ID BLP3_BOMOR STANDARD; PRT; 200 AA. AC P29004; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE BOMBININ-LIKE PEPTIDE 3 PRECURSOR (BLP-3). OS Bombina orientalis (Oriental fire-bellied toad). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Archeobatrachia; Bombinatoridae; Bombina. RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 44-68 AND 105-129. RC TISSUE=SKIN; RX MEDLINE; 92078177. RA Gibson B.W., Tang D., Mandrell R., Kelly M., Spindel E.R.; RT "Bombinin-like peptides with antimicrobial activity from skin RT secretions of the Asian toad, Bombina orientalis."; RL J. Biol. Chem. 266:23103-23111(1991). CC -!- FUNCTION: HAS ANTIMICROBIAL ACTIVITY, BUT NO HEMOLYTIC ACTIVITY. CC PREFERENCE ON KILLING GRAM-NEGATIVE NON-ENTERIC BACTERIA. CC -!- SUBCELLULAR LOCATION: BY VIRTUE OF THEIR SIZE, ALL BOMBININ-LIKE CC PEPTIDES ARE CAPABLE OF SPANNING A BILAYER LIPID MEMBRANE. CC -!- SIMILARITY: BELONGS TO THE BOMBININ FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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 EMBL; M76484; AAA73095.1; -. DR PIR; C41575; C41575. KW Antibiotic; Amidation; Cleavage on pair of basic residues; Signal; KW Amphibian skin; Duplication. FT SIGNAL 1 16 OR 18. FT PEPTIDE 17 43 ACIDIC PEPTIDE 1 (POTENTIAL). FT PEPTIDE 44 68 BOMBININ-LIKE PEPTIDE 3. FT PEPTIDE 72 79 OCTAPEPTIDE 1 (POTENTIAL). FT PEPTIDE 82 104 ACIDIC PEPTIDE 2 (POTENTIAL). FT PEPTIDE 105 129 BOMBININ-LIKE PEPTIDE 3. FT PEPTIDE 133 140 OCTAPEPTIDE 2 (POTENTIAL). FT PEPTIDE 143 177 ACIDIC PEPTIDE 3 (POTENTIAL). FT PEPTIDE 183 200 HYDROPHOBIC PEPTIDE (POTENTIAL). FT MOD_RES 68 68 AMIDATION (G-69 PROVIDE AMIDE GROUP). FT MOD_RES 129 129 AMIDATION (G-130 PROVIDE AMIDE GROUP). SQ SEQUENCE 200 AA; 21934 MW; 1185F0836BF8A277 CRC64; MNFKYIVAVS ILIASAYARS EENDIQSLSQ RDVLEEESLR EIRGIGAAIL SAGKSALKGL AKGLAEHFGK RTAEDHEVMK RLEAAIHSLS QRDVLEEESL REIRGIGAAI LSAGKSALKG LAKGLAEHFG KRTAEEHEMM KRLEAVMRDL DSLDYPEEAS EMETRSFNQE EIANLYTKKE KRILGPILGL VSNALGGLLG //