ID   BMNL1_BOMOR             Reviewed;         204 AA.
AC   P29002;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Bombinin-like peptides 1;
DE   Contains:
DE     RecName: Full=Acidic peptide 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 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 44-70 AND 107-133,
RP   AND AMIDATION AT ASN-70 AND ASN-133.
RC   TISSUE=Skin, and Skin secretion;
RX   PubMed=1744108; DOI=10.1016/s0021-9258(18)54469-0;
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).
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; M76483; AAA73094.1; -; Genomic_DNA.
DR   PIR; A41575; A41575.
DR   AlphaFoldDB; P29002; -.
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_0000003051"
FT   PEPTIDE         44..70
FT                   /note="Bombinin-like peptide 1"
FT                   /id="PRO_0000003052"
FT   PEPTIDE         74..81
FT                   /note="Octapeptide 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003053"
FT   PEPTIDE         84..106
FT                   /note="Acidic peptide 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003054"
FT   PEPTIDE         107..133
FT                   /note="Bombinin-like peptide 1"
FT                   /id="PRO_0000003055"
FT   PEPTIDE         137..144
FT                   /note="Octapeptide 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003056"
FT   PEPTIDE         147..181
FT                   /note="Acidic peptide 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003057"
FT   PEPTIDE         187..204
FT                   /note="GH-1 peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003058"
FT   MOD_RES         70
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:1744108"
FT   MOD_RES         133
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:1744108"
SQ   SEQUENCE   204 AA;  22295 MW;  DF0EF088241E1263 CRC64;
     MNFKYIVAVS ILIASAYARS EENDIQSLSQ RDVLEEESLR EIRGIGASIL SAGKSALKGL
     AKGLAEHFAN GKRTAEDHEV MKRLEAAIQS LSQRDVLEEE SLREIRGIGA SILSAGKSAL
     KGLAKGLAEH FANGKRTAEE HEVMKRLEAV MRDLDSLDYP EEASEMETRS FNQEEIANLY
     TKKEKRILGP ILGLVSNALG GLLG