2563 MW;  3C42EAC8DA060345 CRC64;
     GVVDILKGAA KDLAGHLATK VMNKL