ID   TPE_PELSA               Reviewed;          64 AA.
AC   D5GRW4;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Temporin-SHe {ECO:0000303|PubMed:20308076};
DE            Short=Temp-SHe {ECO:0000303|PubMed:20308076};
DE   Flags: Precursor;
OS   Pelophylax saharicus (Sahara frog) (Rana saharica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=70019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT PHE-62.
RC   TISSUE=Skin;
RX   PubMed=20308076; DOI=10.1074/jbc.m109.097204;
RA   Abbassi F., Lequin O., Piesse C., Goasdoue N., Foulon T., Nicolas P.,
RA   Ladram A.;
RT   "Temporin-SHf, a new type of phe-rich and hydrophobic ultrashort
RT   antimicrobial peptide.";
RL   J. Biol. Chem. 285:16880-16892(2010).
CC   -!- FUNCTION: Non-amphipathic mildly cationic alpha-helical antimicrobial
CC       peptide with potent activity against Gram-positive and Gram-negative
CC       bacteria, and some fungi, as well as against Trypanosoma and Leishmania
CC       (both promastigote and amastigote forms). Strongly and selectively
CC       perturbs anionic bilayer membranes by interacting with the polar head
CC       groups and acyl region of the phospholipids, with formation of regions
CC       of two coexisting phases, one phase rich in peptide and the other
CC       lipid-rich. Shows low hemolytic activity and a low toxicity for human
CC       monocytes THP-1 and THP-1-derived macrophages. Is not toxic to human
CC       hepatoma-derived cells. {ECO:0000250|UniProtKB:D4YWD0}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:D4YWD0}. Target
CC       cell membrane {ECO:0000250|UniProtKB:D4YWD0}. Note=Deeply inserts into
CC       the lipid bilayer. {ECO:0000250|UniProtKB:D4YWD0}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Temporin subfamily. {ECO:0000305}.
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DR   EMBL; FN557008; CBH19885.1; -; mRNA.
DR   AlphaFoldDB; D5GRW4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
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; Cytolysis; Fungicide; Hemolysis;
KW   Immunity; Innate immunity; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..46
FT                   /evidence="ECO:0000305|PubMed:20308076"
FT                   /id="PRO_0000450303"
FT   PEPTIDE         47..62
FT                   /note="Temporin-SHe"
FT                   /evidence="ECO:0000269|PubMed:20308076"
FT                   /id="PRO_5003072910"
FT   MOD_RES         62
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000305|PubMed:20308076"
SQ   SEQUENCE   64 AA;  7173 MW;  A4559F2B3AF4B0BE CRC64;
     MFTLKKSLLL LFFLGTINLS LCEQERDAEE ERRDGTDESD VEVEKRFLPA LAGIAGLLGK
     IFGK