BMNH5_BOMVA
ID BMNH5_BOMVA Reviewed; 21 AA.
AC P82285;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Bombinin-H5;
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 PROTEIN SEQUENCE, D-AMINO ACID AT ILE-2, AND AMIDATION AT ILE-20.
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 and hemolytic activities.
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 PDB; 2AP7; NMR; -; A=1-20.
DR PDB; 2AP8; NMR; -; A=1-20.
DR PDBsum; 2AP7; -.
DR PDBsum; 2AP8; -.
DR AlphaFoldDB; P82285; -.
DR BMRB; P82285; -.
DR SMR; P82285; -.
DR EvolutionaryTrace; P82285; -.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW Antimicrobial; Cytolysis; D-amino acid; Direct protein sequencing;
KW Hemolysis; Secreted.
FT PEPTIDE 1..20
FT /note="Bombinin-H5"
FT /id="PRO_0000003079"
FT MOD_RES 2
FT /note="D-allo-isoleucine"
FT /evidence="ECO:0000269|PubMed:8223491"
FT MOD_RES 20
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:8223491"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:2AP7"
SQ SEQUENCE 21 AA; 1975 MW; 08C7281E1BDBF3BD CRC64;
IIGPVLGLVG SALGGLLKKI G