TPL_RANTE
ID TPL_RANTE Reviewed; 13 AA.
AC P57104;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Temporin-1Tl {ECO:0000303|PubMed:21586570};
DE Short=TL {ECO:0000303|PubMed:21586570};
DE AltName: Full=Temporin-L {ECO:0000303|PubMed:16867990, ECO:0000303|PubMed:9022710};
OS Rana temporaria (European common frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX NCBI_TaxID=8407;
RN [1]
RP PROTEIN SEQUENCE, AMIDATION AT LEU-13, AND SUBCELLULAR LOCATION.
RC TISSUE=Skin secretion;
RX PubMed=9022710; DOI=10.1111/j.1432-1033.1996.0788r.x;
RA Simmaco M., Mignogna G., Canofeni S., Miele R., Mangoni M.L., Barra D.;
RT "Temporins, antimicrobial peptides from the European red frog Rana
RT temporaria.";
RL Eur. J. Biochem. 242:788-792(1996).
RN [2]
RP FUNCTION.
RX PubMed=12133008; DOI=10.1042/bj20020806;
RA Rinaldi A.C., Mangoni M.L., Rufo A., Luzi C., Barra D., Zhao H.,
RA Kinnunen P.K., Bozzi A., Di Giulio A., Simmaco M.;
RT "Temporin L: antimicrobial, haemolytic and cytotoxic activities, and
RT effects on membrane permeabilization in lipid vesicles.";
RL Biochem. J. 368:91-100(2002).
RN [3]
RP FUNCTION, AND BIOASSAY.
RX PubMed=16801429; DOI=10.1128/aac.01553-05;
RA Giacometti A., Cirioni O., Ghiselli R., Mocchegiani F., Orlando F.,
RA Silvestri C., Bozzi A., Di Giulio A., Luzi C., Mangoni M.L., Barra D.,
RA Saba V., Scalise G., Rinaldi A.C.;
RT "Interaction of antimicrobial peptide temporin L with lipopolysaccharide in
RT vitro and in experimental rat models of septic shock caused by gram-
RT negative bacteria.";
RL Antimicrob. Agents Chemother. 50:2478-2486(2006).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16867990; DOI=10.1074/jbc.m606031200;
RA Rosenfeld Y., Barra D., Simmaco M., Shai Y., Mangoni M.L.;
RT "A synergism between temporins toward Gram-negative bacteria overcomes
RT resistance imposed by the lipopolysaccharide protective layer.";
RL J. Biol. Chem. 281:28565-28574(2006).
RN [5]
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 [6]
RP STRUCTURE BY NMR IN SDS AND DPC MICELLES, FUNCTION, AND MUTAGENESIS OF
RP GLN-3.
RX PubMed=18370376; DOI=10.1021/jm701604t;
RA Carotenuto A., Malfi S., Saviello M.R., Campiglia P., Gomez-Monterrey I.,
RA Mangoni M.L., Gaddi L.M., Novellino E., Grieco P.;
RT "A different molecular mechanism underlying antimicrobial and hemolytic
RT actions of temporins A and L.";
RL J. Med. Chem. 51:2354-2362(2008).
RN [7]
RP STRUCTURE BY NMR OF 47-59 IN COMPLEX WITH TEMPORIN-1TL IN LPS MICELLES,
RP FUNCTION, AND SUBUNIT.
RX PubMed=21586570; DOI=10.1074/jbc.m110.189662;
RA Bhunia A., Saravanan R., Mohanram H., Mangoni M.L., Bhattacharjya S.;
RT "NMR structures and interactions of temporin-1Tl and temporin-1Tb with
RT lipopolysaccharide micelles: mechanistic insights into outer membrane
RT permeabilization and synergistic activity.";
RL J. Biol. Chem. 286:24394-24406(2011).
RN [8]
RP STRUCTURE BY NMR IN SDS MICELLES, 3D-STRUCTURE MODELING IN BACTERIAL
RP MIMETIC MEMBRANES, AND FUNCTION.
RX PubMed=31358802; DOI=10.1038/s41598-019-47327-w;
RA Manzo G., Ferguson P.M., Hind C.K., Clifford M., Gustilo V.B., Ali H.,
RA Bansal S.S., Bui T.T., Drake A.F., Atkinson R.A., Sutton J.M., Lorenz C.D.,
RA Phoenix D.A., Mason A.J.;
RT "Temporin L and aurein 2.5 have identical conformations but subtly distinct
RT membrane and antibacterial activities.";
RL Sci. Rep. 9:10934-10934(2019).
CC -!- FUNCTION: Amphipathic alpha-helical antimicrobial peptide with potent
CC activity against both Gram-negative and Gram-positive bacteria, and
CC against fungi (PubMed:9022710, PubMed:12133008, PubMed:16867990,
CC PubMed:18370376, PubMed:31358802). Mainly acts by causing perturbation
CC of bilayer integrity of both neutral and negatively charged membranes,
CC probably by forming pore-like openings (PubMed:12133008,
CC PubMed:31358802). Also displays anti-leishmania activity by damaging
CC parasite membrane (By similarity). Shows hemolytic activity
CC (PubMed:12133008). Also shows cytotoxicity against cancer cell lines
CC (PubMed:12133008). Strongly binds to lipopolysaccharides (LPS) and its
CC lipid A portion (PubMed:16801429) (Probable). Improves temporin-A and
CC temporin-B activities by preventing their homo-oligomerization in LPS
CC (PubMed:16867990, PubMed:21586570). In vivo, its simultaneous
CC administration with beta-lactam antibiotics produces the highest
CC antimicrobial activities and the strongest reduction in plasma LPS and
CC TNF-alpha levels, resulting in the highest survival rates in rat models
CC of septic shock (PubMed:16801429). {ECO:0000250|UniProtKB:P56917,
CC ECO:0000250|UniProtKB:P79874, ECO:0000269|PubMed:12133008,
CC ECO:0000269|PubMed:16801429, ECO:0000269|PubMed:16867990,
CC ECO:0000269|PubMed:18370376, ECO:0000269|PubMed:21586570,
CC ECO:0000269|PubMed:31358802, ECO:0000269|PubMed:9022710,
CC ECO:0000305|PubMed:21586570}.
CC -!- SUBUNIT: Adopts monomeric helical conformations when bound to bacterial
CC (anionic) and eukaryotic (zwitterionic) model membranes (Probable). May
CC also oligomerize as homo-dimers or -trimers in Gram-negative bacteria
CC mimetic membranes, and from homo-dimers to -pentamers in Gram-positive
CC bacteria mimetic membranes (Probable). Adopts an antiparallel dimeric
CC helical structure when complexed with LPS micelles (PubMed:21586570).
CC This dimeric helical structure may interact with the lipid A domain of
CC LPS (Probable). {ECO:0000269|PubMed:21586570,
CC ECO:0000305|PubMed:18370376, ECO:0000305|PubMed:21586570,
CC ECO:0000305|PubMed:31358802}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9022710}. Target
CC cell membrane {ECO:0000269|PubMed:31358802}. Note=Contact and insertion
CC into membrane begin at the N-terminus. {ECO:0000269|PubMed:31358802}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:9022710}.
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=00101";
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DR PDB; 6GS5; NMR; -; A=1-13.
DR PDB; 7OS8; NMR; -; A=1-13.
DR PDB; 7OSD; NMR; -; A=1-13.
DR PDBsum; 6GS5; -.
DR PDBsum; 7OS8; -.
DR PDBsum; 7OSD; -.
DR BMRB; P57104; -.
DR SMR; P57104; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis; Immunity;
KW Innate immunity; Lipid-binding; Membrane; Secreted; Target cell membrane;
KW Target membrane.
FT PEPTIDE 1..13
FT /note="Temporin-1Tl"
FT /evidence="ECO:0000269|PubMed:9022710"
FT /id="PRO_0000043585"
FT MOD_RES 13
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:9022710"
FT MUTAGEN 3
FT /note="Q->P: No change in activity against Gram-positive
FT bacteria, weak increase in activity against Gram-negative
FT bacteria and fungi, and 2-fold decrease in hemolytic
FT activity."
FT /evidence="ECO:0000269|PubMed:18370376"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:6GS5"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:6GS5"
SQ SEQUENCE 13 AA; 1641 MW; 9EBDCB1FAFF7C325 CRC64;
FVQWFSKFLG RIL
