ID   OCE2_LEPLB              Reviewed;          23 AA.
AC   C0HKF2; A0A1W2VMY9;
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-LB2 {ECO:0000303|PubMed:28115922};
DE   AltName: Full=Des-Lys24-Leu25-ocellatin-F1 {ECO:0000303|PubMed:26635873};
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, 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 ASN-23.
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:5U9R, ECO:0007744|PDB:5U9X, ECO:0007744|PDB:5UA7}
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 the Gram-negative
CC       bacterium A.actinomycetemcomitans ATCC 29522 (MIC=210 uM). No activity
CC       against the bacteria E.coli ATCC 25922 and S.aureus ATCC 25923, or the
CC       fungi C.albicans ATCC 18804 and C.lusitaniae ATCC 56936. Does not show
CC       hemolytic activity towards rabbit erythrocytes.
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=2192.8; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:26635873};
CC   -!- MASS SPECTROMETRY: Mass=2304.95; 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; 5U9R; NMR; -; A=1-23.
DR   PDB; 5U9X; NMR; -; A=1-23.
DR   PDB; 5UA7; NMR; -; A=1-23.
DR   PDBsum; 5U9R; -.
DR   PDBsum; 5U9X; -.
DR   PDBsum; 5UA7; -.
DR   AlphaFoldDB; C0HKF2; -.
DR   SMR; C0HKF2; -.
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   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; Secreted.
FT   PEPTIDE         1..23
FT                   /note="Ocellatin-LB2"
FT                   /evidence="ECO:0000269|PubMed:26635873,
FT                   ECO:0000269|PubMed:28115922"
FT                   /id="PRO_0000439886"
FT   MOD_RES         23
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:28115922"
FT   HELIX           2..22
FT                   /evidence="ECO:0007829|PDB:5U9R"
SQ   SEQUENCE   23 AA;  2308 MW;  2AC8DE570755618F CRC64;
     GVVDILKGAA KDIAGHLASK VMN