BMN72_BOMOR
ID BMN72_BOMOR Reviewed; 144 AA.
AC Q9DET7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Bombinins BLP-7/GH-2 {ECO:0000305};
DE Contains:
DE RecName: Full=Bombinin-like peptide 7 {ECO:0000303|PubMed:11090922};
DE Short=BLP-7 {ECO:0000303|PubMed:11090922};
DE Contains:
DE RecName: Full=Bombinin GH-2 {ECO:0000303|PubMed:11090922};
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=11090922; DOI=10.1016/s0196-9781(00)00317-x;
RA Miele R., Borro M., Fiocco D., Barra D., Simmaco M.;
RT "Sequence of a gene from Bombina orientalis coding for the antimicrobial
RT peptide BLP-7.";
RL Peptides 21:1681-1686(2000).
RN [2]
RP FUNCTION.
RX PubMed=22439858; DOI=10.1186/1472-6750-12-10;
RA Ke T., Liang S., Huang J., Mao H., Chen J., Dong C., Huang J., Liu S.,
RA Kang J., Liu D., Ma X.;
RT "A novel PCR-based method for high throughput prokaryotic expression of
RT antimicrobial peptide genes.";
RL BMC Biotechnol. 12:10-10(2012).
RN [3]
RP FUNCTION, MASS SPECTROMETRY, AMIDATION AT ASN-70, AND SYNTHESIS OF 44-70.
RX PubMed=28636781; DOI=10.1111/cbdd.13055;
RA Zhou C., Wang Z., Peng X., Liu Y., Lin Y., Zhang Z., Qiu Y., Jin M.,
RA Wang R., Kong D.;
RT "Discovery of two bombinin peptides with antimicrobial and anticancer
RT activities from the skin secretion of Oriental fire-bellied toad, Bombina
RT orientalis.";
RL Chem. Biol. Drug Des. 91:50-61(2018).
RN [4]
RP FUNCTION, SYNTHESIS OF 44-70, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP PHARMACEUTICAL.
RX PubMed=32540219; DOI=10.1016/j.toxicon.2020.06.006;
RA Wu Y., Qiang Y., Cao K., Zhang W., Zhang G.;
RT "Inhibitory effect of the antimicrobial peptide BLP-7 against
RT Propionibacterium acnes and its anti-inflammatory effect on acne
RT vulgaris.";
RL Toxicon 184:109-115(2020).
CC -!- FUNCTION: [Bombinin-like peptide 7]: Antimicrobial peptide with
CC activity against Gram-positive and -negative bacteria and fungi
CC (PubMed:22439858, PubMed:32540219). Shows activity against P.acnes
CC (MIC=5 uM), E.coli (MIC=5-6.3 uM), S.aureus (MIC=5-6.3 uM), M.luteus,
CC S.cerevisiae and C.albicans (MIC=10-12.5 uM) (PubMed:22439858,
CC PubMed:28636781, PubMed:32540219). Also reduces the production of
CC interleukin (IL)-8 and granulocyte-macrophage colony stimulating factor
CC (CSF2) in normal human epidermal keratinocytes (NHEKs)
CC (PubMed:32540219). Shows anticancer activity against three human
CC hepatoma cell lines (PubMed:28636781). In vivo, using the rat ear edema
CC model, suppress P.acnes-induced skin inflammation, significantly
CC reducing the ear thickness (PubMed:32540219). Shows weak hemolytic
CC activity against human erythrocytes (PubMed:28636781).
CC {ECO:0000269|PubMed:22439858, ECO:0000269|PubMed:28636781,
CC ECO:0000269|PubMed:32540219}.
CC -!- FUNCTION: [Bombinin GH-2]: Shows weak antimicrobial activity but high
CC hemolytic activity. {ECO:0000250|UniProtKB:A0A219CM62}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Bombinin-like peptide 7]:
CC pH dependence:
CC Stable from pH 3.0 to 12.0. {ECO:0000269|PubMed:32540219};
CC Temperature dependence:
CC Highly thermostable, when continuously exposed at the temperatures
CC ranging from 20 to 100 degrees Celsius for 30 minutes.
CC {ECO:0000269|PubMed:32540219};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:32540219}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:32540219}.
CC -!- MASS SPECTROMETRY: [Bombinin-like peptide 7]: Mass=2551.01;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:28636781};
CC -!- PHARMACEUTICAL: [Bombinin-like peptide 7]: Could be used as a potential
CC agent in the treatment against acne, since it shows antibacterial
CC activity against P.acnes and it both reduces the production of pro-
CC inflammatory cytokines and the skin inflammation induced by P.acnes in
CC rat ear edema model. {ECO:0000305|PubMed:32540219}.
CC -!- MISCELLANEOUS: BLP-7 is also encoded by another gene from the same
CC species (AC A0A219CM62). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bombinin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00054";
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DR EMBL; AJ298827; CAC11122.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9DET7; -.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of 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; Fungicide; Pharmaceutical; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..43
FT /evidence="ECO:0000305|PubMed:28636781"
FT /id="PRO_0000451082"
FT PEPTIDE 44..70
FT /note="Bombinin-like peptide 7"
FT /evidence="ECO:0000269|PubMed:28636781"
FT /id="PRO_5004325163"
FT PROPEP 74..123
FT /evidence="ECO:0000305|PubMed:28636781"
FT /id="PRO_0000451083"
FT PEPTIDE 124..143
FT /note="Bombinin GH-2"
FT /evidence="ECO:0000250|UniProtKB:Q58T45"
FT /id="PRO_0000451084"
FT MOD_RES 70
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:28636781"
FT MOD_RES 143
FT /note="Isoleucine amide"
FT /evidence="ECO:0000250|UniProtKB:Q58T45"
SQ SEQUENCE 144 AA; 16053 MW; 4ECE7C481D62764B CRC64;
MNFKYIVAVS FLIASTYARS VKNDEQSLSQ RDVLEEESLR EIRGIGGALL SAGKSALKGL
AKGLAEHFAN GKRTAEEHEV MKRLEAVMRD LDSLDYPEEA SEMETRSFNQ EEIANLFTKK
EKRILGPVLD LVGRALRGLL KKIG
