ID BMNL3_BOMOR Reviewed; 200 AA. AC P29004; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 03-APR-2013, entry version 51. DE RecName: Full=Bombinin-like peptides 3; DE Contains: DE RecName: Full=Acidic peptide 1; DE Contains: DE RecName: Full=Bombinin-like peptide 3; DE Short=BLP-3; DE Contains: DE RecName: Full=Octapeptide 1; DE Contains: DE RecName: Full=Acidic peptide 2; DE Contains: DE RecName: Full=Octapeptide 2; DE Contains: DE RecName: Full=Acidic peptide 3; DE Contains: DE RecName: Full=GH-1 peptide; DE Flags: Precursor; OS Bombina orientalis (Oriental fire-bellied toad). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Bombinatoridae; Bombina. OX NCBI_TaxID=8346; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 44-68 AND RP 105-129. RC TISSUE=Skin, and Skin secretion; RX PubMed=1744108; 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). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=9684858; DOI=10.1016/S0014-5793(98)00718-2; RA Miele R., Ponti D., Boman H.G., Barra D., Simmaco M.; RT "Molecular cloning of a bombinin gene from Bombina orientalis: RT detection of NF-kappaB and NF-IL6 binding sites in its promoter."; RL FEBS Lett. 431:23-28(1998). CC -!- FUNCTION: Has antimicrobial activity, but no hemolytic activity. CC Preference on killing Gram-negative non-enteric bacteria. 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; M76484; AAA73095.1; -; Genomic_DNA. DR EMBL; AJ007445; CAA07511.1; -; Genomic_DNA. DR PIR; C41575; C41575. DR HOVERGEN; HBG031694; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR InterPro; IPR007962; Bombinin. DR Pfam; PF05298; Bombinin; 2. PE 1: Evidence at protein level; KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; KW Cleavage on pair of basic residues; Direct protein sequencing; Repeat; KW Secreted; Signal. FT SIGNAL 1 16 Or 18. FT PEPTIDE 17 43 Acidic peptide 1 (Potential). FT /FTId=PRO_0000003059. FT PEPTIDE 44 68 Bombinin-like peptide 3. FT /FTId=PRO_0000003060. FT PEPTIDE 72 79 Octapeptide 1 (Potential). FT /FTId=PRO_0000003061. FT PEPTIDE 82 104 Acidic peptide 2 (Potential). FT /FTId=PRO_0000003062. FT PEPTIDE 105 129 Bombinin-like peptide 3. FT /FTId=PRO_0000003063. FT PEPTIDE 133 140 Octapeptide 2 (Potential). FT /FTId=PRO_0000003064. FT PEPTIDE 143 177 Acidic peptide 3 (Potential). FT /FTId=PRO_0000003065. FT PEPTIDE 183 200 GH-1 peptide (Potential). FT /FTId=PRO_0000003066. FT MOD_RES 68 68 Phenylalanine amide. FT MOD_RES 129 129 Phenylalanine amide. FT CONFLICT 11 11 I -> F (in Ref. 2; CAA07511). FT CONFLICT 84 84 A -> V (in Ref. 2; CAA07511). FT CONFLICT 87 87 H -> Q (in Ref. 2; CAA07511). FT CONFLICT 139 139 M -> V (in Ref. 2; CAA07511). FT CONFLICT 162 162 M -> R (in Ref. 2; CAA07511). FT CONFLICT 166 166 S -> D (in Ref. 2; CAA07511). FT CONFLICT 172 178 Missing (in Ref. 2; CAA07511). FT CONFLICT 184 184 L -> I (in Ref. 2; CAA07511). FT CONFLICT 187 187 I -> V (in Ref. 2; CAA07511). FT CONFLICT 192 200 SNALGGLLG -> GKPLESLLE (in Ref. 2; FT CAA07511). 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 //