ID BLP_BOMVA STANDARD; PRT; 137 AA. AC P29006; 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 PRECURSOR (BLP). OS Bombina variegata (Yellow-bellied toad). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Amphibia; OC Batrachia; Anura; Archeobatrachia; Bombinatoridae; Bombina. RN [1] RP SEQUENCE FROM N.A., AND PRELIMINARY SEQUENCE OF 44-69. RC TISSUE=SKIN; RX MEDLINE; 91293126. RA SIMMACO M., BARRA D., CHIARINI F., NOVIELLO L., MELCHIORRI P., RA KREIL G., RICHTER K.; RT "A family of bombinin-related peptides from the skin of Bombina RT variegata."; RL Eur. J. Biochem. 199:217-222(1991). RN [2] RP SEQUENCE OF 117-136, AND POST-TRANSLATIONAL MODIFICATIONS. RC TISSUE=SKIN; RX MEDLINE; 94038967. RA MIGNOGNA G., SIMMACO M., KREIL G., BARRA D.; RT "Antibacterial and haemolytic peptides containing D-alloisoleucine RT from the skin of Bombina variegata."; RL EMBO J. 12:4829-4832(1993). CC -!- FUNCTION: HAS ANTIMICROBIAL ACTIVITY, BUT NO HEMOLYTIC ACTIVITY. CC PRELIMINARY EVIDENCE INDICATES THAT THIS PEPTIDE DOES NOT LYSE AND CC THUS KILL THE BACTERIA BY ITS ANTIMICROBIAL ACTIVITY. CC -!- FUNCTION: BOMBININ H HAS ANTIBACTERIAL AND HEMOLYTIC ACTIVITY. 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; X59695; CAA42216.1; -. DR PIR; S16222; S16222. KW Antibiotic; Amidation; Cleavage on pair of basic residues; Signal; KW Amphibian skin; D-amino acid. FT SIGNAL 1 18 POTENTIAL. FT PEPTIDE 19 43 ACIDIC PEPTIDE 1 (POTENTIAL). FT PEPTIDE 44 70 BOMBININ-LIKE PEPTIDE. FT PEPTIDE 74 81 OCTAPEPTIDE (POTENTIAL). FT PEPTIDE 84 114 ACIDIC PEPTIDE 2 (POTENTIAL). FT PEPTIDE 117 136 BOMBININ H. FT MOD_RES 70 70 AMIDATION (G-71 PROVIDE AMIDE GROUP). FT MOD_RES 118 118 D-ALLOISOLEUCINE. FT MOD_RES 136 136 AMIDATION (G-137 PROVIDE AMIDE GROUP). FT VARIANT 117 117 I -> L. FT VARIANT 124 124 L -> M. SQ SEQUENCE 137 AA; 14982 MW; 5EB82692 CRC32; MNFKYIVAVS ILIASAYARS EENDIQSLSQ RDVLEEESLR EIRGIGGALL SAAKVGLKGL AKGLAEHFAN GKRTAEEREV MKRLEAAMRD LDSFEHPEEA SEKETRGFNQ EEKEKRIIGP VLGLVGSALG GLLKKIG //