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TIR domain-containing adapter molecule 1 (TICAM-1) (Proline-rich, vinculin and TIR domain-containing protein B) (Putative NF-kappa-B-activating protein 502H) (Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta) (MyD88-3) (TIR domain-containing adapter protein inducing IFN-beta)

 TCAM1_HUMAN             Reviewed;         712 AA.
Q8IUC6; B3Y691; O75532; Q86XP8; Q96GA0;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
22-NOV-2017, entry version 136.
RecName: Full=TIR domain-containing adapter molecule 1;
Short=TICAM-1;
AltName: Full=Proline-rich, vinculin and TIR domain-containing protein B;
AltName: Full=Putative NF-kappa-B-activating protein 502H;
AltName: Full=Toll-interleukin-1 receptor domain-containing adapter protein inducing interferon beta;
Short=MyD88-3;
Short=TIR domain-containing adapter protein inducing IFN-beta;
Name=TICAM1; Synonyms=PRVTIRB, TRIF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DOMAIN, AND
INTERACTION WITH IRF3; TLR2 AND TLR3.
PubMed=12471095; DOI=10.4049/jimmunol.169.12.6668;
Yamamoto M., Sato S., Mori K., Hoshino K., Takeuchi O., Takeda K.,
Akira S.;
"A novel Toll/IL-1 receptor domain-containing adapter that
preferentially activates the IFN-beta promoter in the Toll-like
receptor signaling.";
J. Immunol. 169:6668-6672(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TLR3, SUBUNIT,
TISSUE SPECIFICITY, DOMAIN, AND MUTAGENESIS OF PRO-434.
TISSUE=Lung;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=18810425; DOI=10.1007/s00251-008-0332-0;
Nakajima T., Ohtani H., Satta Y., Uno Y., Akari H., Ishida T.,
Kimura A.;
"Natural selection in the TLR-related genes in the course of primate
evolution.";
Immunogenetics 60:727-735(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=12761501; DOI=10.1038/sj.onc.1206406;
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
Sugano S.;
"Large-scale identification and characterization of human genes that
activate NF-kappaB and MAPK signaling pathways.";
Oncogene 22:3307-3318(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary, and Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 137-712.
Begum N.A.;
"PRVTIRB is a differentially expressed gene.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 297-712.
TISSUE=Brain;
Yu W., Gibbs R.A.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[8]
INTERACTION WITH TICAM2.
PubMed=12721283; DOI=10.1074/jbc.M303451200;
Bin L.-H., Xu L.-G., Shu H.-B.;
"TIRP, a novel Toll/interleukin-1 receptor (TIR) domain-containing
adapter protein involved in TIR signaling.";
J. Biol. Chem. 278:24526-24532(2003).
[9]
INTERACTION WITH TRAF6 AND TBK1, PHOSPHORYLATION BY TBK1, MOTIF, AND
MUTAGENESIS OF GLU-88; GLU-252 AND GLU-303.
PubMed=14530355; DOI=10.4049/jimmunol.171.8.4304;
Sato S., Sugiyama M., Yamamoto M., Watanabe Y., Kawai T., Takeda K.,
Akira S.;
"Toll/IL-1 receptor domain-containing adaptor inducing IFN-beta (TRIF)
associates with TNF receptor-associated factor 6 and TANK-binding
kinase 1, and activates two distinct transcription factors, NF-kappa B
and IFN-regulatory factor-3, in the Toll-like receptor signaling.";
J. Immunol. 171:4304-4310(2003).
[10]
INTERACTION WITH PIAS4.
PubMed=15251447; DOI=10.1016/j.febslet.2004.05.081;
Zhang J., Xu L.G., Han K.J., Wei X., Shu H.B.;
"PIASy represses TRIF-induced ISRE and NF-kappaB activation but not
apoptosis.";
FEBS Lett. 570:97-101(2004).
[11]
FUNCTION, INTERACTION WITH IKBKB; IKBKE; IRF3; IRF7; TBK1 AND TRAF6,
AND DOMAIN.
PubMed=14739303; DOI=10.1074/jbc.M311629200;
Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.;
"Mechanisms of the TRIF-induced interferon-stimulated response element
and NF-kappaB activation and apoptosis pathways.";
J. Biol. Chem. 279:15652-15661(2004).
[12]
INTERACTION WITH TRAF6, AND MUTAGENESIS OF GLU-252 AND GLU-493.
PubMed=14982987; DOI=10.1073/pnas.0308496101;
Jiang Z., Mak T.W., Sen G., Li X.;
"Toll-like receptor 3-mediated activation of NF-kappaB and IRF3
diverges at Toll-IL-1 receptor domain-containing adapter inducing IFN-
beta.";
Proc. Natl. Acad. Sci. U.S.A. 101:3533-3538(2004).
[13]
INTERACTION WITH AZI2.
PubMed=15611223; DOI=10.4049/jimmunol.174.1.27;
Sasai M., Oshiumi H., Matsumoto M., Inoue N., Fujita F., Nakanishi M.,
Seya T.;
"NF-kappaB-activating kinase-associated protein 1 participates in
TLR3/Toll-IL-1 homology domain-containing adapter molecule-1-mediated
IFN regulatory factor 3 activation.";
J. Immunol. 174:27-30(2005).
[14]
INTERACTION WITH SARM1.
PubMed=16964262; DOI=10.1038/ni1382;
Carty M., Goodbody R., Schroeder M., Stack J., Moynagh P.N.,
Bowie A.G.;
"The human adaptor SARM negatively regulates adaptor protein TRIF-
dependent Toll-like receptor signaling.";
Nat. Immunol. 7:1074-1081(2006).
[15]
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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
SUBCELLULAR LOCATION, AND INTERACTION WITH UBQLN1.
PubMed=21695056; DOI=10.1371/journal.pone.0021153;
Biswas N., Liu S., Ronni T., Aussenberg S.E., Liu W., Fujita T.,
Wang T.;
"The ubiquitin-like protein PLIC-1 or ubiquilin 1 inhibits TLR3-Trif
signaling.";
PLoS ONE 6:E21153-E21153(2011).
[18]
INTERACTION WITH TRIM56.
PubMed=22948160; DOI=10.1074/jbc.M112.397075;
Shen Y., Li N.L., Wang J., Liu B., Lester S., Li K.;
"TRIM56 is an essential component of the TLR3 antiviral signaling
pathway.";
J. Biol. Chem. 287:36404-36413(2012).
[19]
UBIQUITINATION BY TRIM38, AND MUTAGENESIS OF ASP-281 AND ASP-289.
PubMed=23056470; DOI=10.1371/journal.pone.0046825;
Xue Q., Zhou Z., Lei X., Liu X., He B., Wang J., Hung T.;
"TRIM38 negatively regulates TLR3-mediated IFN-beta signaling by
targeting TRIF for degradation.";
PLoS ONE 7:E46825-E46825(2012).
[20]
INTERACTION WITH TLR3; TICAM2; RIPK1; TRAF6 AND TBK1.
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).
[21]
X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 1-153, AND TRIF-NTD REGION.
PubMed=24311583; DOI=10.1107/S0907444913022385;
Ullah M.O., Ve T., Mangan M., Alaidarous M., Sweet M.J., Mansell A.,
Kobe B.;
"The TLR signalling adaptor TRIF/TICAM-1 has an N-terminal helical
domain with structural similarity to IFIT proteins.";
Acta Crystallogr. D 69:2420-2430(2013).
[22]
VARIANT [LARGE SCALE ANALYSIS] ILE-46.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[23]
VARIANT HSE4 LEU-186.
PubMed=22105173; DOI=10.1172/JCI59259;
Sancho-Shimizu V., Perez de Diego R., Lorenzo L., Halwani R.,
Alangari A., Israelsson E., Fabrega S., Cardon A., Maluenda J.,
Tatematsu M., Mahvelati F., Herman M., Ciancanelli M., Guo Y.,
AlSum Z., Alkhamis N., Al-Makadma A.S., Ghadiri A., Boucherit S.,
Plancoulaine S., Picard C., Rozenberg F., Tardieu M., Lebon P.,
Jouanguy E., Rezaei N., Seya T., Matsumoto M., Chaussabel D., Puel A.,
Zhang S.Y., Abel L., Al-Muhsen S., Casanova J.L.;
"Herpes simplex encephalitis in children with autosomal recessive and
dominant TRIF deficiency.";
J. Clin. Invest. 121:4889-4902(2011).
-!- 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:12471095,
ECO:0000269|PubMed:12539043, ECO:0000269|PubMed:14739303}.
-!- SUBUNIT: Homodimer (Probable). Interacts with AZI2, IRF3 and IRF7.
Interacts with TICAM2 in TLR4 recruitment. Interaction with PIAS4
inhibits the TICAM1-induced NF-kappa-B, IRF and IFNB1 activation.
Interacts with IKBKB and IKBKE. Interaction with SARM1 blocks
TICAM1-dependent transcription factor activation. Interacts with
TRAF3 (By similarity). Interacts with TBK1, TRAF6 and RIPK1 and
these interactions are enhanced in the presence of WDFY1
(PubMed:25736436). Interacts with TRAFD1 (By similarity).
Interacts with UBQLN1 (via UBA domain). Interacts with TLR4 in
response to LPS in a WDFY1-dependent manner (By similarity).
Interacts with WDFY1 in response to poly(I:C) (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 TRIM56 (PubMed:22948160).
{ECO:0000250|UniProtKB:Q80UF7, ECO:0000269|PubMed:21695056,
ECO:0000269|PubMed:22948160, ECO:0000269|PubMed:25736436,
ECO:0000305}.
-!- INTERACTION:
Q9UHD2:TBK1; NbExp=3; IntAct=EBI-525995, EBI-356402;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
{ECO:0000269|PubMed:21695056}. Note=Colocalizes with UBQLN1 in the
autophagosome. {ECO:0000269|PubMed:21695056}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed but with higher levels
in liver. {ECO:0000269|PubMed:12471095,
ECO:0000269|PubMed:12539043}.
-!- DOMAIN: The N-terminal region is essential for activation of the
IFNB promoter activity. {ECO:0000269|PubMed:12471095,
ECO:0000269|PubMed:12539043, ECO:0000269|PubMed:14739303}.
-!- 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:0000269|PubMed:24311583}.
-!- PTM: Phosphorylated by TBK1. {ECO:0000269|PubMed:14530355}.
-!- PTM: Polyubiquitinated by TRIM38 with 'Lys-48'-linked chains,
leading to proteasomal degradation. {ECO:0000269|PubMed:23056470}.
-!- DISEASE: Herpes simplex encephalitis 4 (HSE4) [MIM:614850]: A rare
complication of human herpesvirus 1 (HHV-1) infection, occurring
in only a small minority of HHV-1 infected individuals. HSE is
characterized by hemorrhagic necrosis of parts of the temporal and
frontal lobes. Onset is over several days and involves fever,
headache, seizures, stupor, and often coma, frequently with a
fatal outcome. {ECO:0000269|PubMed:22105173}. Note=Disease
susceptibility is associated with variations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAO85488.1; Type=Frameshift; Positions=141, 148, 161; Evidence={ECO:0000305};
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EMBL; AB093555; BAC44839.1; -; mRNA.
EMBL; AB086380; BAC55579.1; -; mRNA.
EMBL; AB446484; BAG55261.1; -; mRNA.
EMBL; AB097023; BAC77376.1; -; mRNA.
EMBL; BC009860; AAH09860.2; -; mRNA.
EMBL; BC136556; AAI36557.1; -; mRNA.
EMBL; BC136557; AAI36558.1; -; mRNA.
EMBL; AF492646; AAO85488.1; ALT_FRAME; mRNA.
EMBL; AF070530; AAC28630.1; -; mRNA.
CCDS; CCDS12136.1; -.
RefSeq; NP_891549.1; NM_182919.3.
UniGene; Hs.29344; -.
PDB; 2M1X; NMR; -; A=387-545.
PDB; 2M63; NMR; -; A=1-156.
PDB; 3RC4; X-ray; 1.50 A; B=360-372.
PDB; 4BSX; X-ray; 2.23 A; A/B/C/D=1-153.
PDB; 4C0M; X-ray; 2.80 A; A/B/C/D=1-153.
PDB; 5JEL; X-ray; 1.60 A; B=199-217.
PDBsum; 2M1X; -.
PDBsum; 2M63; -.
PDBsum; 3RC4; -.
PDBsum; 4BSX; -.
PDBsum; 4C0M; -.
PDBsum; 5JEL; -.
ProteinModelPortal; Q8IUC6; -.
SMR; Q8IUC6; -.
BioGrid; 127114; 35.
CORUM; Q8IUC6; -.
DIP; DIP-33490N; -.
IntAct; Q8IUC6; 11.
MINT; MINT-1202912; -.
STRING; 9606.ENSP00000248244; -.
iPTMnet; Q8IUC6; -.
PhosphoSitePlus; Q8IUC6; -.
BioMuta; TICAM1; -.
DMDM; 74727957; -.
MaxQB; Q8IUC6; -.
PaxDb; Q8IUC6; -.
PeptideAtlas; Q8IUC6; -.
PRIDE; Q8IUC6; -.
Ensembl; ENST00000248244; ENSP00000248244; ENSG00000127666.
GeneID; 148022; -.
KEGG; hsa:148022; -.
UCSC; uc002mbi.5; human.
CTD; 148022; -.
DisGeNET; 148022; -.
EuPathDB; HostDB:ENSG00000127666.9; -.
GeneCards; TICAM1; -.
HGNC; HGNC:18348; TICAM1.
HPA; HPA042460; -.
MalaCards; TICAM1; -.
MIM; 607601; gene.
MIM; 614850; phenotype.
neXtProt; NX_Q8IUC6; -.
OpenTargets; ENSG00000127666; -.
Orphanet; 1930; Herpetic encephalitis.
PharmGKB; PA142670812; -.
eggNOG; ENOG410IJUV; Eukaryota.
eggNOG; ENOG410Y8DE; LUCA.
GeneTree; ENSGT00900000141066; -.
HOGENOM; HOG000068973; -.
HOVERGEN; HBG108551; -.
InParanoid; Q8IUC6; -.
KO; K05842; -.
OMA; EEKLCPA; -.
OrthoDB; EOG091G07G7; -.
PhylomeDB; Q8IUC6; -.
TreeFam; TF336953; -.
Reactome; R-HSA-140534; Ligand-dependent caspase activation.
Reactome; R-HSA-166166; MyD88-independent TLR4 cascade.
Reactome; R-HSA-168164; Toll Like Receptor 3 (TLR3) Cascade.
Reactome; R-HSA-168180; TRAF6 Mediated Induction of proinflammatory cytokines.
Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-2562578; TRIF-mediated programmed cell death.
Reactome; R-HSA-5602566; TICAM1 deficiency - HSE.
Reactome; R-HSA-5602571; TRAF3 deficiency - HSE.
Reactome; R-HSA-9013957; TLR3-mediated TICAM1-dependent programmed cell death.
Reactome; R-HSA-9013973; TICAM1-dependent activation of IRF3/IRF7.
Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
SignaLink; Q8IUC6; -.
SIGNOR; Q8IUC6; -.
ChiTaRS; TICAM1; human.
EvolutionaryTrace; Q8IUC6; -.
GenomeRNAi; 148022; -.
PRO; PR:Q8IUC6; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000127666; -.
CleanEx; HS_TICAM1; -.
ExpressionAtlas; Q8IUC6; baseline and differential.
Genevisible; Q8IUC6; HS.
GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0097342; C:ripoptosome; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:ParkinsonsUK-UCL.
GO; GO:0140052; P:cellular response to oxidised low-density lipoprotein particle stimulus; ISS:ARUK-UCL.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
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; IEA:Ensembl.
GO; GO:0002281; P:macrophage activation involved in immune response; IEA:Ensembl.
GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0070266; P:necroptotic process; TAS:Reactome.
GO; GO:0034128; P:negative regulation of MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0010508; P:positive regulation of autophagy; ISS:ParkinsonsUK-UCL.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IEA:Ensembl.
GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISS:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0045359; P:positive regulation of interferon-beta biosynthetic process; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0032816; P:positive regulation of natural killer cell activation; 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:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0043496; P:regulation of protein homodimerization activity; IEA:Ensembl.
GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; ISS: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;
3D-structure; Antiviral defense; Apoptosis; Complete proteome;
Cytoplasmic vesicle; Disease mutation; Immunity;
Inflammatory response; Innate immunity; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 712 TIR domain-containing adapter molecule 1.
/FTId=PRO_0000317663.
DOMAIN 390 460 TIR.
REGION 1 153 TRIF-NTD. {ECO:0000269|PubMed:24311583}.
REGION 512 712 Sufficient to induce apoptosis.
MOTIF 84 91 TRAF6-binding.
MOTIF 248 255 TRAF6-binding.
MOTIF 299 309 TRAF6-binding.
COMPBIAS 213 371 Pro-rich.
COMPBIAS 614 678 Pro-rich.
VARIANT 46 46 M -> I (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_038789.
VARIANT 75 75 R -> C (in dbSNP:rs11466719).
/FTId=VAR_051416.
VARIANT 186 186 S -> L (in HSE4; dbSNP:rs146550489).
{ECO:0000269|PubMed:22105173}.
/FTId=VAR_069082.
VARIANT 275 275 L -> V (in dbSNP:rs11466721).
/FTId=VAR_051417.
VARIANT 666 666 A -> T (in dbSNP:rs11466724).
/FTId=VAR_051418.
MUTAGEN 88 88 E->A: Reduces binding to TRAF6 and
activation of NFKB signaling pathway;
when associated with A-252 and A-303.
{ECO:0000269|PubMed:14530355}.
MUTAGEN 252 252 E->A: Loss of TCAM1-induced NF-kappa-B
activation. Reduces interaction with
TRAF6 and activation of NF-kappa-B
signaling pathway; when associated with
A-88 and A-303.
{ECO:0000269|PubMed:14530355,
ECO:0000269|PubMed:14982987}.
MUTAGEN 281 281 D->E: Resistant to caspase cleavage, no
effect on TRIM38-mediated degradation;
when associated with E-289.
{ECO:0000269|PubMed:23056470}.
MUTAGEN 289 289 D->E: Resistant to caspase cleavage, no
effect on TRIM38-mediated degradation;
when associated with E-281.
{ECO:0000269|PubMed:23056470}.
MUTAGEN 303 303 E->A: Reduces binding to TRAF6 and
activation of NFKB signaling pathway;
when associated with A-88 and A-252.
{ECO:0000269|PubMed:14530355}.
MUTAGEN 434 434 P->H: Abolishes interaction with TLR3.
{ECO:0000269|PubMed:12539043}.
MUTAGEN 493 493 E->A: Loss of TCAM1-induced NF-kappa-B
and IRF3 activation.
{ECO:0000269|PubMed:14982987}.
CONFLICT 147 147 D -> T (in Ref. 6; AAO85488).
{ECO:0000305}.
CONFLICT 150 150 G -> W (in Ref. 6; AAO85488).
{ECO:0000305}.
CONFLICT 162 162 L -> S (in Ref. 6; AAO85488).
{ECO:0000305}.
CONFLICT 633 659 Missing (in Ref. 6; AAO85488).
{ECO:0000305}.
CONFLICT 660 660 S -> P (in Ref. 6; AAO85488).
{ECO:0000305}.
HELIX 8 16 {ECO:0000244|PDB:4BSX}.
HELIX 20 30 {ECO:0000244|PDB:4BSX}.
HELIX 40 50 {ECO:0000244|PDB:4BSX}.
HELIX 54 62 {ECO:0000244|PDB:4BSX}.
TURN 63 66 {ECO:0000244|PDB:4BSX}.
HELIX 68 76 {ECO:0000244|PDB:4BSX}.
STRAND 83 85 {ECO:0000244|PDB:4BSX}.
HELIX 93 105 {ECO:0000244|PDB:4BSX}.
HELIX 111 127 {ECO:0000244|PDB:4BSX}.
HELIX 133 144 {ECO:0000244|PDB:4BSX}.
HELIX 200 206 {ECO:0000244|PDB:5JEL}.
STRAND 369 371 {ECO:0000244|PDB:3RC4}.
HELIX 406 417 {ECO:0000244|PDB:2M1X}.
STRAND 431 433 {ECO:0000244|PDB:2M1X}.
HELIX 444 447 {ECO:0000244|PDB:2M1X}.
STRAND 448 455 {ECO:0000244|PDB:2M1X}.
HELIX 462 475 {ECO:0000244|PDB:2M1X}.
TURN 477 480 {ECO:0000244|PDB:2M1X}.
STRAND 486 490 {ECO:0000244|PDB:2M1X}.
STRAND 492 494 {ECO:0000244|PDB:2M1X}.
HELIX 503 506 {ECO:0000244|PDB:2M1X}.
STRAND 508 510 {ECO:0000244|PDB:2M1X}.
STRAND 513 516 {ECO:0000244|PDB:2M1X}.
HELIX 520 527 {ECO:0000244|PDB:2M1X}.
HELIX 530 535 {ECO:0000244|PDB:2M1X}.
TURN 536 540 {ECO:0000244|PDB:2M1X}.
HELIX 541 543 {ECO:0000244|PDB:2M1X}.
SEQUENCE 712 AA; 76422 MW; 5D071E3BE9240D9A CRC64;
MACTGPSLPS AFDILGAAGQ DKLLYLKHKL KTPRPGCQGQ DLLHAMVLLK LGQETEARIS
LEALKADAVA RLVARQWAGV DSTEDPEEPP DVSWAVARLY HLLAEEKLCP ASLRDVAYQE
AVRTLSSRDD HRLGELQDEA RNRCGWDIAG DPGSIRTLQS NLGCLPPSSA LPSGTRSLPR
PIDGVSDWSQ GCSLRSTGSP ASLASNLEIS QSPTMPFLSL HRSPHGPSKL CDDPQASLVP
EPVPGGCQEP EEMSWPPSGE IASPPELPSS PPPGLPEVAP DATSTGLPDT PAAPETSTNY
PVECTEGSAG PQSLPLPILE PVKNPCSVKD QTPLQLSVED TTSPNTKPCP PTPTTPETSP
PPPPPPPSST PCSAHLTPSS LFPSSLESSS EQKFYNFVIL HARADEHIAL RVREKLEALG
VPDGATFCED FQVPGRGELS CLQDAIDHSA FIILLLTSNF DCRLSLHQVN QAMMSNLTRQ
GSPDCVIPFL PLESSPAQLS SDTASLLSGL VRLDEHSQIF ARKVANTFKP HRLQARKAMW
RKEQDTRALR EQSQHLDGER MQAAALNAAY SAYLQSYLSY QAQMEQLQVA FGSHMSFGTG
APYGARMPFG GQVPLGAPPP FPTWPGCPQP PPLHAWQAGT PPPPSPQPAA FPQSLPFPQS
PAFPTASPAP PQSPGLQPLI IHHAQMVQLG LNNHMWNQRG SQAPEDKTQE AE


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