BMN_BOMVA
ID BMN_BOMVA Reviewed; 24 AA.
AC P01505;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Bombinin;
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, AND AMIDATION AT ASN-24.
RC TISSUE=Skin secretion;
RA Csordas A., Michl H.;
RT "Isolation and structural resolution of a haemolytically active polypeptide
RT from the immune secretion of a European toad.";
RL Monatsh. Chem. 101:182-189(1970).
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}.
CC -!- CAUTION: Residue 20 is assigned as E by similarity to other bombin
CC sequences instead of Z (Glutamic acid or Gutamine) given in the
CC original sequence by the authors. {ECO:0000305}.
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DR PIR; A01766; BMTD.
DR AlphaFoldDB; P01505; -.
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 Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW Direct protein sequencing; Hemolysis; Secreted.
FT PEPTIDE 1..24
FT /note="Bombinin"
FT /id="PRO_0000043500"
FT MOD_RES 24
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 24 AA; 2295 MW; ACC0FCE3A5D02E85 CRC64;
GIGALSAKGA LKGLAKGLAE HFAN