B1SN2_SYLSP
ID B1SN2_SYLSP Reviewed; 71 AA.
AC E7EKH2;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Brevinin-1SN2 {ECO:0000303|PubMed:24055160};
DE Flags: Precursor;
OS Sylvirana spinulosa (Fine-spined frog) (Hylarana spinulosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Sylvirana.
OX NCBI_TaxID=369515 {ECO:0000303|PubMed:24055160};
RN [1] {ECO:0000312|EMBL:ADV36172.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-71, FUNCTION, SYNTHESIS,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Skin {ECO:0000303|PubMed:24055160};
RX PubMed=24055160; DOI=10.1016/j.biochi.2013.09.002;
RA Yang X., Hu Y., Xu S., Hu Y., Meng H., Guo C., Liu Y., Liu J., Yu Z.,
RA Wang H.;
RT "Identification of multiple antimicrobial peptides from the skin of fine-
RT spined frog, Hylarana spinulosa (Ranidae).";
RL Biochimie 95:2429-2436(2013).
CC -!- FUNCTION: Antimicrobial peptide. Active against a variety of Gram-
CC negative and Gram-positive bacterial strains. Active against fungus
CC C.glabrata 090902 and C.albicans ATCC 10231. Shows hemolytic activity
CC against human erythrocytes. {ECO:0000269|PubMed:24055160}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24055160}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:24055160}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000255}.
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DR EMBL; HQ735149; ADV36172.1; -; mRNA.
DR AlphaFoldDB; E7EKH2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
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; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..45
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:24055160"
FT /id="PRO_0000439770"
FT PEPTIDE 48..71
FT /note="Brevinin-1SN2"
FT /evidence="ECO:0000269|PubMed:24055160"
FT /id="PRO_0000439771"
FT DISULFID 65..71
FT /evidence="ECO:0000250|UniProtKB:E7EKC4"
SQ SEQUENCE 71 AA; 8077 MW; E9C3FC3AECF7099D CRC64;
MFTMKKSLLL IFFLGTINLS LCEEERNADE DEKRDGDDES DVEVQKRFMG TALKIAANVL
PAAFCKIFKK C