BMNL2_BOMVA
ID BMNL2_BOMVA Reviewed; 137 AA.
AC P82286;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Bombinin-like peptides 2;
DE Contains:
DE RecName: Full=Acidic peptide 2-1;
DE Contains:
DE RecName: Full=Bombinin-like peptide 2;
DE Short=BLP-2;
DE Contains:
DE RecName: Full=Octapeptide 2;
DE Contains:
DE RecName: Full=Acidic peptide 2-2;
DE Contains:
DE RecName: Full=Bombinin-H2;
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 PROTEIN SEQUENCE OF
RP 117-136.
RC TISSUE=Skin, and Skin secretion;
RX PubMed=10333736;
RX DOI=10.1002/(sici)1097-0282(1998)47:6<435::aid-bip3>3.0.co;2-8;
RA Simmaco M., Mignogna G., Barra D.;
RT "Antimicrobial peptides from amphibian skin: what do they tell us?";
RL Biopolymers 47:435-450(1998).
RN [2]
RP PROTEIN SEQUENCE OF 117-136, AND AMIDATION AT 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: Bombinin-like peptide 2 has antimicrobial activity, but no
CC hemolytic activity. Preliminary evidence indicates that this peptide
CC does not lyse and thus kill the bacteria by its antimicrobial activity.
CC -!- FUNCTION: Bombinin H2 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; AJ251565; CAB61443.1; -; mRNA.
DR AlphaFoldDB; P82286; -.
DR BMRB; P82286; -.
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; Direct protein sequencing;
KW Hemolysis; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PEPTIDE 19..43
FT /note="Acidic peptide 2-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003072"
FT PEPTIDE 44..70
FT /note="Bombinin-like peptide 2"
FT /id="PRO_0000003073"
FT PEPTIDE 74..81
FT /note="Octapeptide 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003074"
FT PEPTIDE 84..114
FT /note="Acidic peptide 2-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003075"
FT PEPTIDE 117..136
FT /note="Bombinin-H2"
FT /id="PRO_0000003076"
FT REGION 92..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:10333736"
FT MOD_RES 136
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:8223491"
SQ SEQUENCE 137 AA; 15035 MW; 6BFBD1A5F0E6CCD6 CRC64;
MNFKYIVAVS ILIASAYARR EENNIQSLSQ RDVLEEESLR EIRGIGASIL SAGKSALKGF
AKGLAEHFAN GKRTAEDHEM MKRLEAAVRD LDSLEHPEEA SEKETRGFNQ EEKEKRIIGP
VLGLVGSALG GLLKKIG
