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TIR domain-containing adapter molecule 1 (TICAM-1) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (TIR domain-containing adapter protein inducing IFN-beta)

 TCAM1_MOUSE             Reviewed;         732 AA.
Q80UF7; Q3UDB7; Q3UP66; Q6P6J2; Q8CIB7; Q8JZV0;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
25-OCT-2017, entry version 114.
RecName: Full=TIR domain-containing adapter molecule 1;
Short=TICAM-1;
AltName: Full=Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta;
Short=TIR domain-containing adapter protein inducing IFN-beta;
Name=Ticam1; Synonyms=Trif;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12539043; DOI=10.1038/ni886;
Oshiumi H., Matsumoto M., Funami K., Akazawa T., Seya T.;
"TICAM-1, an adapter molecule that participates in Toll-like receptor
3 mediated interferon-beta induction.";
Nat. Immunol. 4:161-167(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, FVB/N, and FVB/N-3;
TISSUE=Eye, Jaw, Limb, Mammary tumor, and Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12855817; DOI=10.1126/science.1087262;
Yamamoto M., Sato S., Hemmi H., Hoshino K., Kaisho T., Sanjo H.,
Takeuchi O., Sugiyama M., Okabe M., Takeda K., Akira S.;
"Role of adaptor TRIF in the MyD88-independent toll-like receptor
signaling pathway.";
Science 301:640-643(2003).
[5]
FUNCTION.
PubMed=16002681; DOI=10.4049/jimmunol.175.2.839;
De Trez C., Pajak B., Brait M., Glaichenhaus N., Urbain J., Moser M.,
Lauvau G., Muraille E.;
"TLR4 and Toll-IL-1 receptor domain-containing adapter-inducing IFN-
beta, but not MyD88, regulate Escherichia coli-induced dendritic cell
maturation and apoptosis in vivo.";
J. Immunol. 175:839-846(2005).
[6]
INTERACTION WITH TRAF3.
PubMed=16306936; DOI=10.1038/nature04374;
Oganesyan G., Saha S.K., Guo B., He J.Q., Shahangian A., Zarnegar B.,
Perry A., Cheng G.;
"Critical role of TRAF3 in the Toll-like receptor-dependent and
-independent antiviral response.";
Nature 439:208-211(2006).
[7]
REVIEW.
PubMed=17457343; DOI=10.1038/nri2079;
O'Neill L.A., Bowie A.G.;
"The family of five: TIR-domain-containing adaptors in Toll-like
receptor signalling.";
Nat. Rev. Immunol. 7:353-364(2007).
[8]
INTERACTION WITH TRAFD1.
PubMed=18849341; DOI=10.1074/jbc.M806923200;
Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T.,
Yoshimura A.;
"FLN29 deficiency reveals its negative regulatory role in the Toll-
like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like
helicase signaling pathway.";
J. Biol. Chem. 283:33858-33864(2008).
[9]
INTERACTION WITH WDFY1; TLR3 AND TLR4.
PubMed=25736436; DOI=10.15252/embr.201439637;
Hu Y.H., Zhang Y., Jiang L.Q., Wang S., Lei C.Q., Sun M.S., Shu H.B.,
Liu Y.;
"WDFY1 mediates TLR3/4 signaling by recruiting TRIF.";
EMBO Rep. 16:447-455(2015).
-!- FUNCTION: Involved in innate immunity against invading pathogens.
Adapter used by TLR3 and TLR4 (through TICAM2) to mediate NF-
kappa-B and interferon-regulatory factor (IRF) activation, and to
induce apoptosis. Ligand binding to these receptors results in
TRIF recruitment through its TIR domain. Distinct protein-
interaction motifs allow recruitment of the effector proteins
TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of
transcription factors IRF3 and IRF7, NF-kappa-B and FADD
respectively. {ECO:0000269|PubMed:12855817,
ECO:0000269|PubMed:16002681}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with AZI2, IRF3 and
IRF7 (By similarity). Interacts with TICAM2 in TLR4 recruitment
(By similarity). Interaction with PIAS4 inhibits the TICAM1-
induced NF-kappa-B, IRF and IFNB1 activation (By similarity).
Interacts with IKBKB and IKBKE (By similarity). Interaction with
SARM1 blocks TICAM1-dependent transcription factor activation (By
similarity). Interacts with TRAF3. Interacts with TRAFD1.
Interacts with UBQLN1 (via UBA domain). Interacts with TBK1, TRAF6
and RIPK1 and these interactions are enhanced in the presence of
WDFY1 (By similarity). Interacts (via the TIR domain) with TLR3 in
response to poly(I:C) and this interaction is enhanced in the
presence of WDFY1 (PubMed:25736436). Interacts with TLR4 in
response to poly(I:C) in a WDFY1-dependent manner
(PubMed:25736436). Interacts with WDFY1 in response to poly(I:C)
(PubMed:25736436). Interacts with TRIM56 (By similarity).
{ECO:0000250|UniProtKB:Q8IUC6, ECO:0000269|PubMed:16306936,
ECO:0000269|PubMed:18849341, ECO:0000269|PubMed:25736436}.
-!- INTERACTION:
P35991:Btk; NbExp=2; IntAct=EBI-3649271, EBI-625119;
Q3TTA7:Cblb; NbExp=2; IntAct=EBI-3649271, EBI-3649276;
Q9WUN2:Tbk1; NbExp=2; IntAct=EBI-3649271, EBI-764193;
Q60803:Traf3; NbExp=2; IntAct=EBI-3649271, EBI-520135;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
{ECO:0000250|UniProtKB:Q8IUC6}. Note=Colocalizes with UBQLN1 in
the autophagosome. {ECO:0000250|UniProtKB:Q8IUC6}.
-!- DOMAIN: The N-terminal region is essential for activation of the
IFNB promoter activity. {ECO:0000250}.
-!- DOMAIN: The N-terminal domain (TRIF-NTD) is globular and consists
of two alpha-helical subdomains connected by a 14-residue linker.
It shares structural similarity with IFIT family members N-
terminal regions. {ECO:0000250|UniProtKB:Q8IUC6}.
-!- PTM: Phosphorylated by TBK1. {ECO:0000250}.
-!- PTM: Polyubiquitinated by TRIM38 with 'Lys-48'-linked chains,
leading to proteasomal degradation.
{ECO:0000250|UniProtKB:Q8IUC6}.
-!- DISRUPTION PHENOTYPE: Mice are viable but exhibit abnormalities of
the innate immune system. {ECO:0000269|PubMed:12855817}.
-!- SEQUENCE CAUTION:
Sequence=AAH33406.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
Sequence=AAH37048.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH62191.1; Type=Frameshift; Positions=350; Evidence={ECO:0000305};
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EMBL; AB091053; BAC55581.1; -; mRNA.
EMBL; AK143766; BAE25531.1; -; mRNA.
EMBL; AK150150; BAE29344.1; -; mRNA.
EMBL; AK155245; BAE33144.1; -; mRNA.
EMBL; BC033406; AAH33406.1; ALT_SEQ; mRNA.
EMBL; BC037048; AAH37048.1; ALT_INIT; mRNA.
EMBL; BC062191; AAH62191.1; ALT_FRAME; mRNA.
EMBL; BC094338; AAH94338.1; -; mRNA.
CCDS; CCDS28900.1; -.
RefSeq; NP_778154.1; NM_174989.4.
UniGene; Mm.203952; -.
ProteinModelPortal; Q80UF7; -.
SMR; Q80UF7; -.
BioGrid; 223122; 9.
DIP; DIP-60033N; -.
IntAct; Q80UF7; 6.
STRING; 10090.ENSMUSP00000055104; -.
PhosphoSitePlus; Q80UF7; -.
PaxDb; Q80UF7; -.
PRIDE; Q80UF7; -.
Ensembl; ENSMUST00000058136; ENSMUSP00000055104; ENSMUSG00000047123.
GeneID; 106759; -.
KEGG; mmu:106759; -.
UCSC; uc008dbm.2; mouse.
CTD; 148022; -.
MGI; MGI:2147032; Ticam1.
eggNOG; ENOG410IJUV; Eukaryota.
eggNOG; ENOG410Y8DE; LUCA.
GeneTree; ENSGT00900000141066; -.
HOGENOM; HOG000068973; -.
HOVERGEN; HBG108551; -.
InParanoid; Q80UF7; -.
KO; K05842; -.
OMA; EEKLCPA; -.
OrthoDB; EOG091G07G7; -.
PhylomeDB; Q80UF7; -.
TreeFam; TF336953; -.
Reactome; R-MMU-166166; MyD88-independent TLR3/TLR4 cascade.
PRO; PR:Q80UF7; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000047123; -.
CleanEx; MM_TICAM1; -.
Genevisible; Q80UF7; MM.
GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0097342; C:ripoptosome; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004871; F:signal transducer activity; ISO:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IMP:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:ParkinsonsUK-UCL.
GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; IMP:ARUK-UCL.
GO; GO:0051607; P:defense response to virus; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:MGI.
GO; GO:0002281; P:macrophage activation involved in immune response; IMP:MGI.
GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; IMP:MGI.
GO; GO:0010508; P:positive regulation of autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0050871; P:positive regulation of B cell activation; IMP:MGI.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IMP:MGI.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IMP:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; IMP:MGI.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:MGI.
GO; GO:0032816; P:positive regulation of natural killer cell activation; IMP:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:MGI.
GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
GO; GO:0032481; P:positive regulation of type I interferon production; IMP:MGI.
GO; GO:0043496; P:regulation of protein homodimerization activity; IMP:MGI.
GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; IMP:ParkinsonsUK-UCL.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR025735; RHIM_dom.
InterPro; IPR017278; TICAM1.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR23213:SF331; PTHR23213:SF331; 1.
Pfam; PF12721; RHIM; 1.
PIRSF; PIRSF037744; TIR_Ticam; 1.
SUPFAM; SSF52200; SSF52200; 1.
1: Evidence at protein level;
Antiviral defense; Apoptosis; Complete proteome; Cytoplasmic vesicle;
Immunity; Inflammatory response; Innate immunity; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 732 TIR domain-containing adapter molecule 1.
/FTId=PRO_0000317664.
DOMAIN 392 465 TIR.
REGION 1 153 TRIF-NTD. {ECO:0000250|UniProtKB:Q8IUC6}.
REGION 514 713 Sufficient to induce apoptosis.
{ECO:0000250}.
MOTIF 84 91 TRAF6-binding. {ECO:0000250}.
MOTIF 247 254 TRAF6-binding. {ECO:0000250}.
MOTIF 296 306 TRAF6-binding. {ECO:0000250}.
COMPBIAS 348 384 Pro-rich.
COMPBIAS 602 679 Pro-rich.
CONFLICT 227 227 S -> G (in Ref. 2; BAE29344).
{ECO:0000305}.
CONFLICT 351 435 Missing (in Ref. 3; AAH62191).
{ECO:0000305}.
CONFLICT 435 435 V -> A (in Ref. 2; BAE25531).
{ECO:0000305}.
CONFLICT 513 513 V -> A (in Ref. 2; BAE29344).
{ECO:0000305}.
CONFLICT 628 639 Missing (in Ref. 3; AAH33406).
{ECO:0000305}.
SEQUENCE 732 AA; 79230 MW; 2EAC87F1936B7C83 CRC64;
MDNPGPSLRG AFGILGALER DRLTHLKHKL GSLCSGSQES KLLHAMVLLA LGQDTEARVS
LESLKMNTVA QLVAHQWADM ETTEGPEEPP DLSWTVARLY HLLAEENLCP ASTRDMAYQV
ALRDFASQGD HQLGQLQNEA WDRCSSDIKG DPSGFQPLHS HQGSLQPPSA SPAVTRSQPR
PIDTPDWSWG HTLHSTNSTA SLASHLEISQ SPTLAFLSSH HGTHGPSKLC NTPLDTQEPQ
LVPEGCQEPE EISWPPSVET SVSLGLPHEI SVPEVSPEEA SPILPDALAA PDTSVHCPIE
CTELSTNSRS PLTSTTESVG KQWPITSQRS PQVPVGDDSL QNTTSSSPPA QPPSLQASPK
LPPSPLSSAS SPSSYPAPPT STSPVLDHSE TSDQKFYNFV VIHARADEQV ALRIREKLET
LGVPDGATFC EEFQVPGRGE LHCLQDAIDH SGFTILLLTA SFDCSLSLHQ INHALMNSLT
QSGRQDCVIP LLPLECSQAQ LSPDTTRLLH SIVWLDEHSP IFARKVANTF KTQKLQAQRV
RWKKAQEART LKEQSIQLEA ERQNVAAISA AYTAYVHSYR AWQAEMNKLG VAFGKNLSLG
TPTPSWPGCP QPIPSHPQGG TPVFPYSPQP PSFPQPPCFP QPPSFPQPPS FPLPPVSSPQ
SQSFPSASSP APQTPGPQPL IIHHAQMVQL GVNNHMWGHT GAQSSDDKTE CSENPCMGPL
TDQGEPLLET PE


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