Q9QUK6 (TLR4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Toll-like receptor 4

Alternative name(s):
CD_antigen=CD284

Gene names

Name:	Tlr4
Synonyms:	Lps

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	835 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity. Ref.7
Subunit structure	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 NOX4 By similarity. Interacts with CNPY3 and HSP90B1; this interaction is required for proper folding in the endoplasmic reticulum. Interacts with MLK4; this interaction leads to negative regulation of TLR4 signaling By similarity. Ref.8 Ref.9
Subcellular location	Membrane; Single-pass type I membrane protein By similarity.
Tissue specificity	Highly expressed in heart, spleen, lung and muscle. Lower levels are found in liver and kidney.
Domain	The TIR domain mediates interaction with NOX4 By similarity.
Polymorphism	Interstrain analyzes reveals that TLR4 is a polymorphic protein and that the extracellular domain is far more variable than the cytoplasmic domain, which is variable at the C-terminal.
Involvement in disease	The protein is encoded by the Lps locus, an important susceptibility locus, influencing the propensity to develop a disseminated Gram-negative infection.
Sequence similarities	Belongs to the Toll-like receptor family. Contains 19 LRR (leucine-rich) repeats. Contains 1 LRRCT domain. Contains 1 TIR domain.

Ontologies

Keywords
Biological process	Immunity Inflammatory response Innate immunity
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell proliferation involved in immune response Inferred from mutant phenotype PubMed 10880523. Source: MGI I-kappaB phosphorylation Inferred from electronic annotation. Source: Compara MyD88-dependent toll-like receptor signaling pathway Inferred from electronic annotation. Source: InterPro activation of MAPK activity Inferred from mutant phenotype PubMed 20051628. Source: BHF-UCL activation of NF-kappaB-inducing kinase activity Non-traceable author statement PubMed 11490012. Source: UniProtKB cellular response to lipoteichoic acid Inferred from mutant phenotype PubMed 10549626. Source: MGI cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara defense response to Gram-negative bacterium Inferred from mutant phenotype PubMed 15661922. Source: MGI detection of lipopolysaccharide Traceable author statement PubMed 15356140. Source: BHF-UCL innate immune response Traceable author statement PubMed 15356140. Source: BHF-UCL interferon-gamma production Inferred from genetic interaction PubMed 11489994. Source: MGI intestinal epithelial structure maintenance Inferred from mutant phenotype PubMed 20051628. Source: BHF-UCL macrophage activation Inferred from sequence or structural similarity PubMed 10835634. Source: UniProtKB mast cell activation Non-traceable author statement PubMed 11490012PubMed 11739561. Source: UniProtKB negative regulation of ERK1 and ERK2 cascade Inferred from mutant phenotype PubMed 20051628. Source: BHF-UCL negative regulation of interferon-gamma production Inferred from mutant phenotype PubMed 20051628. Source: BHF-UCL negative regulation of interleukin-17 production Inferred from mutant phenotype PubMed 18203139PubMed 20051628. Source: BHF-UCL negative regulation of interleukin-23 production Inferred from mutant phenotype PubMed 18203139. Source: BHF-UCL negative regulation of interleukin-6 production Inferred from mutant phenotype PubMed 18203139PubMed 20051628. Source: BHF-UCL negative regulation of tumor necrosis factor production Inferred from mutant phenotype PubMed 20051628. Source: BHF-UCL nitric oxide production involved in inflammatory response Inferred from mutant phenotype PubMed 10623794. Source: MGI positive regulation of B cell proliferation Inferred from mutant phenotype PubMed 10549626. Source: MGI positive regulation of ERK1 and ERK2 cascade Inferred from direct assay PubMed 18261938. Source: MGI positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay PubMed 16260493PubMed 18261938PubMed 19734906. Source: MGI positive regulation of JNK cascade Inferred from direct assay PubMed 16260493PubMed 18261938. Source: MGI positive regulation of MHC class II biosynthetic process Inferred from mutant phenotype PubMed 10549626. Source: MGI positive regulation of NF-kappaB import into nucleus Inferred from electronic annotation. Source: Compara positive regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of chemokine production Inferred from direct assay PubMed 15356140. Source: BHF-UCL positive regulation of interferon-alpha production Inferred from direct assay PubMed 15356140. Source: BHF-UCL positive regulation of interferon-beta biosynthetic process Inferred from mutant phenotype PubMed 15661922. Source: MGI positive regulation of interferon-beta production Inferred from direct assay PubMed 15356140. Source: BHF-UCL positive regulation of interferon-gamma production Inferred from mutant phenotype PubMed 18203139. Source: BHF-UCL positive regulation of interleukin-1 biosynthetic process Non-traceable author statement PubMed 11490012. Source: UniProtKB positive regulation of interleukin-1 production Inferred from direct assay PubMed 15356140. Source: BHF-UCL positive regulation of interleukin-10 production Inferred from direct assay PubMed 15356140. Source: BHF-UCL positive regulation of interleukin-12 biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of interleukin-12 production Inferred from direct assay PubMed 15356140. Source: BHF-UCL positive regulation of interleukin-13 biosynthetic process Non-traceable author statement PubMed 11490012. Source: UniProtKB positive regulation of interleukin-6 biosynthetic process Non-traceable author statement PubMed 11490012. Source: UniProtKB positive regulation of interleukin-6 production Inferred from direct assay PubMed 15356140. Source: BHF-UCL positive regulation of interleukin-8 biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of interleukin-8 production Inferred from electronic annotation. Source: Compara positive regulation of macrophage cytokine production Inferred from mutant phenotype PubMed 10549626. Source: MGI positive regulation of nitric oxide biosynthetic process Inferred from mutant phenotype PubMed 10549626. Source: MGI positive regulation of nitric-oxide synthase biosynthetic process Inferred from direct assay PubMed 15356140. Source: BHF-UCL positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway Inferred from direct assay PubMed 18261938. Source: MGI positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway Inferred from direct assay PubMed 18261938. Source: MGI positive regulation of platelet activation Inferred from mutant phenotype PubMed 16514062. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 15356140. Source: BHF-UCL positive regulation of tumor necrosis factor biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of tumor necrosis factor production Inferred from direct assay PubMed 15356140. Source: BHF-UCL regulation of cytokine secretion Inferred from electronic annotation. Source: InterPro regulation of inflammatory response Inferred from mutant phenotype PubMed 18203139. Source: BHF-UCL toll-like receptor 4 signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular_component	external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from electronic annotation. Source: Compara lipopolysaccharide receptor complex Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	lipopolysaccharide receptor activity Inferred from sequence or structural similarity. Source: UniProtKB transmembrane signaling receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ly96	Q9JHF9	3	EBI-1534575,EBI-1534566

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Chain

26 – 835

810

Toll-like receptor 4

PRO_0000034723

Regions

Topological domain

26 – 638

613

Extracellular Potential

Transmembrane

639 – 659

21

Helical; Potential

Topological domain

660 – 835

176

Cytoplasmic Potential

Repeat

54 – 75

22

LRR 1

Repeat

78 – 99

22

LRR 2

Repeat

102 – 123

22

LRR 3

Repeat

126 – 147

22

LRR 4

Repeat

150 – 171

22

LRR 5

Repeat

175 – 198

24

LRR 6

Repeat

204 – 224

21

LRR 7

Repeat

226 – 247

22

LRR 8

Repeat

248 – 269

22

LRR 9

Repeat

329 – 349

21

LRR 10

Repeat

350 – 370

21

LRR 11

Repeat

372 – 392

21

LRR 12

Repeat

398 – 420

23

LRR 13

Repeat

421 – 442

22

LRR 14

Repeat

446 – 467

22

LRR 15

Repeat

470 – 490

21

LRR 16

Repeat

495 – 516

22

LRR 17

Repeat

519 – 540

22

LRR 18

Repeat

543 – 564

22

LRR 19

Domain

576 – 627

52

LRRCT

Domain

670 – 816

147

TIR

Amino acid modifications

Glycosylation

34

1

N-linked (GlcNAc...) Ref.11

Glycosylation

75

1

N-linked (GlcNAc...) Ref.11

Glycosylation

172

1

N-linked (GlcNAc...) Ref.11

Glycosylation

204

1

N-linked (GlcNAc...) Ref.11

Glycosylation

237

1

N-linked (GlcNAc...) Ref.11

Glycosylation

307

1

N-linked (GlcNAc...) Ref.11

Glycosylation

492

1

N-linked (GlcNAc...) Ref.11

Glycosylation

495

1

N-linked (GlcNAc...)

Glycosylation

524

1

N-linked (GlcNAc...) Ref.11

Glycosylation

572

1

N-linked (GlcNAc...) Ref.11

Glycosylation

575

1

N-linked (GlcNAc...) Potential

Glycosylation

613

1

N-linked (GlcNAc...) Potential

Glycosylation

621

1

N-linked (GlcNAc...) Potential

Glycosylation

622

1

N-linked (GlcNAc...) Potential

Disulfide bond

28 ↔ 39

Disulfide bond

280 ↔ 304

Disulfide bond

388 ↔ 389

Disulfide bond

580 ↔ 606

Disulfide bond

582 ↔ 625

Natural variations

Natural variant

94

1

D → N in strain: KK/HLJ. Ref.5

Natural variant

209

1

M → I in strain: A/J, BALB/cJ, P/J, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK. Ref.5

Natural variant

219

1

D → G in strain: SEA/GNJ. Ref.5

Natural variant

254

1

V → I in strain: A/J, BALB/cJ and SEA/GNJ. Ref.5

Natural variant

423

1

Q → L in strain: SEA/GNJ. Ref.5

Natural variant

477

1

A → S in strain: P/J. Ref.5

Natural variant

516

1

T → A in strain: LP/J. Ref.5

Natural variant

593

1

E → D in strain: A/J, BALB/cJ, P/J, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK. Ref.5

Natural variant

600

1

N → I in strain: KK/HLJ. Ref.5

Natural variant

607

1

A → V in strain: P/J. Ref.5

Natural variant

637

1

V → I in strain: P/J. Ref.5

Natural variant

712

1

P → H in Lps-tolerant mice. Ref.2 Ref.3

Natural variant

761

1

R → H in strain: A/J, BALB/cJ, SODL/EI, SEA/GNJ, NZW/LACJ and VM/DK. Ref.5

Natural variant

811

1

N → K in strain: P/J. Ref.5

Experimental info

Sequence conflict

87 – 154

68

CEIET…TLKKL → EMNTESKSSEAHALALSHIL SPCQPSRRKLRVKLGSLSYQ RAEEGVRSSEIGYSCLHVDT RHDINAVD Ref.6

Secondary structure

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835

Helix Strand Turn

Details...

Beta strand

29 – 32

4

Turn

33 – 35

3

Beta strand

36 – 38

3

Beta strand

40 – 42

3

Beta strand

49 – 51

3

Beta strand

57 – 59

3

Turn

70 – 75

6

Beta strand

81 – 83

3

Turn

94 – 99

6

Beta strand

105 – 107

3

Turn

118 – 123

6

Beta strand

129 – 131

3

Beta strand

140 – 143

4

Beta strand

153 – 155

3

Helix

168 – 171

4

Beta strand

178 – 180

3

Turn

191 – 194

4

Helix

195 – 199

5

Beta strand

206 – 208

3

Turn

219 – 224

6

Beta strand

226 – 234

9

Helix

239 – 247

9

Turn

248 – 251

4

Beta strand

253 – 260

8

Helix

273 – 276

4

Helix

279 – 281

3

Beta strand

282 – 289

8

Helix

297 – 300

4

Helix

303 – 305

3

Beta strand

309 – 315

7

Beta strand

331 – 337

7

Beta strand

353 – 358

6

Beta strand

375 – 377

3

Beta strand

380 – 382

3

Beta strand

383 – 388

6

Helix

391 – 394

4

Beta strand

401 – 403

3

Beta strand

408 – 412

5

Beta strand

424 – 426

3

Beta strand

430 – 434

5

Turn

435 – 443

9

Beta strand

449 – 451

3

Turn

462 – 467

6

Beta strand

473 – 475

3

Helix

482 – 484

3

Beta strand

498 – 500

3

Turn

511 – 516

6

Beta strand

522 – 524

3

Beta strand

532 – 534

3

Helix

535 – 537

3

Turn

538 – 540

3

Beta strand

546 – 548

3

Beta strand

557 – 559

3

Helix

561 – 563

3

Beta strand

570 – 572

3

Helix

582 – 584

3

Helix

585 – 588

4

Turn

589 – 593

5

Beta strand

594 – 600

7

Helix

601 – 603

3

Beta strand

608 – 610

3

Helix

616 – 618

3

Sequences

	Sequence		Length	Mass (Da)
	Q9QUK6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 9C83B59F9A220C17	FASTA	835	95,519
	10 20 30 40 50 60 MMPPWLLART LIMALFFSCL TPGSLNPCIE VVPNITYQCM DQKLSKVPDD IPSSTKNIDL 70 80 90 100 110 120 SFNPLKILKS YSFSNFSELQ WLDLSRCEIE TIEDKAWHGL HHLSNLILTG NPIQSFSPGS 130 140 150 160 170 180 FSGLTSLENL VAVETKLASL ESFPIGQLIT LKKLNVAHNF IHSCKLPAYF SNLTNLVHVD 190 200 210 220 230 240 LSYNYIQTIT VNDLQFLREN PQVNLSLDMS LNPIDFIQDQ AFQGIKLHEL TLRGNFNSSN 250 260 270 280 290 300 IMKTCLQNLA GLHVHRLILG EFKDERNLEI FEPSIMEGLC DVTIDEFRLT YTNDFSDDIV 310 320 330 340 350 360 KFHCLANVSA MSLAGVSIKY LEDVPKHFKW QSLSIIRCQL KQFPTLDLPF LKSLTLTMNK 370 380 390 400 410 420 GSISFKKVAL PSLSYLDLSR NALSFSGCCS YSDLGTNSLR HLDLSFNGAI IMSANFMGLE 430 440 450 460 470 480 ELQHLDFQHS TLKRVTEFSA FLSLEKLLYL DISYTNTKID FDGIFLGLTS LNTLKMAGNS 490 500 510 520 530 540 FKDNTLSNVF ANTTNLTFLD LSKCQLEQIS WGVFDTLHRL QLLNMSHNNL LFLDSSHYNQ 550 560 570 580 590 600 LYSLSTLDCS FNRIETSKGI LQHFPKSLAF FNLTNNSVAC ICEHQKFLQW VKEQKQFLVN 610 620 630 640 650 660 VEQMTCATPV EMNTSLVLDF NNSTCYMYKT IISVSVVSVI VVSTVAFLIY HFYFHLILIA 670 680 690 700 710 720 GCKKYSRGES IYDAFVIYSS QNEDWVRNEL VKNLEEGVPR FHLCLHYRDF IPGVAIAANI 730 740 750 760 770 780 IQEGFHKSRK VIVVVSRHFI QSRWCIFEYE IAQTWQFLSS RSGIIFIVLE KVEKSLLRQQ 790 800 810 820 830 VELYRLLSRN TYLEWEDNPL GRHIFWRRLK NALLDGKASN PEQTAEEEQE TATWT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic and physical mapping of the Lps locus: identification of the Toll-4 receptor as a candidate gene in the critical region." Poltorak A., Smirnova I., He X., Liu M.-Y., Van Huffel C., Birdwell D., Alejos E., Silva M., Du X., Thompson P., Chan E.K.L., Ledesma J., Roe B., Clifton S., Vogel S.N., Beutler B. Blood Cells Mol. Dis. 24:340-355(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C3H/HeJ.
[2]	"Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene." Poltorak A., He X., Smirnova I., Liu M.-Y., Van Huffel C., Du X., Birdwell D., Alejos E., Silva M., Galanos C., Freudenberg M., Ricciardi-Castagnoli P., Layton B., Beutler B. Science 282:2085-2088(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LPS-TOLERANT HIS-712. Strain: C3H/HeJ.
[3]	"Endotoxin-tolerant mice have mutations in Toll-like receptor 4 (Tlr4)." Qureshi S.T., Lariviere L., Leveque G., Clermont S., Moore K.J., Gros P., Malo D. J. Exp. Med. 189:615-625(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LPS-TOLERANT HIS-712. Strain: C57BL/6J.
[4]	"The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens." Underhill D.M., Ozinsky A., Hajjar A.M., Stevens A., Wilson C.B., Bassetti M., Aderem A. Nature 401:811-815(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Macrophage.
[5]	"Phylogenetic variation and polymorphism at the Toll-like receptor 4 locus (TLR4)." Smirnova I., Poltorak A., Chan E.K.L., McBride C., Beutler B. Genome Biol. 1:RESEARCH002.1-RESEARCH002.10(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-94; ILE-209; GLY-219; ILE-254; LEU-423; SER-477; ALA-516; ASP-593; ILE-600; VAL-607; ILE-637; HIS-761 AND LYS-811. Strain: Various strains.
[6]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-154. Strain: C57BL/6J. Tissue: Skin.
[7]	"Murine Toll-like receptor 4 confers lipopolysaccharide responsiveness as determined by activation of NF kappa B and expression of the inducible cyclooxygenase." Rhee S.H., Hwang D. J. Biol. Chem. 275:34035-34040(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"A single base mutation in the PRAT4A gene reveals differential interaction of PRAT4A with Toll-like receptors." Kiyokawa T., Akashi-Takamura S., Shibata T., Matsumoto F., Nishitani C., Kuroki Y., Seto Y., Miyake K. Int. Immunol. 20:1407-1415(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CNPY3.
[9]	"Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone." Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z. Nat. Commun. 1:79-79(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HSP90B1.
[10]	Erratum Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z. Nat. Commun. 3:653-653(2012)
[11]	"Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran." Kim H.M., Park B.S., Kim J.-I., Kim S.E., Lee J., Oh S.C., Enkhbayar P., Matsushima N., Lee H., Yoo O.J., Lee J.-O. Cell 130:906-917(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 27-625 IN COMPLEX WITH LY96, GLYCOSYLATION AT ASN-34; ASN-75; ASN-172; ASN-204; ASN-237; ASN-307; ASN-492; ASN-524 AND ASN-572.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF095353 mRNA. Translation: AAC99411.1.
AF110133 mRNA. Translation: AAD29272.1.
AF185285 mRNA. Translation: AAF04278.1.
AF177767 Genomic DNA. Translation: AAF05317.1.
AK014533 mRNA. No translation available.

IPI

IPI00131730.

RefSeq

NP_067272.1. NM_021297.2.

UniGene

Mm.38049.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Z64	X-ray	2.84	A	27-625	[»]
3VQ1	X-ray	2.70	A/B	22-627	[»]
3VQ2	X-ray	2.48	A/B	22-627	[»]

ProteinModelPortal

Q9QUK6.

SMR

Q9QUK6. Positions 27-814.

ModBase

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Protein-protein interaction databases

DIP

DIP-38573N.

IntAct

Q9QUK6. 2 interactions.

STRING

10090.ENSMUSP00000045770.

PTM databases

PhosphoSite

Q9QUK6.

Proteomic databases

PRIDE

Q9QUK6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000048096; ENSMUSP00000045770; ENSMUSG00000039005.

GeneID

21898.

KEGG

mmu:21898.

UCSC

uc008thv.1. mouse.

Organism-specific databases

CTD

7099.

MGI

MGI:96824. Tlr4.

Phylogenomic databases

eggNOG

NOG249751.

GeneTree

ENSGT00700000104185.

HOGENOM

HOG000037951.

HOVERGEN

HBG018823.

InParanoid

Q9QUK6.

KO

K10160.

OMA

TNIIQEG.

OrthoDB

EOG4P8FHQ.

Gene expression databases

Bgee

Q9QUK6.

CleanEx

MM_TLR4.

Genevestigator

Q9QUK6.

GermOnline

ENSMUSG00000039005. Mus musculus.

Family and domain databases

InterPro

IPR000483. Cys-rich_flank_reg_C.
IPR000157. TIR_dom.
IPR027168. TLR4.
IPR017241. Toll-like_receptor.
[Graphical view]

PANTHER

PTHR24365:SF9. PTHR24365:SF9. 1 hit.

Pfam

PF01582. TIR. 1 hit.
[Graphical view]

PIRSF

PIRSF037595. Toll-like_receptor. 1 hit.

SMART

SM00082. LRRCT. 1 hit.
SM00255. TIR. 1 hit.
[Graphical view]

SUPFAM

SSF52200. TIR. 1 hit.

PROSITE

PS50104. TIR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9QUK6.

ChEMBL

CHEMBL1795167.

EvolutionaryTrace

Q9QUK6.

NextBio

301436.

SOURCE

Search...

Entry information

Entry name

TLR4_MOUSE

Accession

Primary (citable) accession number: Q9QUK6
Secondary accession number(s): Q9D691, Q9QZF5, Q9Z203

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 11, 2002
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program