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   11-DEC-2019, entry version 59.
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; Amphibia;
OC   Batrachia; Anura; Bombinatoridae; Bombina.
OX   NCBI_TaxID=8346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 44-68 AND 105-129,
RP   AND AMIDATION AT PHE-68 AND PHE-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 secretions of
RT   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: detection of
RT   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. {ECO:0000305}.
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DR   EMBL; M76484; AAA73095.1; -; Genomic_DNA.
DR   EMBL; AJ007445; CAA07511.1; -; Genomic_DNA.
DR   PIR; C41575; C41575.
DR   SMR; P29004; -.
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
FT                   /note="Or 18"
FT   PEPTIDE         17..43
FT                   /note="Acidic peptide 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003059"
FT   PEPTIDE         44..68
FT                   /note="Bombinin-like peptide 3"
FT                   /id="PRO_0000003060"
FT   PEPTIDE         72..79
FT                   /note="Octapeptide 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003061"
FT   PEPTIDE         82..104
FT                   /note="Acidic peptide 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003062"
FT   PEPTIDE         105..129
FT                   /note="Bombinin-like peptide 3"
FT                   /id="PRO_0000003063"
FT   PEPTIDE         133..140
FT                   /note="Octapeptide 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003064"
FT   PEPTIDE         143..177
FT                   /note="Acidic peptide 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003065"
FT   PEPTIDE         183..200
FT                   /note="GH-1 peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003066"
FT   MOD_RES         68
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:1744108"
FT   MOD_RES         129
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:1744108"
FT   CONFLICT        11
FT                   /note="I -> F (in Ref. 2; CAA07511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="A -> V (in Ref. 2; CAA07511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="H -> Q (in Ref. 2; CAA07511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139
FT                   /note="M -> V (in Ref. 2; CAA07511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="M -> R (in Ref. 2; CAA07511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="S -> D (in Ref. 2; CAA07511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172..178
FT                   /note="Missing (in Ref. 2; CAA07511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="L -> I (in Ref. 2; CAA07511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="I -> V (in Ref. 2; CAA07511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192..200
FT                   /note="SNALGGLLG -> GKPLESLLE (in Ref. 2; CAA07511)"
FT                   /evidence="ECO:0000305"
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
//