ID   BR2GB_SYLGU             Reviewed;          72 AA.
AC   A0AEI5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Brevinin-2GHb;
DE   AltName: Full=AMP-2;
DE   Flags: Precursor;
GN   Name=br2GHb {ECO:0000312|EMBL:CAK18909.1};
OS   Sylvirana guentheri (Gunther's frog) (Rana guentheri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Sylvirana.
OX   NCBI_TaxID=110109;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAK18909.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-72, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISULFIDE BOND, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000269|PubMed:16979798}, and
RC   Skin secretion {ECO:0000269|PubMed:16979798};
RX   PubMed=16979798; DOI=10.1016/j.peptides.2006.08.007;
RA   Zhou J., McClean S., Thompson A., Zhang Y., Shaw C., Rao P., Bjourson A.J.;
RT   "Purification and characterization of novel antimicrobial peptides from the
RT   skin secretion of Hylarana guentheri.";
RL   Peptides 27:3077-3084(2006).
CC   -!- FUNCTION: Antimicrobial peptide. Active against the Gram-positive
CC       bacteria S.aureus FDA209P (MIC=16.5 ug/ml) and B.subtilis ATCC 6633
CC       (MIC>64 ug/ml), and the Gram-negative bacteria E.coli O111 (MIC=8.2
CC       ug/ml) and E.coli ATCC 25922 (MIC=8.2 ug/ml). Not active against the
CC       fungus C.albicans. {ECO:0000269|PubMed:16979798}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16979798}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:16979798}.
CC   -!- MASS SPECTROMETRY: Mass=3079.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16979798};
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; AM262989; CAK18909.1; -; mRNA.
DR   AlphaFoldDB; A0AEI5; -.
DR   SMR; A0AEI5; -.
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:0044179; P:hemolysis in another organism; IEA:UniProt.
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; Direct protein sequencing;
KW   Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..42
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:16979798"
FT                   /id="PRO_0000271186"
FT   PEPTIDE         43..72
FT                   /note="Brevinin-2GHb"
FT                   /evidence="ECO:0000269|PubMed:16979798"
FT                   /id="PRO_5000147964"
FT   DISULFID        66..72
FT                   /evidence="ECO:0000269|PubMed:16979798"
SQ   SEQUENCE   72 AA;  7835 MW;  62AD49E1AEB76284 CRC64;
     MFTMKKSLLL LFFLGTVSLS LCEQERGADE DDGGEMTEEL KRGVITDALK GAAKTVAAEL
     LRKAHCKLTN SC