ID RN2B_LITSE Reviewed; 28 AA. AC P85058; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 14-DEC-2022, entry version 26. DE RecName: Full=Ranatuerin-2SEb {ECO:0000303|PubMed:16386333}; OS Lithobates sevosus (Dusky gopher frog) (Rana sevosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates. OX NCBI_TaxID=299683; RN [1] {ECO:0000305} RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP MASS SPECTROMETRY. RC TISSUE=Skin secretion {ECO:0000269|PubMed:16386333}; RX PubMed=16386333; DOI=10.1016/j.peptides.2005.11.021; RA Graham C., Richter S.C., McClean S., O'Kane E., Flatt P.R., Shaw C.; RT "Histamine-releasing and antimicrobial peptides from the skin secretions of RT the dusky gopher frog, Rana sevosa."; RL Peptides 27:1313-1319(2006). CC -!- FUNCTION: Mast cell degranulating peptide. Causes histamine release CC from rat peritoneal mast cells in vitro. Has antibacterial activity CC against the Gram-negative bacterium E.coli K12 and Gram-positive CC bacterium M.luteus NCT C2665. {ECO:0000269|PubMed:16386333}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16386333}. CC -!- TISSUE SPECIFICITY: Expressed by the skin glands. CC {ECO:0000269|PubMed:16386333}. CC -!- MASS SPECTROMETRY: Mass=2948; Method=MALDI; CC Evidence={ECO:0000269|PubMed:16386333}; CC -!- MASS SPECTROMETRY: Mass=2948; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:16386333}; CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. CC Ranatuerin subfamily. {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; P85058; -. DR SMR; P85058; -. 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:0002553; P:histamine secretion by mast cell; IDA:UniProtKB. DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IDA:UniProtKB. DR InterPro; IPR012521; Antimicrobial_frog_2. DR Pfam; PF08023; Antimicrobial_2; 1. PE 1: Evidence at protein level; KW Amphibian defense peptide; Antibiotic; Antimicrobial; KW Direct protein sequencing; Disulfide bond; Inflammatory response; KW Mast cell degranulation; Secreted. FT PEPTIDE 1..28 FT /note="Ranatuerin-2SEb" FT /id="PRO_0000271260" FT DISULFID 23..28 FT /evidence="ECO:0000250|UniProtKB:P40840" SQ SEQUENCE 28 AA; 2950 MW; 3A0689B5B2BDBED0 CRC64; AIMDTIKDTA KTVAVGLLNK LKCKITGC //