ID   OCE1_LEPOE              Reviewed;          25 AA.
AC   P83951;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Ocellatin-1;
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]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND AMIDATION AT VAL-25.
RC   TISSUE=Skin secretion;
RX   PubMed=15648972; DOI=10.1007/s10930-004-7877-z;
RA   Nascimento A.C.C., Zanotta L.C., Kyaw C.M., Schwartz E.N.F., Schwartz C.A.,
RA   Sebben A., Sousa M.V., Fontes W., Castro M.S.;
RT   "Ocellatins: new antimicrobial peptides from the skin secretion of the
RT   South American frog Leptodactylus ocellatus (Anura: Leptodactylidae).";
RL   Protein J. 23:501-508(2004).
CC   -!- FUNCTION: Has hemolytic activity against human erythrocytes and
CC       antibacterial activity against the Gram-negative bacterium E.coli.
CC       {ECO:0000269|PubMed:15648972, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15648972,
CC       ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC       {ECO:0000269|PubMed:15648972, ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=2559.19; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15648972, ECO:0000305};
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=00543";
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DR   AlphaFoldDB; P83951; -.
DR   SMR; P83951; -.
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:0044179; P:hemolysis in another organism; 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; Cytolysis;
KW   Direct protein sequencing; Hemolysis; Secreted.
FT   PEPTIDE         1..25
FT                   /note="Ocellatin-1"
FT                   /id="PRO_0000043815"
FT   MOD_RES         25
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:15648972"
SQ   SEQUENCE   25 AA;  2560 MW;  F982E21B91961A8D CRC64;
     GVVDILKGAG KDLLAHLVGK ISEKV