ID   TPC_PELSA               Reviewed;          50 AA.
AC   B3KYH6;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Temporin-SHc {ECO:0000303|PubMed:18795798};
DE   AltName: Full=Temporin-1Sc {ECO:0000303|PubMed:18584916};
DE            Short=Temp-1Sc {ECO:0000303|PubMed:18584916};
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], PROTEIN SEQUENCE OF 36-48, FUNCTION, MASS
RP   SPECTROMETRY, SUBCELLULAR LOCATION, AMIDATION AT PHE-48, AND SYNTHESISI OF
RP   36-48.
RC   TISSUE=Skin;
RX   PubMed=18584916; DOI=10.1016/j.peptides.2008.05.008;
RA   Abbassi F., Oury B., Blasco T., Sereno D., Bolbach G., Nicolas P., Hani K.,
RA   Amiche M., Ladram A.;
RT   "Isolation, characterization and molecular cloning of new temporins from
RT   the skin of the North African ranid Pelophylax saharica.";
RL   Peptides 29:1526-1533(2008).
RN   [2]
RP   STRUCTURE BY NMR OF 36-48 IN SDS MICELLES, FUNCTION, AND SYNTHESIS OF
RP   36-48.
RX   PubMed=18795798; DOI=10.1021/bi8006884;
RA   Abbassi F., Galanth C., Amiche M., Saito K., Piesse C., Zargarian L.,
RA   Hani K., Nicolas P., Lequin O., Ladram A.;
RT   "Solution structure and model membrane interactions of temporins-SH,
RT   antimicrobial peptides from amphibian skin. A NMR spectroscopy and
RT   differential scanning calorimetry study.";
RL   Biochemistry 47:10513-10525(2008).
CC   -!- FUNCTION: Amphipathic alpha-helical antimicrobial peptide with potent
CC       activity against some Gram-positive bacteria (MIC=4->80 uM), potent
CC       activity against fungi (MIC=10-20 uM), and no activity against Gram-
CC       negative bacteria (PubMed:18584916, PubMed:18795798). Does not display
CC       anti-leishmania activity (PubMed:18584916). Does not show hemolytic
CC       activity (LC(50)>80 uM) (PubMed:18584916, PubMed:18795798).
CC       {ECO:0000269|PubMed:18584916, ECO:0000269|PubMed:18795798}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18584916}. Target
CC       cell membrane {ECO:0000305|PubMed:18795798}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:18584916}.
CC   -!- MASS SPECTROMETRY: Mass=1463.78; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18584916};
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=00900";
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DR   EMBL; AM748901; CAO77284.1; -; mRNA.
DR   AlphaFoldDB; B3KYH6; -.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; 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; Fungicide;
KW   Immunity; Innate immunity; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          <1..10
FT                   /evidence="ECO:0000250|UniProtKB:P79874"
FT   PROPEP          11..35
FT                   /evidence="ECO:0000305|PubMed:18584916"
FT                   /id="PRO_0000450299"
FT   PEPTIDE         36..48
FT                   /note="Temporin-SHc"
FT                   /evidence="ECO:0000269|PubMed:18584916"
FT                   /id="PRO_0000450300"
FT   MOD_RES         48
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:18584916"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:CAO77284.1"
SQ   SEQUENCE   50 AA;  5712 MW;  95691D47D3F1DDE3 CRC64;
     FLGTINLSLC EQERDADEEE RRDEPDGSNV EVEKRFLSHI AGFLSNLFGK