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 12-OCT-2022, entry version 68. 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 PROTEIN SEQUENCE OF 47-59, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR RP LOCATION, AND AMIDATION AT LEU-59. RC TISSUE=Skin secretion {ECO:0000303|PubMed:34235566}; RX PubMed=34235566; DOI=10.1007/s00216-021-03506-1; RA Samgina T.Y., Vasileva I.D., Kovalev S.V., Trebse P., Torkar G., RA Surin A.K., Zubarev R.A., Lebedev A.T.; RT "Differentiation of Central Slovenian and Moscow populations of Rana RT temporaria frogs using peptide biomarkers of temporins family."; RL Anal. Bioanal. Chem. 413:5333-5347(2021). RN [3] 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 [4] 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:34235566, CC ECO:0000269|PubMed:9022710}. CC -!- TISSUE SPECIFICITY: Expressed by the skin glands. CC {ECO:0000305|PubMed:34235566, ECO:0000305|PubMed:9022710}. CC -!- MASS SPECTROMETRY: Mass=1456.89; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:34235566}; 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"; 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; 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; IDA:UniProtKB. 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; Direct protein sequencing; Immunity; KW Innate immunity; Secreted; 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 //