BMNL1_BOMVA
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 25-MAY-2022, entry version 65.
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; Amphibia;
OC Batrachia; Anura; Bombinatoridae; Bombina.
OX NCBI_TaxID=8348;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT ASN-70, AND PRELIMINARY PROTEIN
RP SEQUENCE OF 44-69.
RC TISSUE=Skin, and Skin secretion;
RX PubMed=1712299; DOI=10.1111/j.1432-1033.1991.tb16112.x;
RA Simmaco M., Barra D., Chiarini F., Noviello L., Melchiorri P., Kreil G.,
RA 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 PubMed=8223491; DOI=10.1002/j.1460-2075.1993.tb06172.x;
RA Mignogna G., Simmaco M., Kreil G., Barra D.;
RT "Antibacterial and haemolytic peptides containing D-alloisoleucine from the
RT 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 thus
CC 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. {ECO:0000305}.
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DR EMBL; X59695; CAA42216.1; -; mRNA.
DR PIR; S16222; S16222.
DR AlphaFoldDB; P29006; -.
DR BMRB; P29006; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another 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
FT /evidence="ECO:0000255"
FT PEPTIDE 19..43
FT /note="Acidic peptide 1-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003067"
FT PEPTIDE 44..70
FT /note="Bombinin-like peptide 1"
FT /id="PRO_0000003068"
FT PEPTIDE 74..81
FT /note="Octapeptide 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003069"
FT PEPTIDE 84..114
FT /note="Acidic peptide 1-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003070"
FT PEPTIDE 117..136
FT /note="Bombinin-H"
FT /id="PRO_0000003071"
FT REGION 91..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:1712299"
FT MOD_RES 118
FT /note="D-allo-isoleucine"
FT /evidence="ECO:0000269|PubMed:8223491"
FT MOD_RES 136
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:8223491"
FT VARIANT 117
FT /note="I -> L"
FT VARIANT 124
FT /note="L -> M"
SQ SEQUENCE 137 AA; 14982 MW; 3EC3EF6E47CA1F92 CRC64;
MNFKYIVAVS ILIASAYARS EENDIQSLSQ RDVLEEESLR EIRGIGGALL SAAKVGLKGL
AKGLAEHFAN GKRTAEEREV MKRLEAAMRD LDSFEHPEEA SEKETRGFNQ EEKEKRIIGP
VLGLVGSALG GLLKKIG
