ID   TEMG_RANTE              Reviewed;          61 AA.
AC   P79875;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-JUL-2012, entry version 51.
DE   RecName: Full=Temporin-G;
DE   Flags: Precursor;
OS   Rana temporaria (European common frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana;
OC   Rana.
OX   NCBI_TaxID=8407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RX   MEDLINE=97175050; PubMed=9022710;
RX   DOI=10.1111/j.1432-1033.1996.0788r.x;
RA   Simmaco M., Mignogna G., Canofeni S., Miele R., Mangoni M.L.,
RA   Barra D.;
RT   "Temporins, antimicrobial peptides from the European red frog Rana
RT   temporaria.";
RL   Eur. J. Biochem. 242:788-792(1996).
CC   -!- FUNCTION: Antimicrobial peptide (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily.
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DR   EMBL; Y09395; CAA70564.1; -; mRNA.
DR   TCDB; 1.C.52.1.5; dermaseptin family.
DR   HOVERGEN; HBG005608; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Brevinin.
DR   Pfam; PF03032; Brevenin; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Secreted; Signal.
FT   SIGNAL        1     22       Potential.
FT   PROPEP       23     46       Potential.
FT                                /FTId=PRO_0000003473.
FT   PEPTIDE      47     59       Temporin-G.
FT                                /FTId=PRO_0000003474.
FT   MOD_RES      59     59       Leucine amide (By similarity).
SQ   SEQUENCE   61 AA;  7171 MW;  EDF5A8BC79DFD9F2 CRC64;
     MFTLKKSLLL LFFLGTINLS LCEEERDADE ERRDDLEERD VEVEKRFFPV IGRILNGILG
     K
//