OCE1_LEPLD
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