TPA_PELSA
ID TPA_PELSA Reviewed; 50 AA.
AC B3KYH4;
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-SHa {ECO:0000303|PubMed:24919960};
DE AltName: Full=Temporin-1Sa {ECO:0000303|PubMed:18584916};
DE Short=Temp-1Sa {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, AMIDATION AT PHE-48, SUBCELLULAR LOCATION, AND SYNTHESIS 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 BIOTECHNOLOGY.
RX PubMed=24919960; DOI=10.1002/psc.2654;
RA Lombana A., Raja Z., Casale S., Pradier C.M., Foulon T., Ladram A.,
RA Humblot V.;
RT "Temporin-SHa peptides grafted on gold surfaces display antibacterial
RT activity.";
RL J. Pept. Sci. 20:563-569(2014).
RN [3]
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 [4]
RP FUNCTION, AND MUTAGENESIS OF SER-38.
RX PubMed=28319176; DOI=10.1371/journal.pone.0174024;
RA Raja Z., Andre S., Abbassi F., Humblot V., Lequin O., Bouceba T.,
RA Correia I., Casale S., Foulon T., Sereno D., Oury B., Ladram A.;
RT "Insight into the mechanism of action of temporin-SHa, a new broad-spectrum
RT antiparasitic and antibacterial agent.";
RL PLoS ONE 12:e0174024-e0174024(2017).
RN [5]
RP FUNCTION AS ANTIVIRAL PEPTIDE, AND MUTAGENESIS OF SER-38.
RX PubMed=30669255; DOI=10.3390/v11010077;
RA Roy M., Lebeau L., Chessa C., Damour A., Ladram A., Oury B., Boutolleau D.,
RA Bodet C., Leveque N.;
RT "Comparison of anti-viral activity of frog skin anti-microbial peptides
RT temporin-SHa and [K3]SHa to LL-37 and Temporin-Tb against herpes simplex
RT virus type 1.";
RL Viruses 11:1-13(2019).
RN [6]
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 highly
CC potent activity against Gram-positive bacteria, and potent activity
CC Gram-negative bacteria and fungi (MIC=2-30 uM) (PubMed:18584916,
CC PubMed:18795798, PubMed:28319176). Acts through membranolytic mechanism
CC involving rapid membrane permeabilization and depolarization
CC (PubMed:28319176, PubMed:18795798). Shows a direct extra-cellular
CC antiviral activity probably through degradation of the viral envelope
CC (PubMed:30669255). Also shows a weak indirect antiviral activity by
CC inhibiting virus replication (PubMed:30669255). Also displays anti-
CC trypanosoma and anti-leishmania (prosmastigotes and axenic amastigotes)
CC activity through membranolytic mechanism (PubMed:18584916,
CC PubMed:25668079). Also induces apoptosis in leishmania promastigotes at
CC high peptide concentrations (PubMed:28319176). Shows moderate hemolytic
CC activity (LC(50)=25 uM) (PubMed:18584916, PubMed:18795798). In contrast
CC to many antibiotics, this peptide does not induce bacterial resistance
CC (PubMed:28319176). {ECO:0000269|PubMed:18584916,
CC ECO:0000269|PubMed:18795798, ECO:0000269|PubMed:25668079,
CC ECO:0000269|PubMed:28319176, ECO:0000269|PubMed:30669255}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18584916}. Target
CC cell membrane {ECO:0000269|PubMed:18795798}. Note=May insert into the
CC lipid bilayer with an in-plane (parallel) orientation.
CC {ECO:0000305|PubMed:18795798}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:18584916}.
CC -!- MASS SPECTROMETRY: Mass=1379.80; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18584916};
CC -!- BIOTECHNOLOGY: Attractive candidate as antimicrobial coating agent.
CC When this peptide is covalently grafted to a surface, the adhering
CC bacteria are most probably permeabilized (killed or at least damaged),
CC thus unable to grow. {ECO:0000305|PubMed:24919960}.
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=00898";
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DR EMBL; AM748899; CAO77282.1; -; mRNA.
DR AlphaFoldDB; B3KYH4; -.
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..35
FT /evidence="ECO:0000250|UniProtKB:P79874"
FT /id="PRO_0000450295"
FT PEPTIDE 36..48
FT /note="Temporin-SHa"
FT /evidence="ECO:0000269|PubMed:18584916"
FT /id="PRO_0000450296"
FT MOD_RES 48
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:18584916"
FT MUTAGEN 38
FT /note="S->K: Increase in antimicrobial specificity. Small
FT increase in potency against Gram-positive bacteria,
FT moderate increase in potency against Gram-negative bacteria
FT and fungi, small increase in antiviral activity, small
FT increase in anti-leishmania activity but no change in anti-
FT trypanosoma activity, small decrease of hemolytic activity
FT and no change in induction of bacterial resistance."
FT /evidence="ECO:0000269|PubMed:28319176,
FT ECO:0000269|PubMed:30669255"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:CAO77282.1"
SQ SEQUENCE 50 AA; 5699 MW; 18F93C4B279C1DEF CRC64;
FLGTINLSLC EQERDADEEE RRDEPNESNV EVEKRFLSGI VGMLGKLFGK
