NOD2_MOUSE
ID NOD2_MOUSE Reviewed; 1020 AA.
AC Q8K3Z0;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Nucleotide-binding oligomerization domain-containing protein 2;
DE AltName: Full=Caspase recruitment domain-containing protein 15;
GN Name=Nod2; Synonyms=Card15;
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] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Monocyte;
RX PubMed=12835899; DOI=10.1007/s00011-003-1170-z;
RA Iwanaga Y., Davey M.P., Martin T.M., Planck S.R., DePriest M.L.,
RA Baugh M.M., Suing C.M., Rosenbaum J.T.;
RT "Cloning, sequencing and expression analysis of the mouse Nod2/Card15
RT gene.";
RL Inflamm. Res. 52:272-276(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ALA-212;
RP ARG-240; CYS-422; VAL-485; ALA-603; ILE-675 AND GLN-925.
RC STRAIN=NMRI; TISSUE=Mammary cancer;
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 [3]
RP INTERACTION WITH ERBIN.
RX PubMed=16203728; DOI=10.1074/jbc.m508538200;
RA McDonald C., Chen F.F., Ollendorff V., Ogura Y., Marchetto S., Lecine P.,
RA Borg J.P., Nunez G.;
RT "A role for Erbin in the regulation of Nod2-dependent NF-kappaB
RT signaling.";
RL J. Biol. Chem. 280:40301-40309(2005).
RN [4]
RP INTERACTION WITH CARD9.
RX PubMed=17187069; DOI=10.1038/ni1426;
RA Hsu Y.M., Zhang Y., You Y., Wang D., Li H., Duramad O., Qin X.F., Dong C.,
RA Lin X.;
RT "The adaptor protein CARD9 is required for innate immune responses to
RT intracellular pathogens.";
RL Nat. Immunol. 8:198-205(2007).
RN [5]
RP FUNCTION, AND INTERACTION WITH CASP1.
RX PubMed=18511561; DOI=10.1073/pnas.0802726105;
RA Hsu L.C., Ali S.R., McGillivray S., Tseng P.H., Mariathasan S., Humke E.W.,
RA Eckmann L., Powell J.J., Nizet V., Dixit V.M., Karin M.;
RT "A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in
RT response to Bacillus anthracis infection and muramyl dipeptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7803-7808(2008).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19805227; DOI=10.1073/pnas.0907722106;
RA Petnicki-Ocwieja T., Hrncir T., Liu Y.J., Biswas A., Hudcovic T.,
RA Tlaskalova-Hogenova H., Kobayashi K.S.;
RT "Nod2 is required for the regulation of commensal microbiota in the
RT intestine.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15813-15818(2009).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=21715553; DOI=10.2337/db11-0004;
RA Schertzer J.D., Tamrakar A.K., Magalhaes J.G., Pereira S., Bilan P.J.,
RA Fullerton M.D., Liu Z., Steinberg G.R., Giacca A., Philpott D.J., Klip A.;
RT "NOD1 activators link innate immunity to insulin resistance.";
RL Diabetes 60:2206-2215(2011).
RN [8]
RP INTERACTION WITH HSP90 AND SOCS3.
RX PubMed=23019338; DOI=10.1074/jbc.m112.410027;
RA Lee K.H., Biswas A., Liu Y.J., Kobayashi K.S.;
RT "Proteasomal degradation of Nod2 protein mediates tolerance to bacterial
RT cell wall components.";
RL J. Biol. Chem. 287:39800-39811(2012).
RN [9]
RP FUNCTION.
RX PubMed=22607974; DOI=10.1016/j.molcel.2012.04.014;
RA Damgaard R.B., Nachbur U., Yabal M., Wong W.W., Fiil B.K., Kastirr M.,
RA Rieser E., Rickard J.A., Bankovacki A., Peschel C., Ruland J.,
RA Bekker-Jensen S., Mailand N., Kaufmann T., Strasser A., Walczak H.,
RA Silke J., Jost P.J., Gyrd-Hansen M.;
RT "The ubiquitin ligase XIAP recruits LUBAC for NOD2 signaling in
RT inflammation and innate immunity.";
RL Mol. Cell 46:746-758(2012).
CC -!- FUNCTION: Pattern recognition receptor (PRR) that detects bacterial
CC peptidoglycan fragments and other danger signals and plays an important
CC role in gastrointestinal immunity (PubMed:19805227, PubMed:21715553).
CC Upon stimulation by muramyl dipeptide (MDP), a fragment of bacterial
CC peptidoglycan, binds the proximal adapter receptor-interacting RIPK2,
CC which recruits ubiquitin ligases as XIAP, BIRC2, BIRC3, INAVA and the
CC LUBAC complex, triggering activation of MAP kinases and activation of
CC NF-kappa-B signaling. This in turn leads to the transcriptional
CC activation of hundreds of genes involved in immune response
CC (PubMed:22607974). Required for MDP-induced NLRP1-dependent CASP1
CC activation and IL1B release in macrophages (PubMed:18511561). Component
CC of an autophagy-mediated antibacterial pathway together with ATG16L1.
CC Also plays a role in sensing single-stranded RNA (ssRNA) from viruses.
CC Interacts with mitochondrial antiviral signaling/MAVS, leading to
CC activation of interferon regulatory factor-3/IRF3 and expression of
CC type I interferon. Besides recognizing pathogens, participates in
CC surveillance of cellular homeostasis through sensing and binding to the
CC cytosolic metabolite sphingosine-1-phosphate and then initating
CC inflammation process. {ECO:0000250|UniProtKB:Q9HC29,
CC ECO:0000269|PubMed:18511561, ECO:0000269|PubMed:19805227,
CC ECO:0000269|PubMed:22607974}.
CC -!- SUBUNIT: Component of a signaling complex consisting of ARHGEF2, NOD2
CC and RIPK2. Interacts (via CARD domain) with RIPK2 (via CARD domain).
CC Interacts with ATG16L1. Interacts (via NACHT domain) with CARD9
CC (PubMed:17187069). Interacts with ANKRD17 (via N-terminus). Interacts
CC with HSPA1A; the interaction enhances NOD2 stability. Interacts (via
CC both CARD domains) with HSP90; the interaction enhances NOD2 stability
CC (PubMed:23019338). Interacts (via CARD domain) with SOCS3; the
CC interaction promotes NOD2 degradation. Interacts (via CARD domain) with
CC ERBBI2P; the interaction inhibits activation of NOD2 (PubMed:16203728).
CC Interacts (via CARD domain) with CASP1; this interaction leads to IL1B
CC processing (PubMed:18511561). Also interacts with CASP4. Interacts with
CC NLRP1; this interaction is enhanced in the presence of muramyl
CC dipeptide (MDP) and leads to increased IL1B release. Interacts with
CC MAPKBP1; the interaction is enhanced in the presence of muramyl
CC dipeptide (MDP). Interacts with INAVA; the interaction takes place upon
CC PRR stimulation. Interacts with ANKHD1, C10ORF67, CHMP5, DOCK7, ENTR1,
CC KRT15, LDOC1, PPP1R12C, PPP2R3B, TRIM41 and VIM (By similarity).
CC Interacts with NLRP12; this interaction promotes degradation of NOD2
CC through the ubiquitin-proteasome pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q9HC29, ECO:0000269|PubMed:16203728,
CC ECO:0000269|PubMed:17187069, ECO:0000269|PubMed:18511561,
CC ECO:0000269|PubMed:23019338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9HC29}.
CC Membrane {ECO:0000250|UniProtKB:Q9HC29}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K3Z0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K3Z0-2; Sequence=VSP_007069, VSP_007070;
CC -!- DOMAIN: The ATG16L1-binding motif mediates interaction with ATG16L1.
CC {ECO:0000250}.
CC -!- DOMAIN: Intramolecular interactions between the N-terminal moiety and
CC the leucine-rich repeats (LRR) may be important for autoinhibition in
CC the absence of activating signal. In the absence of LRRs, the protein
CC becomes a constitutive activator of CASP1 cleavage and proIL1B
CC processing. {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- PTM: Polyubiquitinated following MDP stimulation, leading to
CC proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q9HC29}.
CC -!- PTM: Palmitoylated. Palmitoylation is required for proper recruitment
CC to the bacterial entry site and hence for proper signaling upon cognate
CC peptidoglycan detection. {ECO:0000250|UniProtKB:Q9Y239}.
CC -!- DISRUPTION PHENOTYPE: Deletion mice have an altered composition of the
CC gut microbiota with a net increase in the abundance of bacteroidetes
CC and firmicutes phyla in the feces and terminal ileum compared to WT
CC mice due to the fact that they are unable to kill bacteria effectively
CC (PubMed:19805227). NOD1/NOD2 double knockout mice are protected from
CC high-fat diet-induced inflammation, lipid accumulation, and peripheral
CC insulin intolerance (PubMed:21715553). {ECO:0000269|PubMed:19805227,
CC ECO:0000269|PubMed:21715553}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH44774.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF520774; AAM76073.1; -; mRNA.
DR EMBL; BC044774; AAH44774.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q8K3Z0; -.
DR SMR; Q8K3Z0; -.
DR CORUM; Q8K3Z0; -.
DR DIP; DIP-46115N; -.
DR IntAct; Q8K3Z0; 3.
DR STRING; 10090.ENSMUSP00000050538; -.
DR PhosphoSitePlus; Q8K3Z0; -.
DR PaxDb; Q8K3Z0; -.
DR PRIDE; Q8K3Z0; -.
DR ProteomicsDB; 253090; -. [Q8K3Z0-1]
DR ProteomicsDB; 253091; -. [Q8K3Z0-2]
DR Antibodypedia; 28302; 500 antibodies from 37 providers.
DR Ensembl; ENSMUST00000054324; ENSMUSP00000050538; ENSMUSG00000055994. [Q8K3Z0-2]
DR Ensembl; ENSMUST00000109634; ENSMUSP00000105262; ENSMUSG00000055994. [Q8K3Z0-1]
DR UCSC; uc009mrq.1; mouse. [Q8K3Z0-1]
DR MGI; MGI:2429397; Nod2.
DR VEuPathDB; HostDB:ENSMUSG00000055994; -.
DR eggNOG; KOG4308; Eukaryota.
DR GeneTree; ENSGT00940000160934; -.
DR InParanoid; Q8K3Z0; -.
DR PhylomeDB; Q8K3Z0; -.
DR TreeFam; TF352118; -.
DR Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-MMU-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-MMU-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
DR PRO; PR:Q8K3Z0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8K3Z0; protein.
DR Bgee; ENSMUSG00000055994; Expressed in granulocyte and 39 other tissues.
DR ExpressionAtlas; Q8K3Z0; baseline and differential.
DR GO; GO:0046658; C:anchored component of plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:HGNC-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:HGNC-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; ISS:HGNC-UCL.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050700; F:CARD domain binding; ISS:HGNC-UCL.
DR GO; GO:0019899; F:enzyme binding; ISS:HGNC-UCL.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:0032500; F:muramyl dipeptide binding; IDA:MGI.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISO:MGI.
DR GO; GO:0042834; F:peptidoglycan binding; ISS:HGNC-UCL.
DR GO; GO:0019901; F:protein kinase binding; ISS:HGNC-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0002253; P:activation of immune response; IMP:MGI.
DR GO; GO:0002815; P:biosynthetic process of antibacterial peptides active against Gram-positive bacteria; IMP:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0071224; P:cellular response to peptidoglycan; IMP:MGI.
DR GO; GO:0006952; P:defense response; TAS:HGNC-UCL.
DR GO; GO:0042742; P:defense response to bacterium; ISS:HGNC-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0016045; P:detection of bacterium; ISS:HGNC-UCL.
DR GO; GO:0009595; P:detection of biotic stimulus; TAS:HGNC-UCL.
DR GO; GO:0032498; P:detection of muramyl dipeptide; ISS:HGNC-UCL.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0006954; P:inflammatory response; TAS:HGNC-UCL.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IMP:MGI.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:MGI.
DR GO; GO:0032701; P:negative regulation of interleukin-18 production; IMP:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IMP:MGI.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IDA:BHF-UCL.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IDA:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:MGI.
DR GO; GO:0002710; P:negative regulation of T cell mediated immunity; IMP:MGI.
DR GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; IMP:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:MGI.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; ISO:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IDA:MGI.
DR GO; GO:0050871; P:positive regulation of B cell activation; ISO:MGI.
DR GO; GO:0006965; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-positive bacteria; IMP:MGI.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; ISS:UniProtKB.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISO:MGI.
DR GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; IMP:BHF-UCL.
DR GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0045089; P:positive regulation of innate immune response; IDA:BHF-UCL.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:BHF-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:MGI.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IDA:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:BHF-UCL.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IDA:BHF-UCL.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:BHF-UCL.
DR GO; GO:2000363; P:positive regulation of prostaglandin-E synthase activity; IDA:BHF-UCL.
DR GO; GO:0060585; P:positive regulation of prostaglandin-endoperoxide synthase activity; IDA:BHF-UCL.
DR GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; ISO:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
DR GO; GO:0002830; P:positive regulation of type 2 immune response; ISS:BHF-UCL.
DR GO; GO:1904417; P:positive regulation of xenophagy; IMP:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0090022; P:regulation of neutrophil chemotaxis; IMP:MGI.
DR GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0032495; P:response to muramyl dipeptide; IDA:MGI.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0032494; P:response to peptidoglycan; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:HGNC-UCL.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IDA:MGI.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IMP:MGI.
DR GO; GO:0098792; P:xenophagy; IMP:MGI.
DR Gene3D; 1.10.533.10; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR041267; NLRP_HD2.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF13516; LRR_6; 5.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR SUPFAM; SSF47986; SSF47986; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50209; CARD; 2.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Immunity;
KW Innate immunity; Leucine-rich repeat; Lipoprotein; Membrane;
KW Nucleotide-binding; Palmitate; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1020
FT /note="Nucleotide-binding oligomerization domain-containing
FT protein 2"
FT /id="PRO_0000144091"
FT DOMAIN 6..104
FT /note="CARD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT DOMAIN 106..200
FT /note="CARD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT DOMAIN 273..600
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT REPEAT 685..709
FT /note="LRR 1"
FT REPEAT 726..749
FT /note="LRR 2"
FT REPEAT 766..792
FT /note="LRR 3"
FT REPEAT 794..817
FT /note="LRR 4"
FT REPEAT 822..845
FT /note="LRR 5"
FT REPEAT 850..873
FT /note="LRR 6"
FT REPEAT 906..929
FT /note="LRR 7"
FT REPEAT 934..962
FT /note="LRR 8"
FT REPEAT 963..985
FT /note="LRR 9"
FT REPEAT 1005..1019
FT /note="LRR 10"
FT REGION 221..254
FT /note="Required for CARD9 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HC29"
FT MOTIF 43..57
FT /note="ATG16L1-binding motif"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007069"
FT VAR_SEQ 195
FT /note="E -> EGYSLCRSRCDRGFTLICLFCIL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007070"
FT VARIANT 212
FT /note="T -> A (in strain: NMRI)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 240
FT /note="Q -> R (in strain: NMRI)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 422
FT /note="L -> C (in strain: NMRI; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 485
FT /note="G -> V (in strain: NMRI)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 603
FT /note="V -> A (in strain: NMRI)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 675
FT /note="V -> I (in strain: NMRI)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 925
FT /note="E -> Q (in strain: NMRI)"
FT /evidence="ECO:0000269|PubMed:15489334"
SQ SEQUENCE 1020 AA; 113562 MW; 25504905ECF70FBB CRC64;
MRSSCCDMCS QEEFQAQRSQ LVALLISGSL EGFESILDWL LSWDVLSRED YEGLSLPGQP
LSHSARRLLD TVWNKGVWGC QKLLEAVQEA QANSHTFELY GSWDTHSLHP TRDLQSHRPA
IVRRLYNHVE AMLELAREGG FLSQYECEEI RLPIFTSSQR ARRLLDLAAV KANGLAAFLL
QHVRELPAPL PLPYEAAECQ KFISKLRTMV LTQSRFLSTY DGSENLCLED IYTENILELQ
TEVGTAGALQ KSPAILGLED LFDTHGHLNR DADTILVVGE AGSGKSTLLQ RLHLLWATGR
SFQEFLFIFP FSCRQLQCVA KPLSLRTLLF EHCCWPDVAQ DDVFQFLLDH PDRVLLTFDG
LDEFKFRFTD RERHCSPIDP TSVQTLLFNL LQGNLLKNAC KVLTSRPDAV SALLRKFVRT
ELQLKGFSEE GIQLYLRKHH REPGVADRLI QLIQATSALH GLCHLPVFSW MVSRCHRELL
LQNRGFPTTS TDMYLLILQH FLLHASPPDS SPLGLGPGLL QSRLSTLLHL GHLALRGLAM
SCYVFSAQQL QAAQVDSDDI SLGFLVRAQS SVPGSKAPLE FLHITFQCFF AAFYLAVSAD
TSVASLKHLF SCGRLGSSLL GRLLPNLCIQ GSRVKKGSEA ALLQKAEPHN LQITAAFLAG
LLSQQHRDLL AACQVSERVL LQRQARARSC LAHSLREHFH SIPPAVPGET KSMHAMPGFI
WLIRSLYEMQ EEQLAQEAVR RLDIGHLKLT FCRVGPAECA ALAFVLQHLQ RPVALQLDYN
SVGDVGVEQL RPCLGVCTAL YLRDNNISDR GARTLVECAL RCEQLQKLAL FNNKLTDACA
CSMAKLLAHK QNFLSLRVGN NHITAAGAEV LAQGLKSNTS LKFLGFWGNS VGDKGTQALA
EVVADHQNLK WLSLVGNNIG SMGAEALALM LEKNKSLEEL CLEENHICDE GVYSLAEGLK
RNSTLKFLKL SNNGITYRGA EALLQALSRN SAILEVWLRG NTFSLEEIQT LSSRDARLLL
