RAN3_LITCT
ID RAN3_LITCT Reviewed; 32 AA.
AC P82780;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Ranatuerin-3 {ECO:0000303|PubMed:9784389};
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 PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Skin secretion;
RX PubMed=9784389; DOI=10.1006/bbrc.1998.9362;
RA Goraya J., Knoop F.C., Conlon J.M.;
RT "Ranatuerins: antimicrobial peptides isolated from the skin of the American
RT bullfrog, Rana catesbeiana.";
RL Biochem. Biophys. Res. Commun. 250:589-592(1998).
CC -!- FUNCTION: Antibacterial activity against Gram-positive bacterium
CC S.aureus (MIC=60 uM). Shows no detectable hemolytic activity towards
CC human erythrocytes. {ECO:0000269|PubMed:9784389}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9784389}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:9784389}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P82780; -.
DR SMR; P82780; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Disulfide bond; Secreted.
FT PEPTIDE 1..32
FT /note="Ranatuerin-3"
FT /evidence="ECO:0000269|PubMed:9784389"
FT /id="PRO_0000044657"
FT DISULFID 23..28
FT /evidence="ECO:0000305|PubMed:9784389"
SQ SEQUENCE 32 AA; 3417 MW; 5B5C19D80DDBF94B CRC64;
GFLDIINKLG KTFAGHMLDK IKCTIGTCPP SP