##gff-version 3
Q8K3Z0	UniProtKB	Chain	1	1020	.	.	.	ID=PRO_0000144091;Note=Nucleotide-binding oligomerization domain-containing protein 2	
Q8K3Z0	UniProtKB	Domain	6	104	.	.	.	Note=CARD 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00046	
Q8K3Z0	UniProtKB	Domain	106	200	.	.	.	Note=CARD 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00046	
Q8K3Z0	UniProtKB	Domain	273	600	.	.	.	Note=NACHT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00136	
Q8K3Z0	UniProtKB	Repeat	685	709	.	.	.	Note=LRR 1	
Q8K3Z0	UniProtKB	Repeat	726	749	.	.	.	Note=LRR 2	
Q8K3Z0	UniProtKB	Repeat	766	792	.	.	.	Note=LRR 3	
Q8K3Z0	UniProtKB	Repeat	794	817	.	.	.	Note=LRR 4	
Q8K3Z0	UniProtKB	Repeat	822	845	.	.	.	Note=LRR 5	
Q8K3Z0	UniProtKB	Repeat	850	873	.	.	.	Note=LRR 6	
Q8K3Z0	UniProtKB	Repeat	906	929	.	.	.	Note=LRR 7	
Q8K3Z0	UniProtKB	Repeat	934	962	.	.	.	Note=LRR 8	
Q8K3Z0	UniProtKB	Repeat	963	985	.	.	.	Note=LRR 9	
Q8K3Z0	UniProtKB	Repeat	1005	1019	.	.	.	Note=LRR 10	
Q8K3Z0	UniProtKB	Region	221	254	.	.	.	Note=Required for CARD9 binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HC29	
Q8K3Z0	UniProtKB	Motif	43	57	.	.	.	Note=ATG16L1-binding motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HC29	
Q8K3Z0	UniProtKB	Binding site	219	219	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G1T469	
Q8K3Z0	UniProtKB	Binding site	232	232	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G1T469	
Q8K3Z0	UniProtKB	Binding site	233	233	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G1T469	
Q8K3Z0	UniProtKB	Binding site	282	282	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G1T469	
Q8K3Z0	UniProtKB	Binding site	283	283	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G1T469	
Q8K3Z0	UniProtKB	Binding site	284	284	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G1T469	
Q8K3Z0	UniProtKB	Binding site	285	285	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G1T469	
Q8K3Z0	UniProtKB	Binding site	286	286	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G1T469	
Q8K3Z0	UniProtKB	Binding site	287	287	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G1T469	
Q8K3Z0	UniProtKB	Binding site	583	583	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:G1T469	
Q8K3Z0	UniProtKB	Lipidation	375	375	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HC29	
Q8K3Z0	UniProtKB	Alternative sequence	1	7	.	.	.	ID=VSP_007069;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
Q8K3Z0	UniProtKB	Alternative sequence	195	195	.	.	.	ID=VSP_007070;Note=In isoform 2. E->EGYSLCRSRCDRGFTLICLFCIL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
Q8K3Z0	UniProtKB	Natural variant	212	212	.	.	.	Note=In strain: NMRI. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=PMID:15489334	
Q8K3Z0	UniProtKB	Natural variant	240	240	.	.	.	Note=In strain: NMRI. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=PMID:15489334	
Q8K3Z0	UniProtKB	Natural variant	422	422	.	.	.	Note=In strain: NMRI%3B requires 2 nucleotide substitutions. L->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=PMID:15489334	
Q8K3Z0	UniProtKB	Natural variant	485	485	.	.	.	Note=In strain: NMRI. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=PMID:15489334	
Q8K3Z0	UniProtKB	Natural variant	603	603	.	.	.	Note=In strain: NMRI. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=PMID:15489334	
Q8K3Z0	UniProtKB	Natural variant	675	675	.	.	.	Note=In strain: NMRI. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=PMID:15489334	
Q8K3Z0	UniProtKB	Natural variant	925	925	.	.	.	Note=In strain: NMRI. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=PMID:15489334	
Q8K3Z0	UniProtKB	Mutagenesis	314	314	.	.	.	Note=Mutation that mimics a human variant associated with Blau syndrome (BLAUS)%3B knockin mice show impaired response to muramyl dipeptide. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25429073;Dbxref=PMID:25429073	
Q8K3Z0	UniProtKB	Mutagenesis	987	1020	.	.	.	Note=Mutation that mimics human L1007fsinsC variant%3B knockin mice show elevated NF-kappa-B activation in response to muramyl dipeptide and more efficient processing and secretion of the cytokine IL1B. LSRNSAILEVWLRGNTFSLEEIQTLSSRDARLLL->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15692052;Dbxref=PMID:15692052