ID   RLXN_LITCT              Reviewed;          66 AA.
AC   P39084;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Ranalexin;
DE   Flags: Precursor;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 47-66.
RC   TISSUE=Skin, and Skin secretion;
RX   PubMed=8144672; DOI=10.1016/s0021-9258(17)34136-4;
RA   Clark D.P., Durell S., Maloy W.L., Zasloff M.;
RT   "Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana)
RT   skin, structurally related to the bacterial antibiotic, polymyxin.";
RL   J. Biol. Chem. 269:10849-10855(1994).
RN   [2]
RP   STRUCTURE BY NMR OF RANALEXIN.
RX   PubMed=9578480; DOI=10.1046/j.1432-1327.1998.2530221.x;
RA   Vignal E., Chavanieu A., Roch P., Chiche L., Grassy G., Calas B.,
RA   Aumelas A.;
RT   "Solution structure of the antimicrobial peptide ranalexin and a study of
RT   its interaction with perdeuterated dodecylphosphocholine micelles.";
RL   Eur. J. Biochem. 253:221-228(1998).
CC   -!- FUNCTION: Potent microbicidal activity, active against S.aureus and
CC       E.coli. It acts as well as a membrane-disruptive agent at higher
CC       concentrations.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC   -!- DEVELOPMENTAL STAGE: Expression starts at metamorphosis and continues
CC       into adulthood.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   EMBL; S69903; AAB30394.1; -; mRNA.
DR   PIR; A53744; A53744.
DR   AlphaFoldDB; P39084; -.
DR   GO; GO:0005576; C:extracellular region; 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; IPR012520; Antimicrobial_frog_1.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF08018; Antimicrobial_1; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; Hemolysis; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..44
FT                   /note="Small acidic peptide"
FT                   /id="PRO_0000003465"
FT   PEPTIDE         47..66
FT                   /note="Ranalexin"
FT                   /evidence="ECO:0000269|PubMed:8144672"
FT                   /id="PRO_0000003466"
FT   DISULFID        60..66
FT                   /evidence="ECO:0000269|PubMed:8144672"
SQ   SEQUENCE   66 AA;  7615 MW;  096B8AD58A3C8513 CRC64;
     MFTLKKSLLL LFFLGTINLS LCEEERNAEE ERRDNPDERD VEVEKRFLGG LIKIVPAMIC
     AVTKKC