ID   OCE1_LEPLB              Reviewed;          22 AA.
AC   C0HKF1; A0A1W2VMZ2;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   25-MAY-2022, entry version 11.
DE   RecName: Full=Ocellatin-LB1 {ECO:0000303|PubMed:28115922};
OS   Leptodactylus labyrinthicus (Labyrinth frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Leptodactylidae; Leptodactylinae;
OC   Leptodactylus.
OX   NCBI_TaxID=326590;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   AMIDATION AT MET-22.
RC   TISSUE=Skin secretion;
RX   PubMed=28115922; DOI=10.1186/s40409-017-0094-y;
RA   Gusmao K.A., Dos Santos D.M., Santos V.M., Cortes M.E., Reis P.V.,
RA   Santos V.L., Pilo-Veloso D., Verly R.M., de Lima M.E., Resende J.M.;
RT   "Ocellatin peptides from the skin secretion of the South American frog
RT   Leptodactylus labyrinthicus (Leptodactylidae): characterization,
RT   antimicrobial activities and membrane interactions.";
RL   J. Venom. Anim. Toxins Incl. Trop. Dis. 23:4-4(2017).
RN   [2] {ECO:0007744|PDB:5U9Q, ECO:0007744|PDB:5U9V, ECO:0007744|PDB:5UA6}
RP   STRUCTURE BY NMR IN PRESENCE OF ANIONIC SDS MICELLES; ZWITTERIONIC DPC
RP   MICELLES AND TFE:H2O SOLUTION.
RX   PubMed=29596881; DOI=10.1016/j.peptides.2018.03.016;
RA   Gomes K.A.G.G., Dos Santos D.M., Santos V.M., Pilo-Veloso D., Mundim H.M.,
RA   Rodrigues L.V., Liao L.M., Verly R.M., de Lima M.E., Resende J.M.;
RT   "NMR structures in different membrane environments of three ocellatin
RT   peptides isolated from Leptodactylus labyrinthicus.";
RL   Peptides 103:72-83(2018).
CC   -!- FUNCTION: Antibacterial peptide that inhibits Gram-negative bacteria
CC       A.actinomycetemcomitans ATCC 29522 (MIC=222.37 uM) and E.coli ATCC
CC       25922 (MIC=114.04 uM). Also has antifungal activity against C.albicans
CC       ATCC 18804 (MIC=233.55 uM) and C.lusitaniae ATCC 56936 (MIC=233.55 uM).
CC       No activity against the Gram-positive bacterium S.aureus ATCC 25923.
CC       Shows virtually no hemolytic activity towards rabbit erythrocytes.
CC       {ECO:0000269|PubMed:28115922}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28115922}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:28115922}.
CC   -!- MASS SPECTROMETRY: Mass=2191.18; Mass_error=0.012; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:28115922};
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=02971";
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DR   PDB; 5U9Q; NMR; -; A=1-22.
DR   PDB; 5U9V; NMR; -; A=1-22.
DR   PDB; 5UA6; NMR; -; A=1-22.
DR   PDBsum; 5U9Q; -.
DR   PDBsum; 5U9V; -.
DR   PDBsum; 5UA6; -.
DR   AlphaFoldDB; C0HKF1; -.
DR   SMR; C0HKF1; -.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IEA:InterPro.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR012518; Antimicrobial15.
DR   Pfam; PF08110; Antimicrobial15; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW   Antimicrobial; Direct protein sequencing; Fungicide; Secreted.
FT   PEPTIDE         1..22
FT                   /note="Ocellatin-LB1"
FT                   /evidence="ECO:0000269|PubMed:28115922"
FT                   /id="PRO_0000439885"
FT   MOD_RES         22
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000269|PubMed:28115922"
FT   HELIX           2..21
FT                   /evidence="ECO:0007829|PDB:5U9Q"
SQ   SEQUENCE   22 AA;  2194 MW;  B8DE570755618F7B CRC64;
     GVVDILKGAA KDIAGHLASK VM