BRA_AMOLO
ID BRA_AMOLO Reviewed; 70 AA.
AC A0SN38;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Brevinins-ALa {ECO:0000303|PubMed:17000029};
DE AltName: Full=Amolopin-1a {ECO:0000312|EMBL:ABG72906.1};
DE AltName: Full=Brevinins-1E-AL1 {ECO:0000303|PubMed:19843479};
DE Flags: Precursor;
OS Amolops loloensis (Lolokou Sucker Frog) (Staurois loloensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Amolops.
OX NCBI_TaxID=318551;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-70, SUBCELLULAR
RP LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Skin, and Skin secretion;
RX PubMed=17000029; DOI=10.1016/j.peptides.2006.08.017;
RA Lu Y., Li J., Yu H., Xu X., Liang J., Tian Y., Ma D., Lin G., Huang G.,
RA Lai R.;
RT "Two families of antimicrobial peptides with multiple functions from skin
RT of rufous-spotted torrent frog, Amolops loloensis.";
RL Peptides 27:3085-3091(2006).
RN [2]
RP NOMENCLATURE.
RX PubMed=19843479; DOI=10.1016/j.cbpb.2009.10.003;
RA Wang M., Wang Y., Wang A., Song Y., Ma D., Yang H., Ma Y., Lai R.;
RT "Five novel antimicrobial peptides from skin secretions of the frog,
RT Amolops loloensis.";
RL Comp. Biochem. Physiol. 155:72-76(2010).
CC -!- FUNCTION: Antimicrobial peptide with activity against a variety of
CC Gram-negative and Gram-positive bacteria and against fungi (By
CC similarity). Shows strong hemolytic activity against human erythrocytes
CC (By similarity). {ECO:0000250|UniProtKB:E1B240}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17000029}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:17000029}.
CC -!- MASS SPECTROMETRY: Mass=2665.3; Method=FAB;
CC Evidence={ECO:0000269|PubMed:17000029};
CC -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC that of Brevinin-1MT2 (AC E1B241). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00860";
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DR EMBL; DQ673109; ABG72906.1; -; mRNA.
DR EMBL; DQ673111; ABG72908.1; -; mRNA.
DR AlphaFoldDB; A0SN38; -.
DR TCDB; 1.C.52.1.26; the dermaseptin (dermaseptin) family.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR012520; Antimicrobial_frog_1.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF08018; Antimicrobial_1; 1.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Fungicide; Hemolysis; Immunity; Innate immunity; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..46
FT /evidence="ECO:0000305|PubMed:17000029"
FT /id="PRO_0000450014"
FT PEPTIDE 47..70
FT /note="Brevinins-ALa"
FT /evidence="ECO:0000269|PubMed:17000029"
FT /id="PRO_5007633307"
FT DISULFID 64..70
FT /evidence="ECO:0000250|UniProtKB:E1B240"
SQ SEQUENCE 70 AA; 8189 MW; 5616BDAE077EAD14 CRC64;
MFTLKKSMLL LFFLGTINLS LCEQERNADE EERRDDDEMD VEVEKRFLPM LAGLAANFLP
KLFCKITKKC
