##gff-version 3
Q86XR7	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed	
Q86XR7	UniProtKB	Chain	2	235	.	.	.	ID=PRO_0000317689;Note=TIR domain-containing adapter molecule 2	
Q86XR7	UniProtKB	Domain	73	229	.	.	.	Note=TIR;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00204	
Q86XR7	UniProtKB	Region	1	39	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q86XR7	UniProtKB	Compositional bias	24	39	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q86XR7	UniProtKB	Modified residue	16	16	.	.	.	Note=Phosphoserine%3B by PKC/PRKCE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16757566;Dbxref=PMID:16757566	
Q86XR7	UniProtKB	Modified residue	167	167	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25825441;Dbxref=PMID:25825441	
Q86XR7	UniProtKB	Lipidation	2	2	.	.	.	Note=N-myristoyl glycine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16603631;Dbxref=PMID:16603631	
Q86XR7	UniProtKB	Alternative sequence	1	20	.	.	.	ID=VSP_047437;Note=In isoform 2. MGIGKSKINSCPLSLSWGKR->MPRPGSAQRWAAVAGRWGCRLLALLLLVPGPGGASEITFELPDNAKQCFYEDIAQGTKCTLEFQVITGGHYDVDCRLEDPDGKVLYKEMKKQYDSFTFTASKNGTYKFCFSNEFSTFTHKTVYFDFQVGEDPPLFPSENRVSALTQMESACVSIHEALKSVIDYQTHFRLREAQGRSRAEDLNTRVAYW;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:19412184;Dbxref=PMID:19412184	
Q86XR7	UniProtKB	Mutagenesis	2	2	.	.	.	Note=Results in relocalization from membrane to cytosol%3B Loss of ability to transduce TLR4-signal. Loss of TLR2-mediated activation of IRF7. G->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16603631,ECO:0000269|PubMed:25385819;Dbxref=PMID:16603631,PMID:25385819	
Q86XR7	UniProtKB	Mutagenesis	6	6	.	.	.	Note=Loss of phosphorylation. Significant reduction in the ability to activate IRF3 or NF-kappa-B. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16757566;Dbxref=PMID:16757566	
Q86XR7	UniProtKB	Mutagenesis	10	10	.	.	.	Note=No effect on phosphorylation and on the ability to activate IRF3 or NF-kappa-B. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16757566;Dbxref=PMID:16757566	
Q86XR7	UniProtKB	Mutagenesis	14	14	.	.	.	Note=No effect on phosphorylation and on the ability to activate IRF3 or NF-kappa-B. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16757566;Dbxref=PMID:16757566	
Q86XR7	UniProtKB	Mutagenesis	16	16	.	.	.	Note=Loss of phosphorylation. Abolishes ability to activate IRF3 or NF-kappa-B and to transduce TLR4 signal. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16757566;Dbxref=PMID:16757566	
Q86XR7	UniProtKB	Mutagenesis	16	16	.	.	.	Note=Significant decrease of localization in the membrane. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16757566;Dbxref=PMID:16757566	
Q86XR7	UniProtKB	Mutagenesis	116	116	.	.	.	Note=Loss of ability to dimerize. Significant loss of RANTES-inducing activity. Loss of ability to induce NF-kappa-B activation. P->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517278,ECO:0000269|PubMed:14519765;Dbxref=PMID:14517278,PMID:14519765	
Q86XR7	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Loss of ability to dimerize. Loss of RANTES-inducing activity and ability to induce NF-kappa-B activation. Inhibition of TLR4-dependent activation of IRF3 and IRF7. Loss of interaction with TLR4. C->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517278,ECO:0000269|PubMed:14519765;Dbxref=PMID:14517278,PMID:14519765	
Q86XR7	UniProtKB	Mutagenesis	154	154	.	.	.	Note=No effect on phosphorylation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25825441;Dbxref=PMID:25825441	
Q86XR7	UniProtKB	Mutagenesis	167	167	.	.	.	Note=Complete loss of phosphorylation in response to LPS. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25825441;Dbxref=PMID:25825441	
Q86XR7	UniProtKB	Beta strand	80	84	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Beta strand	87	89	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Helix	90	100	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Turn	101	104	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Beta strand	108	111	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Turn	112	114	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Beta strand	118	120	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Helix	125	128	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Beta strand	130	133	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Beta strand	135	137	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Helix	141	153	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Helix	155	160	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Beta strand	166	168	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Beta strand	176	178	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Helix	182	184	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Turn	187	191	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Beta strand	196	199	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Helix	202	209	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W	
Q86XR7	UniProtKB	Helix	212	232	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2M1W