OCE5_LEPOE
ID OCE5_LEPOE Reviewed; 17 AA.
AC P85443;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Ocellatin-5;
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] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AMIDATION AT LEU-17, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion {ECO:0000269|Ref.1};
RA Nascimento A.C.C.;
RT "Cytolytic peptides and proteases from the skin secretion of the frog
RT Leptodactylus ocellatus).";
RL Thesis (2007), University of Brasilia, Brazil.
CC -!- FUNCTION: Has hemolytic and antibacterial activities.
CC {ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC {ECO:0000269|Ref.1}.
CC -!- MASS SPECTROMETRY: Mass=1729.01; Method=MALDI;
CC Evidence={ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Ocellatin subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P85443; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW Direct protein sequencing; Hemolysis; Secreted.
FT PEPTIDE 1..17
FT /note="Ocellatin-5"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000324673"
FT MOD_RES 17
FT /note="Leucine amide"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 17 AA; 1730 MW; 15ED5C4BEDA2791A CRC64;
GLLDFLKAAG KGLVTNL