ID   RACYE_PELLE             Reviewed;          17 AA.
AC   P83663;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Ranacyclin-E;
OS   Pelophylax lessonae (Pool frog) (Rana lessonae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=45623 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DISULFIDE BOND, AND AMIDATION AT LYS-17.
RC   TISSUE=Skin {ECO:0000269|PubMed:14636071};
RX   PubMed=14636071; DOI=10.1021/bi034521l;
RA   Mangoni M.L., Papo N., Mignogna G., Andreu D., Shai Y., Barra D.,
RA   Simmaco M.;
RT   "Ranacyclins, a new family of short cyclic antimicrobial peptides:
RT   biological function, mode of action and parameters involved in target
RT   specificity.";
RL   Biochemistry 42:14023-14035(2003).
CC   -!- FUNCTION: Has antibacterial activity against Gram-positive bacteria
CC       B.megaterium Bm11, S.lentus and M.luteus, Gram-negative bacteria
CC       Y.pseudotuberculosis YP III and P.syringae pv tabaci, and antifungal
CC       activity against C.tropicalis, C.guiller-mondii and P.nicotianae
CC       spores. Has hemolytic activity. The mature peptide inserts into the
CC       hydrophobic core of the bacterial cell membrane and increases
CC       permeability without disrupting membrane integrity. Probably binds to
CC       the outer membrane surface before aggregating to form transmembrane
CC       pores. {ECO:0000269|PubMed:14636071, ECO:0000303|PubMed:14636071}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14636071}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin granular glands.
CC       {ECO:0000269|PubMed:14636071}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P83663; -.
DR   BMRB; P83663; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR032019; Frog_antimicrobial_Ranidae.
DR   Pfam; PF16048; Antimicrobial23; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Hemolysis; Secreted.
FT   PEPTIDE         1..17
FT                   /note="Ranacyclin-E"
FT                   /id="PRO_0000043555"
FT   MOD_RES         17
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:14636071"
FT   DISULFID        6..16
FT                   /evidence="ECO:0000269|PubMed:14636071"
SQ   SEQUENCE   17 AA;  1906 MW;  FAAF70FAFFABA405 CRC64;
     SAPRGCWTKS YPPKPCK