ID   B2SN4_SYLSP             Reviewed;          72 AA.
AC   E7EKH7;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Brevinin-2SN4 {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:ADV36177.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SYNTHESIS.
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. Not active against fungi.
CC       Shows very weak hemolytic activity against human erythrocytes.
CC       {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; HQ735154; ADV36177.1; -; mRNA.
DR   AlphaFoldDB; E7EKH7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR012521; Antimicrobial_frog_2.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF08023; Antimicrobial_2; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   3: Inferred from homology;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Disulfide bond; Hemolysis;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..40
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:24055160"
FT                   /id="PRO_0000439780"
FT   PEPTIDE         43..72
FT                   /note="Brevinin-2SN4"
FT                   /evidence="ECO:0000303|PubMed:24055160"
FT                   /id="PRO_0000439781"
FT   DISULFID        66..72
FT                   /evidence="ECO:0000303|PubMed:24055160"
SQ   SEQUENCE   72 AA;  7894 MW;  C11307D10F20FB21 CRC64;
     MFTMKKPMLL LFFLGMISMS LCQDERGADE DDGGEMTEEE KRGAFGDLLK GVAKEAGLKL
     LNMAQCKLSG NC