ID   TPD_PELSA               Reviewed;          53 AA.
AC   D4YWD0;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Temporin-SHd {ECO:0000303|PubMed:20308076, ECO:0000303|PubMed:23116712};
DE            Short=Temp-SHd {ECO:0000303|PubMed:20308076, ECO:0000303|PubMed:23116712};
DE   AltName: Full=Temporin-1Sd {ECO:0000312|EMBL:CAP17488.1};
DE            Short=Temp-1Sd {ECO:0000312|EMBL:CAP17488.1};
DE   Flags: Precursor; Fragment;
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-51.
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).
RN   [2]
RP   FUNCTION, PROTEIN SEQUENCE OF 35-51, MASS SPECTROMETRY, SUBCELLULAR
RP   LOCATION, AND SYNTHESIS OF 35-51.
RX   PubMed=23116712; DOI=10.1016/j.biochi.2012.10.015;
RA   Abbassi F., Raja Z., Oury B., Gazanion E., Piesse C., Sereno D.,
RA   Nicolas P., Foulon T., Ladram A.;
RT   "Antibacterial and leishmanicidal activities of temporin-SHd, a 17-residue
RT   long membrane-damaging peptide.";
RL   Biochimie 95:388-399(2013).
CC   -!- FUNCTION: Non-amphipathic mildly cationic alpha-helical antimicrobial
CC       peptide with potent activity against Gram-positive (including
CC       methicillin-resistant Staphylococcus aureus (MRSA)) and Gram-negative
CC       bacteria, and some fungi, as well as against Trypanosoma and Leishmania
CC       (both promastigote and amastigote forms) (PubMed:23116712). Strongly
CC       and selectively perturbs anionic bilayer membranes by interacting with
CC       the polar head groups and acyl region of the phospholipids, with
CC       formation of regions of two coexisting phases, one phase rich in
CC       peptide and the other lipid-rich (PubMed:23116712). Shows low hemolytic
CC       activity (LC(50)=44 uM) and a low toxicity for human monocytes THP-1
CC       and THP-1-derived macrophages (PubMed:23116712). Is not toxic to human
CC       hepatoma-derived cells (PubMed:23116712).
CC       {ECO:0000269|PubMed:23116712}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23116712}. Target
CC       cell membrane {ECO:0000269|PubMed:23116712}. Note=Deeply inserts into
CC       the lipid bilayer. {ECO:0000305|PubMed:23116712}.
CC   -!- MASS SPECTROMETRY: Mass=1657; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23116712};
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=02118";
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DR   EMBL; AM903075; CAP17488.1; -; mRNA.
DR   AlphaFoldDB; D4YWD0; -.
DR   SMR; D4YWD0; -.
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; Direct protein sequencing;
KW   Fungicide; Hemolysis; Immunity; Innate immunity; Membrane; Secreted;
KW   Signal; Target cell membrane; Target membrane.
FT   SIGNAL          <1..10
FT                   /evidence="ECO:0000250|UniProtKB:P79874"
FT   PROPEP          11..34
FT                   /evidence="ECO:0000305|PubMed:20308076"
FT                   /id="PRO_0000450301"
FT   PEPTIDE         35..51
FT                   /note="Temporin-SHd"
FT                   /evidence="ECO:0000269|PubMed:20308076"
FT                   /id="PRO_0000450302"
FT   MOD_RES         51
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:20308076"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:CAP17488.1"
SQ   SEQUENCE   53 AA;  5821 MW;  7E742B177EF3CCBB CRC64;
     FLGTINLSLC EQERDADEEK RDEPDESDVE VEKRFLPAAL AGIGGILGKL FGK