ID   TPH_RANTE               Reviewed;          58 AA.
AC   P79876; P56922;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Temporin-1Th {ECO:0000250|UniProtKB:P56917};
DE            Short=TH {ECO:0000250|UniProtKB:P56917};
DE   AltName: Full=Temporin-H {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], PROTEIN SEQUENCE OF 47-56, AMIDATION AT LEU-56,
RP   SYNTHESIS OF 47-56, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin, and 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=10691983; DOI=10.1046/j.1432-1327.2000.01143.x;
RA   Mangoni M.L., Rinaldi A.C., Di Giulio A., Mignogna G., Bozzi A., Barra D.,
RA   Simmaco M.;
RT   "Structure-function relationships of temporins, small antimicrobial
RT   peptides from amphibian skin.";
RL   Eur. J. Biochem. 267:1447-1454(2000).
CC   -!- FUNCTION: Antimicrobial peptide that renders both the outer and inner
CC       membrane of bacteria permeable to hydrophobic substances of low
CC       molecular mass. {ECO:0000269|PubMed:10691983}.
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=00859";
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DR   EMBL; Y09394; CAA70563.1; -; mRNA.
DR   AlphaFoldDB; P79876; -.
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; Direct protein sequencing; Immunity;
KW   Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..46
FT                   /evidence="ECO:0000305|PubMed:9022710"
FT                   /id="PRO_0000003475"
FT   PEPTIDE         47..56
FT                   /note="Temporin-1Th"
FT                   /evidence="ECO:0000269|PubMed:9022710"
FT                   /id="PRO_0000003476"
FT   REGION          25..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:9022710"
SQ   SEQUENCE   58 AA;  6806 MW;  684AECB0451E5E81 CRC64;
     MFTLKKSLLL LFFLGTINLS LCEEERNAEE ERRDEPDERD VQVEKRLSPN LLKSLLGK