ID   TPF_RANTE               Reviewed;          13 AA.
AC   P56921;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   29-SEP-2021, entry version 43.
DE   RecName: Full=Temporin-1Tf {ECO:0000250|UniProtKB:P56917};
DE            Short=TF {ECO:0000250|UniProtKB:P56917};
DE   AltName: Full=Temporin-F {ECO:0000303|PubMed:9022710};
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   PROTEIN SEQUENCE, AMIDATION AT LEU-13, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin secretion;
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=25668079; DOI=10.3390/molecules20022775;
RA   Eggimann G.A., Sweeney K., Bolt H.L., Rozatian N., Cobb S.L., Denny P.W.;
RT   "The role of phosphoglycans in the susceptibility of Leishmania mexicana to
RT   the temporin family of anti-microbial peptides.";
RL   Molecules 20:2775-2785(2015).
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 potent
CC       activity against Gram-positive bacteria, weak activity against Gram-
CC       negative bacteria, and moderate activity against fungi (By similarity).
CC       Also displays anti-leishmania activity by damaging parasite membrane
CC       (PubMed:25668079). Stimulates insulin release from pancreatic beta-
CC       cells in a dose-dependent manner, without increasing intracellular
CC       calcium (PubMed:29349894). Protects beta-cells against cytokine-induced
CC       apoptosis and augments beta-cells proliferation (PubMed:29349894). In
CC       vivo, intraperitoneal injection together with a glucose load into mice
CC       does not have effect on plasma glucose levels (PubMed:29349894).
CC       {ECO:0000250|UniProtKB:P56917, ECO:0000269|PubMed:25668079,
CC       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=00098";
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   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Immunity; Innate immunity; Secreted.
FT   PEPTIDE         1..13
FT                   /note="Temporin-1Tf"
FT                   /evidence="ECO:0000269|PubMed:9022710"
FT                   /id="PRO_0000043583"
FT   MOD_RES         13
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:9022710"
SQ   SEQUENCE   13 AA;  1370 MW;  2653612B9DECC338 CRC64;
     FLPLIGKVLS GIL