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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
 
 
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