ID   BMNL2_BOMOR             Reviewed;          27 AA.
AC   P29003;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Bombinin-like peptide 2;
DE            Short=BLP-2;
OS   Bombina orientalis (Oriental fire-bellied toad).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Bombinatoridae; Bombina.
OX   NCBI_TaxID=8346;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT ASN-27.
RC   TISSUE=Skin secretion;
RX   PubMed=1744108; DOI=10.1016/s0021-9258(18)54469-0;
RA   Gibson B.W., Tang D., Mandrell R., Kelly M., Spindel E.R.;
RT   "Bombinin-like peptides with antimicrobial activity from skin secretions of
RT   the Asian toad, Bombina orientalis.";
RL   J. Biol. Chem. 266:23103-23111(1991).
CC   -!- FUNCTION: Has antimicrobial activity, but no hemolytic activity.
CC       Preference on killing Gram-negative non-enteric bacteria.
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   PIR; B41575; B41575.
DR   AlphaFoldDB; P29003; -.
DR   SMR; P29003; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; 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   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..27
FT                   /note="Bombinin-like peptide 2"
FT                   /id="PRO_0000043501"
FT   MOD_RES         27
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:1744108"
SQ   SEQUENCE   27 AA;  2582 MW;  FC69D979166710F5 CRC64;
     GIGSAILSAG KSALKGLAKG LAEHFAN