MYD88_MOUSE
ID MYD88_MOUSE Reviewed; 296 AA.
AC P22366; O35916;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Myeloid differentiation primary response protein MyD88;
GN Name=Myd88 {ECO:0000312|MGI:MGI:108005};
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9013863; DOI=10.1016/s0014-5793(96)01506-2;
RA Bonnert T.P., Garka K.E., Parnet P., Sonoda G., Testa J.R., Sims J.E.;
RT "The cloning and characterization of human MyD88: a member of an IL-1
RT receptor related family.";
RL FEBS Lett. 402:81-84(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Myeloid leukemia cell;
RX PubMed=9344657; DOI=10.1006/geno.1997.4940;
RA Hardiman G., Jenkins N.A., Copeland N.G., Gilbert D.J., Garcia D.K.,
RA Naylor S.L., Kastelein R.A., Bazan J.F.;
RT "Genetic structure and chromosomal mapping of MyD88.";
RL Genomics 45:332-339(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland, and Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-296 (ISOFORM 1), INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=2374694;
RA Lord K.A., Hoffman-Liebermann B., Liebermann D.A.;
RT "Nucleotide sequence and expression of a cDNA encoding MyD88, a novel
RT myeloid differentiation primary response gene induced by IL6.";
RL Oncogene 5:1095-1097(1990).
RN [5]
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND MUTAGENESIS OF PHE-56.
RC TISSUE=Bone marrow;
RX PubMed=9575168; DOI=10.1074/jbc.273.20.12203;
RA Burns K., Martinon F., Esslinger C., Pahl H., Schneider P., Bodmer J.-L.,
RA Di Marco F., French L., Tschopp J.;
RT "MyD88, an adapter protein involved in interleukin-1 signaling.";
RL J. Biol. Chem. 273:12203-12209(1998).
RN [6]
RP FUNCTION, INTERACTION WITH IL18R1, AND DISRUPTION PHENOTYPE.
RX PubMed=9697844; DOI=10.1016/s1074-7613(00)80596-8;
RA Adachi O., Kawai T., Takeda K., Matsumoto M., Tsutsui H., Sakagami M.,
RA Nakanishi K., Akira S.;
RT "Targeted disruption of the MyD88 gene results in loss of IL-1- and IL-18-
RT mediated function.";
RL Immunity 9:143-150(1998).
RN [7]
RP ALTERNATIVE SPLICING, IDENTIFICATION OF ISOFORM 2, FUNCTION, SUBUNIT, AND
RP TISSUE SPECIFICITY.
RX PubMed=11909531; DOI=10.1016/s0960-9822(02)00712-1;
RA Janssens S., Burns K., Tschopp J., Beyaert R.;
RT "Regulation of interleukin-1- and lipopolysaccharide-induced NF-kappaB
RT activation by alternative splicing of MyD88.";
RL Curr. Biol. 12:467-471(2002).
RN [8]
RP IDENTIFICATION IN COMPLEX WITH IRAK1; IRAK4; TRAF6 AND PELI1.
RX PubMed=16951688; DOI=10.1038/ni1383;
RA Choi K.C., Lee Y.S., Lim S., Choi H.K., Lee C.H., Lee E.K., Hong S.,
RA Kim I.H., Kim S.J., Park S.H.;
RT "Smad6 negatively regulates interleukin 1-receptor-Toll-like receptor
RT signaling through direct interaction with the adapter Pellino-1.";
RL Nat. Immunol. 7:1057-1065(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IRF1.
RX PubMed=17018642; DOI=10.1073/pnas.0607181103;
RA Negishi H., Fujita Y., Yanai H., Sakaguchi S., Ouyang X., Shinohara M.,
RA Takayanagi H., Ohba Y., Taniguchi T., Honda K.;
RT "Evidence for licensing of IFN-gamma-induced IFN regulatory factor 1
RT transcription factor by MyD88 in Toll-like receptor-dependent gene
RT induction program.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15136-15141(2006).
RN [10]
RP FUNCTION.
RX PubMed=17635956; DOI=10.1084/jem.20070563;
RA Brandl K., Plitas G., Schnabl B., DeMatteo R.P., Pamer E.G.;
RT "MyD88-mediated signals induce the bactericidal lectin RegIII gamma and
RT protect mice against intestinal Listeria monocytogenes infection.";
RL J. Exp. Med. 204:1891-1900(2007).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18941239; DOI=10.4049/jimmunol.181.9.6481;
RA Babcock A.A., Toft-Hansen H., Owens T.;
RT "Signaling through MyD88 regulates leukocyte recruitment after brain
RT injury.";
RL J. Immunol. 181:6481-6490(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21998396; DOI=10.1126/science.1209791;
RA Vaishnava S., Yamamoto M., Severson K.M., Ruhn K.A., Yu X., Koren O.,
RA Ley R., Wakeland E.K., Hooper L.V.;
RT "The antibacterial lectin RegIIIgamma promotes the spatial segregation of
RT microbiota and host in the intestine.";
RL Science 334:255-258(2011).
RN [14]
RP INTERACTION WITH PIK3AP1.
RX PubMed=22187460; DOI=10.1073/pnas.1118579109;
RA Troutman T.D., Hu W., Fulenchek S., Yamazaki T., Kurosaki T., Bazan J.F.,
RA Pasare C.;
RT "Role for B-cell adapter for PI3K (BCAP) as a signaling adapter linking
RT Toll-like receptors (TLRs) to serine/threonine kinases PI3K/Akt.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:273-278(2012).
RN [15]
RP INTERACTION WITH OTUD4.
RX PubMed=29395066; DOI=10.1016/j.molcel.2018.01.009;
RA Zhao Y., Mudge M.C., Soll J.M., Rodrigues R.B., Byrum A.K.,
RA Schwarzkopf E.A., Bradstreet T.R., Gygi S.P., Edelson B.T.,
RA Mosammaparast N.;
RT "OTUD4 Is a Phospho-Activated K63 Deubiquitinase that Regulates MyD88-
RT Dependent Signaling.";
RL Mol. Cell 69:505-516(2018).
CC -!- FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1
CC receptor signaling pathway in the innate immune response
CC (PubMed:9697844). Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-
CC kappa-B activation, cytokine secretion and the inflammatory response
CC (PubMed:9575168, PubMed:9697844). Increases IL-8 transcription.
CC Involved in IL-18-mediated signaling pathway (PubMed:9697844).
CC Activates IRF1 resulting in its rapid migration into the nucleus to
CC mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes
CC (PubMed:17018642). Upon TLR8 activation by GU-rich single-stranded RNA
CC (GU-rich RNA) derived from viruses, induces IL1B release through NLRP3
CC inflammasome activation (By similarity). MyD88-mediated signaling in
CC intestinal epithelial cells is crucial for maintenance of gut
CC homeostasis and controls the expression of the antimicrobial lectin
CC REG3G in the small intestine (PubMed:17635956, PubMed:21998396).
CC Mediates leukocyte recruitment at the inflammatory site
CC (PubMed:18941239). {ECO:0000250|UniProtKB:Q99836,
CC ECO:0000269|PubMed:11909531, ECO:0000269|PubMed:17018642,
CC ECO:0000269|PubMed:17635956, ECO:0000269|PubMed:18941239,
CC ECO:0000269|PubMed:21998396, ECO:0000269|PubMed:9575168,
CC ECO:0000269|PubMed:9697844}.
CC -!- FUNCTION: [Isoform 2]: Defective in its ability to induce IRAK
CC phosphorylation and NF-kappa-B activation and can function as a
CC negative regulator of activation by IL-1 or lipopolysaccharide (LPS).
CC {ECO:0000269|PubMed:11909531}.
CC -!- SUBUNIT: Homodimer. Also forms heterodimers with TIRAP. Binds to TLR2,
CC TLR4, IRAK1, IRAK2 and IRAK4 via their respective TIR domains.
CC Interacts with IL18R1. Interacts with BMX, IL1RL1, IKBKE and IRF7.
CC Interacts with LRRFIP1 and LRRFIP2; this interaction positively
CC regulates Toll-like receptor (TLR) signaling in response to agonist.
CC Interacts with FLII. LRRFIP1 and LRRFIP2 compete with FLII for MYD88-
CC binding. Interacts with IRF1. Upon IL1B treatment, forms a complex with
CC PELI1, IRAK1, IRAK4 and TRAF6; this complex recruits MAP3K7/TAK1, TAB1
CC and TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to
CC PELI1 prevents the complex formation and hence negatively regulates
CC IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression.
CC May interact with PIK3AP1. Interacts (via TIR domain) with DHX9 (via
CC H2A and OB-fold regions); this interaction is direct. Interacts with
CC OTUD4 deubiquitinase; the interaction is direct (PubMed:29395066).
CC {ECO:0000250|UniProtKB:Q99836, ECO:0000269|PubMed:11909531,
CC ECO:0000269|PubMed:16951688, ECO:0000269|PubMed:17018642,
CC ECO:0000269|PubMed:22187460, ECO:0000269|PubMed:29395066,
CC ECO:0000269|PubMed:9575168, ECO:0000269|PubMed:9697844}.
CC -!- INTERACTION:
CC P22366; P35991: Btk; NbExp=2; IntAct=EBI-525108, EBI-625119;
CC P22366; Q3TTA7: Cblb; NbExp=2; IntAct=EBI-525108, EBI-3649276;
CC P22366; P13504: Il1r1; NbExp=2; IntAct=EBI-525108, EBI-1782675;
CC P22366; Q62406: Irak1; NbExp=3; IntAct=EBI-525108, EBI-448533;
CC P22366; Q8R4K2: Irak4; NbExp=8; IntAct=EBI-525108, EBI-3842721;
CC P22366; Q9EQ32: Pik3ap1; NbExp=2; IntAct=EBI-525108, EBI-643949;
CC P22366; Q9QUN7: Tlr2; NbExp=2; IntAct=EBI-525108, EBI-3505834;
CC P22366; Q9QUK6: Tlr4; NbExp=2; IntAct=EBI-525108, EBI-1534575;
CC P22366; Q9WUU8: Tnip1; NbExp=3; IntAct=EBI-525108, EBI-6126152;
CC P22366; Q60803: Traf3; NbExp=5; IntAct=EBI-525108, EBI-520135;
CC P22366; P70196: Traf6; NbExp=4; IntAct=EBI-525108, EBI-448028;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17018642}. Nucleus
CC {ECO:0000250|UniProtKB:Q99836}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=MyD88L;
CC IsoId=P22366-1; Sequence=Displayed;
CC Name=2; Synonyms=MyD88S;
CC IsoId=P22366-2; Sequence=VSP_038888;
CC -!- TISSUE SPECIFICITY: Detected in bone marrow. Isoform 1 is expressed in
CC testis, kidney, lung, ovary, adrenal gland, provstate, thymus and
CC heart, and weakly in skeletal muscle, liver, spleen and brain. Isoform
CC 2 is mainly expressed in the spleen and weakly in brain.
CC {ECO:0000269|PubMed:11909531, ECO:0000269|PubMed:21998396,
CC ECO:0000269|PubMed:2374694, ECO:0000269|PubMed:9013863,
CC ECO:0000269|PubMed:9575168}.
CC -!- INDUCTION: By interleukin-6. {ECO:0000269|PubMed:2374694}.
CC -!- DOMAIN: The intermediate domain (ID) is required for the
CC phosphorylation and activation of IRAK. {ECO:0000269|PubMed:11909531}.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination. OTUD4
CC specifically hydrolyzes 'Lys-63'-linked polyubiquitinated MYD88.
CC {ECO:0000250|UniProtKB:Q99836}.
CC -!- DISRUPTION PHENOTYPE: Mice appear normal, but display loss of
CC activation of NF-kappa-B in response to IL-1 or IL-18. They show no
CC increase in interferon gamma production or in stimulation of natural
CC killer cell activity in response to IL-18. They are impaired in
CC production of cytokines in response to IL-1. They have defects in pro-
CC inflammatory gene expression and leukocyte recruitment after brain
CC injury. Mice have a diminished capacity to kill L.monocytogenes in the
CC lumen of the distal small intestine and express markedly diminished
CC levels of REG3G. {ECO:0000269|PubMed:18941239,
CC ECO:0000269|PubMed:21998396, ECO:0000269|PubMed:9697844}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35762.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U84409; AAC53013.1; -; mRNA.
DR EMBL; U89023; AAB83958.1; -; Genomic_DNA.
DR EMBL; BC005591; AAH05591.1; -; mRNA.
DR EMBL; BC058787; AAH58787.1; -; mRNA.
DR EMBL; X51397; CAA35762.1; ALT_INIT; mRNA.
DR CCDS; CCDS23612.1; -. [P22366-1]
DR PIR; S11226; S11226.
DR RefSeq; NP_034981.1; NM_010851.2. [P22366-1]
DR AlphaFoldDB; P22366; -.
DR SMR; P22366; -.
DR BioGRID; 201639; 41.
DR CORUM; P22366; -.
DR DIP; DIP-34957N; -.
DR IntAct; P22366; 28.
DR MINT; P22366; -.
DR STRING; 10090.ENSMUSP00000035092; -.
DR ChEMBL; CHEMBL4523204; -.
DR iPTMnet; P22366; -.
DR PhosphoSitePlus; P22366; -.
DR EPD; P22366; -.
DR MaxQB; P22366; -.
DR PaxDb; P22366; -.
DR PeptideAtlas; P22366; -.
DR PRIDE; P22366; -.
DR ProteomicsDB; 287567; -. [P22366-1]
DR ProteomicsDB; 287568; -. [P22366-2]
DR Antibodypedia; 3965; 977 antibodies from 51 providers.
DR DNASU; 17874; -.
DR Ensembl; ENSMUST00000035092; ENSMUSP00000035092; ENSMUSG00000032508. [P22366-1]
DR GeneID; 17874; -.
DR KEGG; mmu:17874; -.
DR UCSC; uc009sar.1; mouse. [P22366-1]
DR CTD; 4615; -.
DR MGI; MGI:108005; Myd88.
DR VEuPathDB; HostDB:ENSMUSG00000032508; -.
DR eggNOG; ENOG502QWKI; Eukaryota.
DR GeneTree; ENSGT00510000048324; -.
DR HOGENOM; CLU_045884_0_0_1; -.
DR InParanoid; P22366; -.
DR OMA; CTQSWFW; -.
DR PhylomeDB; P22366; -.
DR TreeFam; TF326264; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-MMU-209543; p75NTR recruits signalling complexes.
DR Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR BioGRID-ORCS; 17874; 0 hits in 72 CRISPR screens.
DR PRO; PR:P22366; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P22366; protein.
DR Bgee; ENSMUSG00000032508; Expressed in granulocyte and 159 other tissues.
DR ExpressionAtlas; P22366; baseline and differential.
DR Genevisible; P22366; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005149; F:interleukin-1 receptor binding; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0070976; F:TIR domain binding; ISO:MGI.
DR GO; GO:0005121; F:Toll binding; ISO:MGI.
DR GO; GO:0035325; F:Toll-like receptor binding; IPI:UniProtKB.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:ARUK-UCL.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; IMP:ARUK-UCL.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0042832; P:defense response to protozoan; IMP:ARUK-UCL.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; IMP:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0006955; P:immune response; TAS:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR GO; GO:0009682; P:induced systemic resistance; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; IMP:MGI.
DR GO; GO:0002269; P:leukocyte activation involved in inflammatory response; IGI:MGI.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:MGI.
DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IMP:MGI.
DR GO; GO:0002283; P:neutrophil activation involved in immune response; IGI:MGI.
DR GO; GO:0070944; P:neutrophil-mediated killing of bacterium; IGI:MGI.
DR GO; GO:0006909; P:phagocytosis; IMP:UniProtKB.
DR GO; GO:0032722; P:positive regulation of chemokine production; IGI:MGI.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IMP:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IMP:BHF-UCL.
DR GO; GO:0032747; P:positive regulation of interleukin-23 production; IMP:BHF-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:BHF-UCL.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:MGI.
DR GO; GO:0050671; P:positive regulation of lymphocyte proliferation; IMP:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:MGI.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:2000338; P:regulation of chemokine (C-X-C motif) ligand 1 production; IMP:MGI.
DR GO; GO:2000341; P:regulation of chemokine (C-X-C motif) ligand 2 production; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:BHF-UCL.
DR GO; GO:0032675; P:regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:1902622; P:regulation of neutrophil migration; IMP:MGI.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0002238; P:response to molecule of fungal origin; IMP:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0032494; P:response to peptidoglycan; IMP:MGI.
DR GO; GO:0009615; P:response to virus; IMP:MGI.
DR GO; GO:0008063; P:Toll signaling pathway; ISO:MGI.
DR GO; GO:0034158; P:toll-like receptor 8 signaling pathway; ISS:UniProtKB.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; TAS:MGI.
DR GO; GO:0060337; P:type I interferon signaling pathway; ISO:MGI.
DR CDD; cd08312; Death_MyD88; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR034249; MyD88_Death.
DR InterPro; IPR017281; Myelin_different_resp_MyD88.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR15079; PTHR15079; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF01582; TIR; 1.
DR PIRSF; PIRSF037756; MyD88; 1.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Immunity; Inflammatory response;
KW Innate immunity; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..296
FT /note="Myeloid differentiation primary response protein
FT MyD88"
FT /id="PRO_0000096667"
FT DOMAIN 54..109
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT DOMAIN 159..293
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 110..155
FT /note="Intermediate domain"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99836"
FT VAR_SEQ 110..155
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038888"
FT MUTAGEN 56
FT /note="F->N: Prevents dimerization of death domains and
FT activation of JNK and NF-kappa-B."
FT /evidence="ECO:0000269|PubMed:9575168"
FT CONFLICT 51
FT /note="A -> P (in Ref. 1; AAC53013 and 4; CAA35762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 33753 MW; 393A75C3723FFE69 CRC64;
MSAGDPRVGS GSLDSFMFSI PLVALNVGVR RRLSLFLNPR TPVAADWTLL AEEMGFEYLE
IRELETRPDP TRSLLDAWQG RSGASVGRLL ELLALLDRED ILKELKSRIE EDCQKYLGKQ
QNQESEKPLQ VARVESSVPQ TKELGGITTL DDPLGQTPEL FDAFICYCPN DIEFVQEMIR
QLEQTDYRLK LCVSDRDVLP GTCVWSIASE LIEKRCRRMV VVVSDDYLQS KECDFQTKFA
LSLSPGVQQK RLIPIKYKAM KKDFPSILRF ITICDYTNPC TKSWFWTRLA KALSLP
