TPG_RANTE
ID TPG_RANTE Reviewed; 61 AA.
AC P79875;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Temporin-1Tg {ECO:0000250|UniProtKB:P56917};
DE Short=TG {ECO:0000250|UniProtKB:P56917};
DE AltName: Full=Temporin-G {ECO:0000303|PubMed:22439858, ECO:0000303|PubMed:9022710};
DE Flags: Precursor;
OS Rana temporaria (European common frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX NCBI_TaxID=8407;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT LEU-59, AND SUBCELLULAR LOCATION.
RC TISSUE=Skin;
RX PubMed=9022710; DOI=10.1111/j.1432-1033.1996.0788r.x;
RA Simmaco M., Mignogna G., Canofeni S., Miele R., Mangoni M.L., Barra D.;
RT "Temporins, antimicrobial peptides from the European red frog Rana
RT temporaria.";
RL Eur. J. Biochem. 242:788-792(1996).
RN [2]
RP FUNCTION.
RX PubMed=22439858; DOI=10.1186/1472-6750-12-10;
RA Ke T., Liang S., Huang J., Mao H., Chen J., Dong C., Huang J., Liu S.,
RA Kang J., Liu D., Ma X.;
RT "A novel PCR-based method for high throughput prokaryotic expression of
RT antimicrobial peptide genes.";
RL BMC Biotechnol. 12:10-10(2012).
RN [3]
RP FUNCTION AS INSULINOTROPIC PEPTIDE, AND BIOASSAY.
RX PubMed=29349894; DOI=10.1002/psc.3065;
RA Musale V., Casciaro B., Mangoni M.L., Abdel-Wahab Y.H.A., Flatt P.R.,
RA Conlon J.M.;
RT "Assessment of the potential of temporin peptides from the frog Rana
RT temporaria (Ranidae) as anti-diabetic agents.";
RL J. Pept. Sci. 24:1-12(2018).
CC -!- FUNCTION: Amphipathic alpha-helical antimicrobial peptide with activity
CC against Gram-positive bacteria (M.luteus), Gram-negative bacteria
CC (E.coli), and fungi (S.cerevisiae) (PubMed:22439858). Stimulates
CC insulin release from pancreatic beta-cells in a dose-dependent manner,
CC without increasing intracellular calcium (PubMed:29349894). Does not
CC protects BRIN-BD11 beta-cells against cytokine-induced apoptosis
CC (PubMed:29349894). In vivo, intraperitoneal injection together with a
CC glucose load into mice improves glucose tolerance with a concomitant
CC increase in insulin secretion (PubMed:29349894).
CC {ECO:0000269|PubMed:22439858, ECO:0000269|PubMed:29349894}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9022710}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:9022710}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Temporin subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00099";
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DR EMBL; Y09395; CAA70564.1; -; mRNA.
DR AlphaFoldDB; P79875; -.
DR TCDB; 1.C.52.1.5; the dermaseptin (dermaseptin) family.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:UniProt.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Immunity; Innate immunity; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..44
FT /evidence="ECO:0000305|PubMed:9022710"
FT /id="PRO_0000003473"
FT PEPTIDE 47..59
FT /note="Temporin-1Tg"
FT /evidence="ECO:0000269|PubMed:9022710"
FT /id="PRO_0000003474"
FT MOD_RES 59
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:9022710"
SQ SEQUENCE 61 AA; 7171 MW; EDF5A8BC79DFD9F2 CRC64;
MFTLKKSLLL LFFLGTINLS LCEEERDADE ERRDDLEERD VEVEKRFFPV IGRILNGILG
K