ID   OCEF1_LEPLB             Reviewed;          25 AA.
AC   C0HKF0; A0A1W2VMZ4;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Ocellatin-F1 {ECO:0000303|PubMed:26635873, ECO:0000303|PubMed:28115922};
DE            Short=OF1 {ECO:0000303|PubMed:26635873, ECO:0000303|PubMed:28115922};
DE   AltName: Full=Fallaxin {ECO:0000250|UniProtKB:P0DQJ8};
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, AND MASS SPECTROMETRY.
RC   TISSUE=Skin secretion;
RX   PubMed=26635873; DOI=10.1186/s40409-015-0048-1;
RA   Cunha Neto Rdos S., Vigerelli H., Jared C., Antoniazzi M.M., Chaves L.B.,
RA   da Silva Ade C., Melo R.L., Sciani J.M., Pimenta D.C.;
RT   "Synergic effects between ocellatin-F1 and bufotenine on the inhibition of
RT   BHK-21 cellular infection by the rabies virus.";
RL   J. Venom. Anim. Toxins Incl. Trop. Dis. 21:50-50(2015).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   AMIDATION AT LEU-25.
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   [3] {ECO:0007744|PDB:5U9S, ECO:0007744|PDB:5U9Y, ECO:0007744|PDB:5UA8}
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 reference strains of both
CC       Gram-negative bacteria (E.coli, P.aeruginosa, E.cloacae, K.pneumoniae,
CC       and A.actinomycetemcomitans) and Gram-positive bacteria (S.aureus) with
CC       relatively low potencies (MIC=25-400 uM) (PubMed:28115922) (By
CC       similarity). Shows antifungal activity against C.lusitaniae (MIC=50.25
CC       uM), but no activity against C.albicans (PubMed:28115922). In the
CC       presence of an alkaloid (bufotenine), inhibits cellular infection by
CC       the rabies virus (PubMed:26635873). The peptide shows very low
CC       hemolytic activity against rabbit erythrocytes (PubMed:28115922) (By
CC       similarity). The low amphipathicity of alpha-helices demonstrated by
CC       wheel projection as well as the low cationicity may explain the low
CC       antibacterial and hemolytic potencies (By similarity).
CC       {ECO:0000250|UniProtKB:P0DQJ8, ECO:0000269|PubMed:26635873,
CC       ECO:0000269|PubMed:28115922}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26635873,
CC       ECO:0000269|PubMed:28115922}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:26635873, ECO:0000305|PubMed:28115922}.
CC   -!- MASS SPECTROMETRY: Mass=2547.98; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:26635873};
CC   -!- MASS SPECTROMETRY: Mass=2546.52; Mass_error=0.012; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:28115922};
CC   -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC       that of Ocellatin-F1 from Leptodactylus fallax (AC P0DQJ8).
CC       {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=00533";
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DR   PDB; 5U9S; NMR; -; A=1-25.
DR   PDB; 5U9Y; NMR; -; A=1-24.
DR   PDB; 5UA8; NMR; -; A=1-25.
DR   PDBsum; 5U9S; -.
DR   PDBsum; 5U9Y; -.
DR   PDBsum; 5UA8; -.
DR   AlphaFoldDB; C0HKF0; -.
DR   SMR; C0HKF0; -.
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   GO; GO:0050688; P:regulation of defense response to virus; 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; Antiviral protein; Direct protein sequencing; Fungicide;
KW   Secreted.
FT   PEPTIDE         1..25
FT                   /note="Ocellatin-F1"
FT                   /evidence="ECO:0000269|PubMed:26635873,
FT                   ECO:0000269|PubMed:28115922"
FT                   /id="PRO_0000439884"
FT   MOD_RES         25
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:28115922"
FT   HELIX           3..24
FT                   /evidence="ECO:0007829|PDB:5U9S"
SQ   SEQUENCE   25 AA;  2549 MW;  3C42EAC8DE570755 CRC64;
     GVVDILKGAA KDIAGHLASK VMNKL