TPF_PELSA
ID TPF_PELSA Reviewed; 45 AA.
AC D4YWD1;
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-SHf {ECO:0000303|PubMed:20308076};
DE Short=Temp-SHf {ECO:0000303|PubMed:20308076};
DE AltName: Full=Phe-rich antimicrobial peptide {ECO:0000303|PubMed:20308076};
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 36-43, FUNCTION,
RP SUBCELLULAR LOCATION, AMIDATION AT PHE-43, MASS SPECTROMETRY, SYNTHESIS OF
RP 36-43, AND STRUCTURE BY NMR OF 36-43 IN DPC MICELLES.
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, MUTAGENESIS OF SER-40, AND PHARMACEUTICAL.
RX PubMed=26181487; DOI=10.1021/acschembio.5b00495;
RA Andre S., Washington S.K., Darby E., Vega M.M., Filip A.D., Ash N.S.,
RA Muzikar K.A., Piesse C., Foulon T., O'Leary D.J., Ladram A.;
RT "Structure-activity relationship-based optimization of small temporin-SHf
RT analogs with potent antibacterial activity.";
RL ACS Chem. Biol. 10:2257-2266(2015).
RN [3]
RP FUNCTION, BIOTECHNOLOGY, AND MUTAGENESIS OF PHE-36; PHE-37; PHE-38 AND
RP PHE-43.
RX PubMed=27915018; DOI=10.1016/j.actbio.2016.11.061;
RA Mishra B., Lushnikova T., Golla R.M., Wang X., Wang G.;
RT "Design and surface immobilization of short anti-biofilm peptides.";
RL Acta Biomater. 49:316-328(2017).
CC -!- FUNCTION: Non-amphipathic alpha-helical antimicrobial peptide with
CC potent activity against some Gram-positive bacteria (including
CC methicillin-resistant Staphylococcus aureus (MRSA)), weak activity
CC against Gram-negative bacteria and no activity against fungi
CC (PubMed:20308076, PubMed:26181487, PubMed:27915018). Permeabilizates
CC membranes through a detergent-like effect probably via the carpet
CC mechanism (PubMed:20308076). More precisely, it strongly and
CC selectively perturbs anionic bilayers membranes by interacting with the
CC polar headgroups and the glycerol backbone region of the phospholipids,
CC hence disrupting the acyl chain packing of the bilayer
CC (PubMed:20308076). Is not active against Leishmania (promastigote and
CC axenic amastigote forms) (PubMed:20308076). Does not show hemolytic
CC activity (PubMed:20308076, PubMed:26181487). Does not show toxicity for
CC human THP-1-derived macrophages (PubMed:26181487).
CC {ECO:0000269|PubMed:20308076, ECO:0000269|PubMed:26181487,
CC ECO:0000269|PubMed:27915018}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20308076}. Target
CC cell membrane {ECO:0000269|PubMed:20308076}. Note=Inserts into the
CC lipid bilayer with an in-plane (parallel) orientation.
CC {ECO:0000269|PubMed:20308076}.
CC -!- MASS SPECTROMETRY: Mass=1075.6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20308076};
CC -!- BIOTECHNOLOGY: Has potential application in preventing biofilm
CC formation on medical devices, since it has the ability to prevent
CC methicillin-resistant S.aureus biofilm formation on the polyethylene
CC terephthalate (PET) surface, which is widely used in making prosthetic
CC heart valves cuffs and other bio devices.
CC {ECO:0000305|PubMed:27915018}.
CC -!- PHARMACEUTICAL: Owing to its short length, simple composition, and
CC broad spectrum of antimicrobial activity, this peptide is a promising
CC candidate for the development of a new class of antibiotics
CC (PubMed:20308076). The analog [p-(t)BuF(2), R5]SHf emerged as a highly
CC potent bactericidal ultrashort peptide, but weakly or non-cytotoxic
CC against mammalian cells (PubMed:26181487).
CC {ECO:0000269|PubMed:26181487, ECO:0000303|PubMed:20308076}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Temporin subfamily. {ECO:0000305|PubMed:20308076}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=01534";
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DR EMBL; AM903076; CAP17489.1; -; mRNA.
DR AlphaFoldDB; D4YWD1; -.
DR SMR; D4YWD1; -.
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: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 Hemolysis; Immunity; Innate immunity; Membrane; Pharmaceutical; 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:0000305|PubMed:20308076"
FT /id="PRO_0000450304"
FT PEPTIDE 36..43
FT /note="Temporin-SHf"
FT /evidence="ECO:0000269|PubMed:20308076"
FT /id="PRO_0000450305"
FT MOD_RES 43
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:20308076"
FT MUTAGEN 36
FT /note="F->W: In TetraF2W-RR; important increase in activity
FT against both Gram-positive (including MRSA) and Gram-
FT negative bacteria."
FT /evidence="ECO:0000269|PubMed:27915018"
FT MUTAGEN 37
FT /note="F->W: In TetraF2W-RR; important increase in activity
FT against both Gram-positive (including MRSA) and Gram-
FT negative bacteria."
FT /evidence="ECO:0000269|PubMed:27915018"
FT MUTAGEN 38
FT /note="F->W: In TetraF2W-RR; important increase in activity
FT against both Gram-positive (including MRSA) and Gram-
FT negative bacteria."
FT /evidence="ECO:0000269|PubMed:27915018"
FT MUTAGEN 40
FT /note="S->R: In combination with F-37 chemically modified
FT ([p-(t)BuF2, R5]SHf); important increase in activity
FT against both Gram-positive and Gram-negative bacteria,
FT small increase in cytotoxicity towards human cells, and no
FT change in hemolytic activity. In TetraF2W-RR; important
FT increase in activity against both Gram-positive (including
FT MRSA) and Gram-negative bacteria."
FT /evidence="ECO:0000269|PubMed:26181487"
FT MUTAGEN 43
FT /note="F->W: In TetraF2W-RR; important increase in activity
FT against both Gram-positive (including MRSA) and Gram-
FT negative bacteria."
FT /evidence="ECO:0000269|PubMed:27915018"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:CAP17489.1"
SQ SEQUENCE 45 AA; 5395 MW; DEECADCD31686857 CRC64;
FLGTINLSLC EEERDADEEE RRDEPDESNV EVKKRFFFLS RIFGK
