TCAM1_MOUSE
ID TCAM1_MOUSE Reviewed; 732 AA.
AC Q80UF7; Q3UDB7; Q3UP66; Q6P6J2; Q8CIB7; Q8JZV0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=TIR domain-containing adapter molecule 1;
DE Short=TICAM-1;
DE AltName: Full=Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta;
DE Short=TIR domain-containing adapter protein inducing IFN-beta;
GN Name=Ticam1; Synonyms=Trif;
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].
RX PubMed=12539043; DOI=10.1038/ni886;
RA Oshiumi H., Matsumoto M., Funami K., Akazawa T., Seya T.;
RT "TICAM-1, an adapter molecule that participates in Toll-like receptor 3
RT mediated interferon-beta induction.";
RL Nat. Immunol. 4:161-167(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, FVB/N, and FVB/N-3;
RC TISSUE=Eye, Jaw, Limb, Mammary tumor, and Salivary gland;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12855817; DOI=10.1126/science.1087262;
RA Yamamoto M., Sato S., Hemmi H., Hoshino K., Kaisho T., Sanjo H.,
RA Takeuchi O., Sugiyama M., Okabe M., Takeda K., Akira S.;
RT "Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling
RT pathway.";
RL Science 301:640-643(2003).
RN [5]
RP FUNCTION.
RX PubMed=16002681; DOI=10.4049/jimmunol.175.2.839;
RA De Trez C., Pajak B., Brait M., Glaichenhaus N., Urbain J., Moser M.,
RA Lauvau G., Muraille E.;
RT "TLR4 and Toll-IL-1 receptor domain-containing adapter-inducing IFN-beta,
RT but not MyD88, regulate Escherichia coli-induced dendritic cell maturation
RT and apoptosis in vivo.";
RL J. Immunol. 175:839-846(2005).
RN [6]
RP INTERACTION WITH TRAF3.
RX PubMed=16306936; DOI=10.1038/nature04374;
RA Oganesyan G., Saha S.K., Guo B., He J.Q., Shahangian A., Zarnegar B.,
RA Perry A., Cheng G.;
RT "Critical role of TRAF3 in the Toll-like receptor-dependent and
RT -independent antiviral response.";
RL Nature 439:208-211(2006).
RN [7]
RP REVIEW.
RX PubMed=17457343; DOI=10.1038/nri2079;
RA O'Neill L.A., Bowie A.G.;
RT "The family of five: TIR-domain-containing adaptors in Toll-like receptor
RT signalling.";
RL Nat. Rev. Immunol. 7:353-364(2007).
RN [8]
RP INTERACTION WITH TRAFD1.
RX PubMed=18849341; DOI=10.1074/jbc.m806923200;
RA Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T., Yoshimura A.;
RT "FLN29 deficiency reveals its negative regulatory role in the Toll-like
RT receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like helicase
RT signaling pathway.";
RL J. Biol. Chem. 283:33858-33864(2008).
RN [9]
RP FUNCTION, INTERACTION WITH DDX21 AND DHX36, IDENTIFICATION IN A COMPLEX
RP WITH DDX1; DDX21 AND DHX36, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21703541; DOI=10.1016/j.immuni.2011.03.027;
RA Zhang Z., Kim T., Bao M., Facchinetti V., Jung S.Y., Ghaffari A.A., Qin J.,
RA Cheng G., Liu Y.J.;
RT "DDX1, DDX21, and DHX36 helicases form a complex with the adaptor molecule
RT TRIF to sense dsRNA in dendritic cells.";
RL Immunity 34:866-878(2011).
RN [10]
RP INTERACTION WITH WDFY1; TLR3 AND TLR4.
RX PubMed=25736436; DOI=10.15252/embr.201439637;
RA Hu Y.H., Zhang Y., Jiang L.Q., Wang S., Lei C.Q., Sun M.S., Shu H.B.,
RA Liu Y.;
RT "WDFY1 mediates TLR3/4 signaling by recruiting TRIF.";
RL EMBO Rep. 16:447-455(2015).
RN [11]
RP UBIQUITINATION AT LYS-228, AND MUTAGENESIS OF LYS-228 AND LYS-321.
RX PubMed=26392463; DOI=10.4049/jimmunol.1500859;
RA Hu M.M., Xie X.Q., Yang Q., Liao C.Y., Ye W., Lin H., Shu H.B.;
RT "TRIM38 negatively regulates TLR3/4-mediated innate immune and inflammatory
RT responses by two sequential and distinct mechanisms.";
RL J. Immunol. 195:4415-4425(2015).
CC -!- FUNCTION: Involved in innate immunity against invading pathogens.
CC Adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate NF-
CC kappa-B and interferon-regulatory factor (IRF) activation, and to
CC induce apoptosis (PubMed:12855817, PubMed:16002681, PubMed:21703541).
CC Ligand binding to these receptors results in TRIF recruitment through
CC its TIR domain (PubMed:12855817, PubMed:16002681, PubMed:21703541).
CC Distinct protein-interaction motifs allow recruitment of the effector
CC proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation
CC of transcription factors IRF3 and IRF7, NF-kappa-B and FADD
CC respectively (PubMed:12855817, PubMed:16002681, PubMed:21703541).
CC Phosphorylation by TBK1 on the pLxIS motif leads to recruitment and
CC subsequent activation of the transcription factor IRF3 to induce
CC expression of type I interferon and exert a potent immunity against
CC invading pathogens (By similarity). Component of a multi-helicase-
CC TICAM1 complex that acts as a cytoplasmic sensor of viral double-
CC stranded RNA (dsRNA) and plays a role in the activation of a cascade of
CC antiviral responses including the induction of pro-inflammatory
CC cytokines (PubMed:21703541). {ECO:0000250|UniProtKB:Q8IUC6,
CC ECO:0000269|PubMed:12855817, ECO:0000269|PubMed:16002681,
CC ECO:0000269|PubMed:21703541}.
CC -!- SUBUNIT: Homodimer (By similarity). Found in a multi-helicase-TICAM1
CC complex at least composed of DHX36, DDX1, DDX21 and TICAM1; this
CC complex exists in resting cells with or without poly(I:C) RNA ligand
CC stimulation (PubMed:21703541). Interacts (via TIR domain) with DDX21
CC (via C-terminus) (PubMed:21703541). Interacts (via TIR domain) with
CC DHX36 (via C-terminus) (PubMed:21703541). Interacts with AZI2 and IRF7
CC (By similarity). Interacts (when phosphorylated) with IRF3; following
CC activation and phosphorylation on the pLxIS motif by TBK1, recruits
CC IRF3 (By similarity). Interacts with TICAM2 in TLR4 recruitment (By
CC similarity). Interaction with PIAS4 inhibits the TICAM1-induced NF-
CC kappa-B, IRF and IFNB1 activation (By similarity). Interacts with IKBKB
CC and IKBKE (By similarity). Interaction with SARM1 blocks TICAM1-
CC dependent transcription factor activation (By similarity). Interacts
CC with TRAF3. Interacts with TRAFD1. Interacts with UBQLN1 (via UBA
CC domain). Interacts with TBK1, TRAF6 and RIPK1 and these interactions
CC are enhanced in the presence of WDFY1 (By similarity). Interacts (via
CC the TIR domain) with TLR3 in response to poly(I:C) and this interaction
CC is enhanced in the presence of WDFY1 (PubMed:25736436). Interacts with
CC TLR4 in response to poly(I:C) in a WDFY1-dependent manner
CC (PubMed:25736436). Interacts with WDFY1 in response to poly(I:C)
CC (PubMed:25736436). Interacts with TRIM56 (By similarity). Interacts
CC (via the TIR domain) with TLR5 (By similarity). Interacts with TRIM8
CC (By similarity). {ECO:0000250|UniProtKB:Q8IUC6,
CC ECO:0000269|PubMed:16306936, ECO:0000269|PubMed:18849341,
CC ECO:0000269|PubMed:21703541, ECO:0000269|PubMed:25736436}.
CC -!- INTERACTION:
CC Q80UF7; P35991: Btk; NbExp=2; IntAct=EBI-3649271, EBI-625119;
CC Q80UF7; Q3TTA7: Cblb; NbExp=2; IntAct=EBI-3649271, EBI-3649276;
CC Q80UF7; Q9WUN2: Tbk1; NbExp=2; IntAct=EBI-3649271, EBI-764193;
CC Q80UF7; Q60803: Traf3; NbExp=2; IntAct=EBI-3649271, EBI-520135;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21703541}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8IUC6}.
CC Mitochondrion {ECO:0000269|PubMed:21703541}. Note=Colocalizes with
CC UBQLN1 in the autophagosome. Colocalizes in the cytosol with DDX1,
CC DDX21 and DHX36 (PubMed:21703541). Colocalizes in the mitochondria with
CC DDX1 and poly(I:C) RNA ligand (PubMed:21703541). The multi-helicase-
CC TICAM1 complex may translocate to the mitochondria upon poly(I:C) RNA
CC ligand stimulation (PubMed:21703541). {ECO:0000250|UniProtKB:Q8IUC6,
CC ECO:0000269|PubMed:21703541}.
CC -!- DOMAIN: The pLxIS motif constitutes an IRF3-binding motif: following
CC phosphorylation by TBK1, the phosphorylated pLxIS motif of TICAM1
CC recruits IRF3. IRF3 is then phosphorylated and activated by TBK1 to
CC induce type-I interferons and other cytokines.
CC {ECO:0000250|UniProtKB:Q8IUC6}.
CC -!- DOMAIN: The N-terminal region is essential for activation of the IFNB
CC promoter activity. {ECO:0000250|UniProtKB:Q8IUC6}.
CC -!- DOMAIN: The N-terminal domain (TRIF-NTD) is globular and consists of
CC two alpha-helical subdomains connected by a 14-residue linker. It
CC shares structural similarity with IFIT family members N-terminal
CC regions. {ECO:0000250|UniProtKB:Q8IUC6}.
CC -!- PTM: Phosphorylated by TBK1. Following activation, phosphorylated by
CC TBK1 at Ser-209 in the pLxIS motif. The phosphorylated pLxIS motif
CC constitutes an IRF3-binding motif, leading to recruitment of the
CC transcription factor IRF3 to induce type-I interferons and other
CC cytokines. {ECO:0000250|UniProtKB:Q8IUC6}.
CC -!- PTM: Polyubiquitinated at Lys-228 by TRIM38 with 'Lys-48'-linked
CC chains, leading to proteasomal degradation (PubMed:26392463).
CC Polyubiquitinated with 'Lys-6'- and 'Lys-33'-linked chains in a TRIM8-
CC dependent manner; ubiquitination disrupts the interaction with TBK1 and
CC subsequent interferon production (By similarity).
CC {ECO:0000250|UniProtKB:Q8IUC6, ECO:0000269|PubMed:26392463}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable but exhibit abnormalities of the
CC innate immune system. {ECO:0000269|PubMed:12855817}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33406.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
CC Sequence=AAH37048.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH62191.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB091053; BAC55581.1; -; mRNA.
DR EMBL; AK143766; BAE25531.1; -; mRNA.
DR EMBL; AK150150; BAE29344.1; -; mRNA.
DR EMBL; AK155245; BAE33144.1; -; mRNA.
DR EMBL; BC033406; AAH33406.1; ALT_SEQ; mRNA.
DR EMBL; BC037048; AAH37048.1; ALT_INIT; mRNA.
DR EMBL; BC062191; AAH62191.1; ALT_FRAME; mRNA.
DR EMBL; BC094338; AAH94338.1; -; mRNA.
DR CCDS; CCDS28900.1; -.
DR RefSeq; NP_778154.1; NM_174989.4.
DR AlphaFoldDB; Q80UF7; -.
DR SMR; Q80UF7; -.
DR BioGRID; 223122; 9.
DR DIP; DIP-60033N; -.
DR IntAct; Q80UF7; 6.
DR STRING; 10090.ENSMUSP00000055104; -.
DR PhosphoSitePlus; Q80UF7; -.
DR EPD; Q80UF7; -.
DR PaxDb; Q80UF7; -.
DR PRIDE; Q80UF7; -.
DR ProteomicsDB; 263143; -.
DR Antibodypedia; 11536; 361 antibodies from 42 providers.
DR DNASU; 106759; -.
DR Ensembl; ENSMUST00000058136; ENSMUSP00000055104; ENSMUSG00000047123.
DR GeneID; 106759; -.
DR KEGG; mmu:106759; -.
DR UCSC; uc008dbm.2; mouse.
DR CTD; 148022; -.
DR MGI; MGI:2147032; Ticam1.
DR VEuPathDB; HostDB:ENSMUSG00000047123; -.
DR eggNOG; ENOG502RXF3; Eukaryota.
DR GeneTree; ENSGT00940000162411; -.
DR HOGENOM; CLU_022539_0_0_1; -.
DR InParanoid; Q80UF7; -.
DR OMA; GVNNHMW; -.
DR OrthoDB; 435629at2759; -.
DR PhylomeDB; Q80UF7; -.
DR TreeFam; TF336953; -.
DR Reactome; R-MMU-140534; Caspase activation via Death Receptors in the presence of ligand.
DR Reactome; R-MMU-166166; MyD88-independent TLR4 cascade.
DR Reactome; R-MMU-2562578; TRIF-mediated programmed cell death.
DR Reactome; R-MMU-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
DR Reactome; R-MMU-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-MMU-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-MMU-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR BioGRID-ORCS; 106759; 5 hits in 74 CRISPR screens.
DR PRO; PR:Q80UF7; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q80UF7; protein.
DR Bgee; ENSMUSG00000047123; Expressed in ureteric bud trunk and 137 other tissues.
DR Genevisible; Q80UF7; MM.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0097342; C:ripoptosome; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0042113; P:B cell activation; IMP:MGI.
DR GO; GO:0042100; P:B cell proliferation; IMP:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:ParkinsonsUK-UCL.
DR GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; IMP:ARUK-UCL.
DR GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:MGI.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IMP:MGI.
DR GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; IMP:MGI.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0050871; P:positive regulation of B cell activation; IMP:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; IMP: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:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IDA:MGI.
DR GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; IMP:UniProtKB.
DR GO; GO:0032816; P:positive regulation of natural killer cell activation; IMP:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IMP:MGI.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IMP:MGI.
DR GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; IMP:ParkinsonsUK-UCL.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR025735; RHIM_dom.
DR InterPro; IPR017278; TICAM1.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR InterPro; IPR040886; TRIF_N.
DR PANTHER; PTHR47230; PTHR47230; 1.
DR Pfam; PF12721; RHIM; 1.
DR Pfam; PF17798; TRIF-NTD; 1.
DR PIRSF; PIRSF037744; TIR_Ticam; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; Apoptosis; Cytoplasm; Cytoplasmic vesicle; Immunity;
KW Inflammatory response; Innate immunity; Isopeptide bond; Mitochondrion;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..732
FT /note="TIR domain-containing adapter molecule 1"
FT /id="PRO_0000317664"
FT DOMAIN 395..534
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 1..153
FT /note="TRIF-NTD"
FT /evidence="ECO:0000250|UniProtKB:Q8IUC6"
FT REGION 144..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..713
FT /note="Sufficient to induce apoptosis"
FT /evidence="ECO:0000250|UniProtKB:Q8IUC6"
FT REGION 603..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 84..91
FT /note="TRAF6-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8IUC6"
FT MOTIF 206..209
FT /note="pLxIS motif"
FT /evidence="ECO:0000250|UniProtKB:Q8IUC6"
FT MOTIF 247..254
FT /note="TRAF6-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8IUC6"
FT MOTIF 296..306
FT /note="TRAF6-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8IUC6"
FT COMPBIAS 157..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUC6"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:26392463"
FT MUTAGEN 228
FT /note="K->R: Abolished ubiquitination by TRIM38."
FT /evidence="ECO:0000269|PubMed:26392463"
FT MUTAGEN 321
FT /note="K->R: Does not affect ubiquitination by TRIM38."
FT /evidence="ECO:0000269|PubMed:26392463"
FT CONFLICT 227
FT /note="S -> G (in Ref. 2; BAE29344)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..435
FT /note="Missing (in Ref. 3; AAH62191)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="V -> A (in Ref. 2; BAE25531)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="V -> A (in Ref. 2; BAE29344)"
FT /evidence="ECO:0000305"
FT CONFLICT 628..639
FT /note="Missing (in Ref. 3; AAH33406)"
FT /evidence="ECO:0000305"
SQ 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
