ID BMNL1_BOMVA Reviewed; 137 AA. AC P29006; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 05-APR-2011, entry version 52. DE RecName: Full=Bombinin-like peptides 1; DE Contains: DE RecName: Full=Acidic peptide 1-1; DE Contains: DE RecName: Full=Bombinin-like peptide 1; DE Short=BLP-1; DE Contains: DE RecName: Full=Octapeptide 1; DE Contains: DE RecName: Full=Acidic peptide 1-2; DE Contains: DE RecName: Full=Bombinin-H; DE Flags: Precursor; OS Bombina variegata (Yellow-bellied toad). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Archeobatrachia; Bombinatoridae; Bombina. OX NCBI_TaxID=8348; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PRELIMINARY PROTEIN SEQUENCE OF 44-69. RC TISSUE=Skin, and Skin secretion; RX MEDLINE=91293126; PubMed=1712299; RX DOI=10.1111/j.1432-1033.1991.tb16112.x; 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 PROTEIN SEQUENCE OF 117-136, D-AMINO ACID AT ILE-118, AND AMIDATION AT RP ILE-136. RC TISSUE=Skin secretion; RX MEDLINE=94038967; PubMed=8223491; 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: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the skin glands. CC -!- SIMILARITY: Belongs to the bombinin family. 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; -; mRNA. DR PIR; S16222; S16222. DR HOVERGEN; HBG031694; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW. DR InterPro; IPR007962; Bombinin. DR Pfam; PF05298; Bombinin; 1. PE 1: Evidence at protein level; KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; KW Cleavage on pair of basic residues; Cytolysis; D-amino acid; KW Direct protein sequencing; Hemolysis; Secreted; Signal. FT SIGNAL 1 18 Potential. FT PEPTIDE 19 43 Acidic peptide 1-1 (Potential). FT /FTId=PRO_0000003067. FT PEPTIDE 44 70 Bombinin-like peptide 1. FT /FTId=PRO_0000003068. FT PEPTIDE 74 81 Octapeptide 1 (Potential). FT /FTId=PRO_0000003069. FT PEPTIDE 84 114 Acidic peptide 1-2 (Potential). FT /FTId=PRO_0000003070. FT PEPTIDE 117 136 Bombinin-H. FT /FTId=PRO_0000003071. FT MOD_RES 70 70 Asparagine amide. FT MOD_RES 118 118 D-allo-isoleucine. FT MOD_RES 136 136 Isoleucine amide. FT VARIANT 117 117 I -> L. FT VARIANT 124 124 L -> M. SQ SEQUENCE 137 AA; 14982 MW; 3EC3EF6E47CA1F92 CRC64; MNFKYIVAVS ILIASAYARS EENDIQSLSQ RDVLEEESLR EIRGIGGALL SAAKVGLKGL AKGLAEHFAN GKRTAEEREV MKRLEAAMRD LDSFEHPEEA SEKETRGFNQ EEKEKRIIGP VLGLVGSALG GLLKKIG //