TLR5_MOUSE
ID TLR5_MOUSE Reviewed; 859 AA.
AC Q9JLF7;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Toll-like receptor 5;
DE Flags: Precursor;
GN Name=Tlr5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS.
RC STRAIN=C57BL/6J, and MOLF/EiJ; TISSUE=Liver;
RX PubMed=10756091; DOI=10.1006/geno.2000.6115;
RA Sebastiani G., Leveque G., Lariviere L., Laroche L., Skamene E., Gros P.,
RA Malo D.;
RT "Cloning and characterization of the murine Toll-like receptor 5 (Tlr5)
RT gene: sequence and mRNA expression studies in Salmonella-susceptible
RT MOLF/Ei mice.";
RL Genomics 64:230-240(2000).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=30089902; DOI=10.1038/s41586-018-0395-5;
RA Fulde M., Sommer F., Chassaing B., van Vorst K., Dupont A., Hensel M.,
RA Basic M., Klopfleisch R., Rosenstiel P., Bleich A., Baeckhed F.,
RA Gewirtz A.T., Hornef M.W.;
RT "Neonatal selection by Toll-like receptor 5 influences long-term gut
RT microbiota composition.";
RL Nature 560:489-493(2018).
CC -!- FUNCTION: Pattern recognition receptor (PRR) located on the cell
CC surface that participates in the activation of innate immunity and
CC inflammatory response. Recognizes small molecular motifs named
CC pathogen-associated molecular pattern (PAMPs) expressed by pathogens
CC and microbe-associated molecular patterns (MAMPs) usually expressed by
CC resident microbiota. Upon ligand binding such as bacterial flagellins,
CC recruits intracellular adapter proteins MYD88 and TRIF leading to NF-
CC kappa-B activation, cytokine secretion and induction of the
CC inflammatory response. Plays thereby an important role in the
CC relationship between the intestinal epithelium and enteric microbes and
CC contributes to the gut microbiota composition throughout life.
CC {ECO:0000250|UniProtKB:O60602, ECO:0000269|PubMed:30089902}.
CC -!- SUBUNIT: Homodimer. Interacts with MYD88 (via TIR domain). Interacts
CC with TICAM1 (via TIR domain). Interacts with UNC93B1; this interaction
CC is essential for proper TLR5 localization to the plasma membrane.
CC {ECO:0000250|UniProtKB:O60602}.
CC -!- INTERACTION:
CC Q9JLF7; Q56086: flag; Xeno; NbExp=2; IntAct=EBI-6548397, EBI-6548623;
CC Q9JLF7; A0A0H3NMJ6: fliC; Xeno; NbExp=2; IntAct=EBI-6548397, EBI-6548383;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver (PubMed:30089902).
CC Detected in lung and at very low levels in most other tissues.
CC {ECO:0000269|PubMed:30089902}.
CC -!- PTM: Phosphorylated at Tyr-799 upon flagellin binding; required for
CC signaling. {ECO:0000250}.
CC -!- POLYMORPHISM: The TLR5 gene lies in a locus that is associated with
CC susceptibility to Salmonella. Inbred strains of mice can be classified
CC into 3 categories according to their resistance to infection with
CC S.typhimurium: susceptible (BALB/c, C57BL/6, C3H/He), intermediate
CC (DBA/2, C75L) and resistant (A, CBA). The strain MOLF/Ei is highly
CC susceptible to the infection, has an unique TLR5 haplotype and a lower
CC expression of TRL5.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit a markedly altered enteric
CC microbiota composition, with increased levels of fecal flagellin.
CC {ECO:0000269|PubMed:30089902}.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
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DR EMBL; AF186107; AAF65625.1; -; mRNA.
DR CCDS; CCDS35815.1; -.
DR RefSeq; NP_058624.2; NM_016928.3.
DR AlphaFoldDB; Q9JLF7; -.
DR SMR; Q9JLF7; -.
DR BioGRID; 207467; 2.
DR IntAct; Q9JLF7; 6.
DR STRING; 10090.ENSMUSP00000106625; -.
DR GlyGen; Q9JLF7; 9 sites.
DR iPTMnet; Q9JLF7; -.
DR PhosphoSitePlus; Q9JLF7; -.
DR PaxDb; Q9JLF7; -.
DR PRIDE; Q9JLF7; -.
DR ProteomicsDB; 259515; -.
DR DNASU; 53791; -.
DR GeneID; 53791; -.
DR KEGG; mmu:53791; -.
DR CTD; 7100; -.
DR MGI; MGI:1858171; Tlr5.
DR eggNOG; KOG4641; Eukaryota.
DR InParanoid; Q9JLF7; -.
DR PhylomeDB; Q9JLF7; -.
DR BioGRID-ORCS; 53791; 0 hits in 56 CRISPR screens.
DR PRO; PR:Q9JLF7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JLF7; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005149; F:interleukin-1 receptor binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0034123; P:positive regulation of toll-like receptor signaling pathway; ISO:MGI.
DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; IEA:InterPro.
DR GO; GO:0002224; P:toll-like receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR027176; TLR5.
DR InterPro; IPR017241; Toll-like_receptor.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR24365; PTHR24365; 1.
DR PANTHER; PTHR24365:SF525; PTHR24365:SF525; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01582; TIR; 1.
DR PIRSF; PIRSF037595; Toll-like_receptor; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS51450; LRR; 14.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Immunity; Inflammatory response;
KW Innate immunity; Leucine-rich repeat; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..859
FT /note="Toll-like receptor 5"
FT /id="PRO_0000034730"
FT TOPO_DOM 27..641
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..859
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 45..69
FT /note="LRR 1"
FT REPEAT 72..94
FT /note="LRR 2"
FT REPEAT 96..118
FT /note="LRR 3"
FT REPEAT 121..144
FT /note="LRR 4"
FT REPEAT 147..167
FT /note="LRR 5"
FT REPEAT 172..193
FT /note="LRR 6"
FT REPEAT 198..212
FT /note="LRR 7"
FT REPEAT 215..230
FT /note="LRR 8"
FT REPEAT 235..236
FT /note="LRR 9"
FT REPEAT 261..285
FT /note="LRR 11"
FT REPEAT 290..302
FT /note="LRR 12"
FT REPEAT 314..335
FT /note="LRR 13"
FT REPEAT 338..356
FT /note="LRR 14"
FT REPEAT 386..402
FT /note="LRR 16"
FT REPEAT 413..432
FT /note="LRR 17"
FT REPEAT 450..471
FT /note="LRR 18"
FT REPEAT 475..496
FT /note="LRR 19"
FT REPEAT 504..525
FT /note="LRR 20"
FT REPEAT 528..547
FT /note="LRR 21"
FT REPEAT 550..568
FT /note="LRR 22"
FT DOMAIN 580..632
FT /note="LRRCT"
FT DOMAIN 692..837
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT MOD_RES 799
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60602"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 584..611
FT /evidence="ECO:0000250"
FT DISULFID 586..630
FT /evidence="ECO:0000250"
FT VARIANT 226
FT /note="G -> D (in strain: MOLF/Ei)"
FT VARIANT 399
FT /note="A -> T (in strain: MOLF/Ei)"
FT VARIANT 470
FT /note="P -> T (in strain: MOLF/Ei)"
FT VARIANT 482
FT /note="T -> A (in strain: MOLF/Ei)"
FT VARIANT 609
FT /note="V -> M (in strain: MOLF/Ei)"
FT VARIANT 619
FT /note="G -> A (in strain: MOLF/Ei)"
FT VARIANT 835
FT /note="G -> E (in strain: MOLF/Ei)"
FT VARIANT 843
FT /note="G -> A (in strain: MOLF/Ei)"
SQ SEQUENCE 859 AA; 97627 MW; 74CD915EA3F0275F CRC64;
MACQLDLLIG VIFMASPVLV ISPCSSDGRI AFFRGCNLTQ IPWILNTTTE RLLLSFNYIS
MVVATSFPLL ERLQLLELGT QYANLTIGPG AFRNLPNLRI LDLGQSQIEV LNRDAFQGLP
HLLELRLFSC GLSSAVLSDG YFRNLYSLAR LDLSGNQIHS LRLHSSFREL NSLSDVNFAF
NQIFTICEDE LEPLQGKTLS FFGLKLTKLF SRVSVGWETC RNPFRGVRLE TLDLSENGWT
VDITRNFSNI IQGSQISSLI LKHHIMGPGF GFQNIRDPDQ STFASLARSS VLQLDLSHGF
IFSLNPRLFG TLKDLKMLNL AFNKINKIGE NAFYGLDSLQ VLNLSYNLLG ELYNSNFYGL
PRVAYVDLQR NHIGIIQDQT FRLLKTLQTL DLRDNALKAI GFIPSIQMVL LGGNKLVHLP
HIHFTANFLE LSENRLENLS DLYFLLRVPQ LQFLILNQNR LSSCKAAHTP SENPSLEQLF
LTENMLQLAW ETGLCWDVFQ GLSRLQILYL SNNYLNFLPP GIFNDLVALR MLSLSANKLT
VLSPGSLPAN LEILDISRNQ LLCPDPALFS SLRVLDITHN EFVCNCELST FISWLNQTNV
TLFGSPADVY CMYPNSLLGG SLYNISTEDC DEEEAMRSLK FSLFILCTVT LTLFLVITLV
VIKFRGICFL CYKTIQKLVF KDKVWSLEPG AYRYDAYFCF SSKDFEWAQN ALLKHLDAHY
SSRNRLRLCF EERDFIPGEN HISNIQAAVW GSRKTVCLVS RHFLKDGWCL EAFRYAQSRS
LSDLKSILIV VVVGSLSQYQ LMRHETIRGF LQKQQYLRWP EDLQDVGWFL DKLSGCILKE
EKGKKRSSSI QLRTIATIS
