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 01-JUL-1993 (REL. 26, LAST ANNOTATION UPDATE) DE BOMBININ-LIKE PEPTIDE PRECURSOR (BLP). OS BOMBINA VARIEGATA (YELLOW-BELLIED TOAD). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; AMPHIBIA; ANURA. RN [1] RP SEQUENCE FROM N.A., AND PRELIMINARY SEQUENCE OF 44-69. RC TISSUE=SKIN; RM 91293126 RA SIMMACO M., BARRA D., CHIARINI F., NOVIELLO L., MELCHIORRI P., RA KREIL G., RICHTER K.; RL EUR. J. BIOCHEM. 199:217-222(1991). 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 -!- SUBCELLULAR LOCATION: BY VIRTUE OF THEIR SIZE, ALL BOMBININ-LIKE CC PEPTIDES ARE CAPABLE OF SPANNING A BILAYER LIPID MEMBRANE. CC -!- SIMILARITY: STRONG WITH OTHER BOMBININ-LIKE PEPTIDES. 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; BVBOMBIN. DR PIR; S16222; S16222. KW ANTIBIOTIC; AMIDATION; CLEAVAGE ON PAIR OF BASIC RESIDUES; SIGNAL; KW AMPHIBIAN SKIN. 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 117 133 OR 136, "ILE PEPTIDE". FT MOD_RES 70 70 AMIDATION (G-71 PROVIDES AMIDE GROUP). FT MOD_RES 136 136 AMIDATION (G-137 PROVIDES AMIDE GROUP) FT (PROBABLE). SQ SEQUENCE 137 AA; 14982 MW; 85331 CN; MNFKYIVAVS ILIASAYARS EENDIQSLSQ RDVLEEESLR EIRGIGGALL SAAKVGLKGL AKGLAEHFAN GKRTAEEREV MKRLEAAMRD LDSFEHPEEA SEKETRGFNQ EEKEKRIIGP VLGLVGSALG GLLKKIG //