B2CG1_AMOCU
ID B2CG1_AMOCU Reviewed; 74 AA.
AC E1AWD6;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 28.
DE RecName: Full=Brevinin-2CG1 {ECO:0000303|PubMed:22951323};
DE Flags: Precursor;
OS Amolops chunganensis (Chungan torrent frog) (Hylorana chunganensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Amolops.
OX NCBI_TaxID=325556 {ECO:0000303|PubMed:22951323};
RN [1] {ECO:0000312|EMBL:ADM34208.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-74, FUNCTION, SYNTHESIS,
RP SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion {ECO:0000303|PubMed:22951323};
RX PubMed=22951323; DOI=10.1016/j.peptides.2012.08.008;
RA Yang X., Xia J., Yu Z., Hu Y., Li F., Meng H., Yang S., Liu J., Wang H.;
RT "Characterization of diverse antimicrobial peptides in skin secretions of
RT Chungan torrent frog Amolops chunganensis.";
RL Peptides 38:41-53(2012).
CC -!- FUNCTION: Antimicrobial peptide active against a variety of Gram-
CC positive and some Gram-negative bacterial strains. Has antifungal
CC activity against a slime mold isolate. Has hemolytic activity against
CC human erythrocytes. {ECO:0000269|PubMed:22951323}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC ECO:0000269|PubMed:22951323}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:22951323}.
CC -!- MASS SPECTROMETRY: Mass=3406.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22951323};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HQ009832; ADM34208.1; -; mRNA.
DR AlphaFoldDB; E1AWD6; -.
DR SMR; E1AWD6; -.
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 InterPro; IPR012521; Antimicrobial_frog_2.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF08023; Antimicrobial_2; 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; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..39
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:22951323"
FT /id="PRO_0000439734"
FT PEPTIDE 42..74
FT /note="Brevinin-2CG1"
FT /evidence="ECO:0000269|PubMed:22951323"
FT /id="PRO_0000439735"
FT DISULFID 68..74
FT /evidence="ECO:0000250|UniProtKB:P80398"
SQ SEQUENCE 74 AA; 8165 MW; 3D63B1F2A8DD6811 CRC64;
MFTMKKSMLV LFFLGTISLS LCEEERNADE DDGEMTEEVK RGILDKLKEF GISAARGVAQ
SLLNTASCKL AKTC