ID   OCE4_LEPOE              Reviewed;          21 AA.
AC   P85090;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Ocellatin-4;
OS   Leptodactylus ocellatus (Argus frog) (Leptodactylus macrosternum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Leptodactylidae; Leptodactylinae;
OC   Leptodactylus.
OX   NCBI_TaxID=928525;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND AMIDATION AT ILE-21.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:17884127};
RX   PubMed=17884127; DOI=10.1016/j.toxicon.2007.07.014;
RA   Nascimento A.C.C., Chapeaurouge A., Perales J., Sebben A., Sousa M.V.,
RA   Fontes W., Castro M.S.;
RT   "Purification, characterization and homology analysis of ocellatin 4, a
RT   cytolytic peptide from the skin secretion of the frog Leptodactylus
RT   ocellatus.";
RL   Toxicon 50:1095-1104(2007).
CC   -!- FUNCTION: Has hemolytic activity against human erythrocytes (HC50=14.3
CC       uM). Has antibacterial activity against the Gram-positive bacterium
CC       S.aureus ATCC 25923 (MIC=64 uM) and the Gram-negative bacterium E.coli
CC       ATCC 25922 (MIC=64 uM). {ECO:0000269|PubMed:17884127}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17884127}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC       {ECO:0000269|PubMed:17884127}.
CC   -!- MASS SPECTROMETRY: Mass=2274.24; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:17884127};
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=00894";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P85090; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Hemolysis; Secreted.
FT   PEPTIDE         1..21
FT                   /note="Ocellatin-4"
FT                   /evidence="ECO:0000269|PubMed:17884127"
FT                   /id="PRO_0000306195"
FT   MOD_RES         21
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:17884127"
SQ   SEQUENCE   21 AA;  2276 MW;  76693115D773569F CRC64;
     GLLDFVTGVG KDIFAQLIKQ I