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Toll-like receptor 4 (CD antigen CD284)

 TLR4_CRIGR              Reviewed;         838 AA.
Q9WV82;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 107.
RecName: Full=Toll-like receptor 4;
AltName: CD_antigen=CD284;
Flags: Precursor;
Name=TLR4;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Macrophage;
PubMed=10683379; DOI=10.1172/JCI8541;
Lien E., Means T.K., Heine H., Yoshimura A., Kusumoto S., Fukase K.,
Fenton M.J., Oikawa M., Qureshi N., Monks B., Finberg R.W.,
Ingalls R.R., Golenbock D.T.;
"Toll-like receptor 4 imparts ligand-specific recognition of bacterial
lipopolysaccharide.";
J. Clin. Invest. 105:497-504(2000).
-!- FUNCTION: Cooperates with LY96 and CD14 to mediate the innate
immune response to bacterial lipopolysaccharide (LPS). Acts via
MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine
secretion and the inflammatory response. Also involved in LPS-
independent inflammatory responses triggered by free fatty acids,
such as palmitate. In complex with TLR6, promotes sterile
inflammation in monocytes/macrophages in response to oxidized low-
density lipoprotein (oxLDL) or amyloid-beta 42. In this context,
the initial signal is provided by oxLDL- or amyloid-beta 42-
binding to CD36. This event induces the formation of a heterodimer
of TLR4 and TLR6, which is rapidly internalized and triggers
inflammatory response, leading to the NF-kappa-B-dependent
production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling
pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well
as IL1B secretion. Binds electronegative LDL (LDL(-)) and mediates
the cytokine release induced by LDL(-) (By similarity).
{ECO:0000250|UniProtKB:O00206}.
-!- SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a
multi-protein complex containing at least CD14, LY96 and TLR4.
Binding to bacterial LPS leads to homodimerization. Interacts with
LY96 via the extracellular domain. Interacts with MYD88 and TIRAP
via their respective TIR domains. Interacts with TICAM2. Interacts
with NOX4. Interacts with CNPY3 and HSP90B1; this interaction is
required for proper folding in the endoplasmic reticulum.
Interacts with MAP3K21; this interaction leads to negative
regulation of TLR4 signaling. Interacts with CD36, following CD36
stimulation by oxLDL or amyloid-beta 42, and forms a heterodimer
with TLR6. The trimeric complex is internalized and triggers
inflammatory response. LYN kinase activity facilitates TLR4-TLR6
heterodimerization and signal initiation. Interacts with TICAM1 in
response to LPS in a WDFY1-dependent manner. Interacts with WDFY1
in response to LPS. Interacts with SMPDL3B. Interacts with
CEACAM1; upon lipopolysaccharide stimulation, forms a complex
including TLR4 and the phosphorylated form of SYK and CEACAM1,
which in turn, recruits PTPN6 that dephosphorylates SYK, reducing
the production of reactive oxygen species (ROS) and lysosome
disruption, which in turn, reduces the activity of the
inflammasome (By similarity). {ECO:0000250|UniProtKB:O00206,
ECO:0000250|UniProtKB:Q9QUK6}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:O00206}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:O00206}. Note=Upon complex
formation with CD36 and TLR6, internalized through dynamin-
dependent endocytosis. {ECO:0000250|UniProtKB:O00206}.
-!- TISSUE SPECIFICITY: Expressed in macrophages.
{ECO:0000269|PubMed:10683379}.
-!- DOMAIN: The TIR domain mediates interaction with NOX4.
{ECO:0000250|UniProtKB:O00206}.
-!- SIMILARITY: Belongs to the Toll-like receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF153676; AAD41891.1; -; mRNA.
RefSeq; NP_001233691.1; NM_001246762.1.
ProteinModelPortal; Q9WV82; -.
SMR; Q9WV82; -.
Ensembl; ENSCGRT00000005451; ENSCGRP00000005358; ENSCGRG00000003919.
Ensembl; ENSCGRT00001018473; ENSCGRP00001014236; ENSCGRG00001015165.
GeneID; 100689329; -.
KEGG; cge:100689329; -.
CTD; 7099; -.
HOVERGEN; HBG018823; -.
KO; K10160; -.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
GO; GO:0046696; C:lipopolysaccharide receptor complex; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
GO; GO:0001875; F:lipopolysaccharide receptor activity; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0005102; F:receptor binding; IEA:Ensembl.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
GO; GO:0002322; P:B cell proliferation involved in immune response; IEA:Ensembl.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0071223; P:cellular response to lipoteichoic acid; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; IEA:Ensembl.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
GO; GO:0032497; P:detection of lipopolysaccharide; ISS:UniProtKB.
GO; GO:0007252; P:I-kappaB phosphorylation; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0032609; P:interferon-gamma production; IEA:Ensembl.
GO; GO:0050702; P:interleukin-1 beta secretion; ISS:UniProtKB.
GO; GO:0060729; P:intestinal epithelial structure maintenance; IEA:Ensembl.
GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IEA:Ensembl.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IEA:Ensembl.
GO; GO:0032707; P:negative regulation of interleukin-23 production; IEA:Ensembl.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0002537; P:nitric oxide production involved in inflammatory response; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IEA:Ensembl.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; IEA:Ensembl.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IEA:Ensembl.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IEA:Ensembl.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl.
GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
GO; GO:0070430; P:positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway; IEA:Ensembl.
GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IEA:Ensembl.
GO; GO:1903223; P:positive regulation of oxidative stress-induced neuron death; IEA:Ensembl.
GO; GO:0010572; P:positive regulation of platelet activation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IEA:Ensembl.
GO; GO:0002730; P:regulation of dendritic cell cytokine production; IEA:Ensembl.
GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:InterPro.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; IEA:Ensembl.
Gene3D; 3.40.50.10140; -; 1.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR000157; TIR_dom.
InterPro; IPR027168; TLR4.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR44568; PTHR44568; 1.
Pfam; PF13516; LRR_6; 1.
Pfam; PF13855; LRR_8; 2.
Pfam; PF01582; TIR; 1.
SMART; SM00369; LRR_TYP; 9.
SMART; SM00082; LRRCT; 1.
SMART; SM00255; TIR; 1.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS51450; LRR; 12.
PROSITE; PS50104; TIR; 1.
2: Evidence at transcript level;
Cell membrane; Disulfide bond; Glycoprotein; Immunity;
Inflammatory response; Innate immunity; Leucine-rich repeat; Membrane;
Receptor; Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 838 Toll-like receptor 4.
/FTId=PRO_0000034718.
TOPO_DOM 26 629 Extracellular. {ECO:0000255}.
TRANSMEM 630 650 Helical. {ECO:0000255}.
TOPO_DOM 651 838 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 53 LRRNT.
REPEAT 54 75 LRR 1.
REPEAT 78 99 LRR 2.
REPEAT 102 123 LRR 3.
REPEAT 126 147 LRR 4.
REPEAT 150 171 LRR 5.
REPEAT 175 198 LRR 6.
REPEAT 204 224 LRR 7.
REPEAT 226 235 LRR 8.
REPEAT 372 392 LRR 9.
REPEAT 398 420 LRR 10.
REPEAT 421 442 LRR 11.
REPEAT 446 468 LRR 12.
REPEAT 470 493 LRR 13.
REPEAT 495 516 LRR 14.
REPEAT 519 539 LRR 15.
REPEAT 543 564 LRR 16.
DOMAIN 576 627 LRRCT.
DOMAIN 670 816 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 492 492 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 495 495 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 572 572 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 39 {ECO:0000250|UniProtKB:O00206}.
DISULFID 280 304 {ECO:0000250|UniProtKB:O00206}.
DISULFID 388 389 {ECO:0000250|UniProtKB:O00206}.
DISULFID 580 606 {ECO:0000250|UniProtKB:O00206}.
DISULFID 582 625 {ECO:0000250|UniProtKB:O00206}.
SEQUENCE 838 AA; 96278 MW; 129B33596E908B48 CRC64;
MMPSFCLAGT LMMALFLSSL RPESLDPCVE VDSNTSYQCM DRNLNKIPDN IPSSVKHLDL
SFNPLKTLGS HSFFNFPELK LLDLSRCEIE TIEDKAYQGL HQLTTLILTG NPIQNLSKGT
FSGLANLQNL VAVEIKLASL DSLPIGHLVT LKKLNVAHNL IHSFKLPEYF SNLTNLEHLD
LSNNYIQTIY YTDLQTLREN PQLNLSLELS LNPIDFIQPG AFQGIRLHEL TLRSNFNSTN
VMKTCIHNLD GLQVHRLILG EFKNERNVER FDRYVIEGLC KVTIEEFRFT YANEFSEDIT
DFDCLANVSA MSLANVYLKR LEDIPKYFKW QTLAVIRCEL KQFPPLELPF LKRLIFITNK
GATSFPEVNL PSLTFLDLSG NGMSFRGCCS YTDLGARSLK HLDLSFNGVI SMSENFMGLE
QLEYLDFQHS TLKKATEFSM FLPLEKLLYL DISYTNTKID FNGIFFGLTS LNTLKMAGNS
FKDNILSNVF TNTTNLTFLD ISKCQLQQVS WGVFDTLHRL ELLNMSHNNL LLLDLFHYKQ
LHSLKTLDCS FNHIETSKGI MQHFPKSLAF LNLTNNPFAC ICEHQNFLQW VKDQRLFLVK
TEQMTCATPV EMKDSLVLDF RNATCYVQKT IISVSVISVL VVSTIAFLVY KFYFHLILIA
GCKKYSRGES IYDAFVIYSS QDEDWVRNEL VKNLEEGVPP FQLCLHYRDF IPGVAIAANI
IQEGFHKSRK VIVVVSRHFI QSRWCIFEYE IAQTWQFLSS HSGIIFIVLE KVEKSLLKQQ
VELYRLLSRN TYLEWEDNAL GRHIFWRRLK KALLDGRAWN PEGATEAENN QQETTTSI


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