ID   OCE1_LEPFX              Reviewed;          25 AA.
AC   P0DQJ8;
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-F1 {ECO:0000250|UniProtKB:C0HKF0};
DE            Short=OF1 {ECO:0000250|UniProtKB:C0HKF0};
DE   AltName: Full=Fallaxin {ECO:0000303|PubMed:15544856};
DE   Contains:
DE     RecName: Full=Fallaxin(1-22) {ECO:0000303|PubMed:15544856};
DE     AltName: Full=Ocellatin-LB1 {ECO:0000250|UniProtKB:C0HKF1};
OS   Leptodactylus fallax (Mountain chicken frog) (Leptodactylus dominicensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Leptodactylidae; Leptodactylinae;
OC   Leptodactylus.
OX   NCBI_TaxID=375434;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AMIDATION AT LEU-25, MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=15544856; DOI=10.1016/j.regpep.2004.07.013;
RA   Rollins-Smith L.A., King J.D., Nielsen P.F., Sonnevend A., Conlon J.M.;
RT   "An antimicrobial peptide from the skin secretions of the mountain chicken
RT   frog Leptodactylus fallax (Anura:Leptodactylidae).";
RL   Regul. Pept. 124:173-178(2005).
CC   -!- FUNCTION: [Ocellatin-F1]: Antibacterial peptide that inhibits reference
CC       strains of both Gram-negative bacteria (E.coli, P.aeruginosa,
CC       E.cloacae, K.pneumoniae, and A.actinomycetemcomitans) and Gram-positive
CC       bacteria (S.aureus) with relatively low potencies (MIC=25-400 uM) (By
CC       similarity) (PubMed:15544856). Shows antifungal activity against
CC       C.lusitaniae (MIC=50.25 uM), but no activity against C.albicans (By
CC       similarity) (PubMed:15544856). In the presence of an alkaloid
CC       (bufotenine), inhibits cellular infection by the rabies virus (By
CC       similarity). The peptide shows very low hemolytic activity against
CC       rabbit erythrocytes (By similarity) (PubMed:15544856). The low
CC       amphipathicity of alpha-helices demonstrated by wheel projection as
CC       well as the low cationicity may explain the low antibacterial and
CC       hemolytic potencies (Probable). {ECO:0000250|UniProtKB:C0HKF0,
CC       ECO:0000269|PubMed:15544856, ECO:0000305|PubMed:15544856}.
CC   -!- FUNCTION: [Fallaxin(1-22)]: Does not show activity against the
CC       microorganisms tested. {ECO:0000269|PubMed:15544856}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15544856}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:15544856}.
CC   -!- MASS SPECTROMETRY: [Ocellatin-F1]: Mass=2546.6; Method=MALDI;
CC       Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:15544856};
CC   -!- MASS SPECTROMETRY: [Fallaxin(1-22)]: Mass=2193; Method=MALDI;
CC       Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:15544856};
CC   -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC       that of Ocellatin-F1 from Leptodactylus labyrinthicus (AC C0HKF0). The
CC       cross-references to PDB can be found in this entry (AC C0HKF0).
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   AlphaFoldDB; P0DQJ8; -.
DR   SMR; P0DQJ8; -.
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   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Antiviral protein; Direct protein sequencing; Fungicide; Secreted.
FT   PEPTIDE         1..25
FT                   /note="Ocellatin-F1"
FT                   /evidence="ECO:0000269|PubMed:15544856"
FT                   /id="PRO_0000449460"
FT   PEPTIDE         1..22
FT                   /note="Fallaxin(1-22)"
FT                   /evidence="ECO:0000269|PubMed:15544856"
FT                   /id="PRO_0000449461"
FT   MOD_RES         25
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:15544856"
SQ   SEQUENCE   25 AA;  2549 MW;  3C42EAC8DE570755 CRC64;
     GVVDILKGAA KDIAGHLASK VMNKL