true2002-01-312024-03-27218NOD1_HUMANHuman CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-kappaB.Bertin J.Nir W.-J.Fischer C.M.Tayber O.V.Errada P.R.Grant J.R.Keilty J.J.Gosselin M.L.Robison K.E.Wong G.H.W.Glucksmann M.A.DiStefano P.S.doi:10.1074/jbc.274.19.129551999J. Biol. Chem.27412955-12958NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)TISSUE SPECIFICITYEndothelial cellNod1, an Apaf-1-like activator of caspase-9 and nuclear factor-kappaB.Inohara N.Koseki T.del Peso L.Hu Y.Yee C.Chen S.Carrio R.Merino J.Liu D.Ni J.Nunez G.doi:10.1074/jbc.274.21.145601999J. Biol. Chem.27414560-14567NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1)MUTAGENESIS OF VAL-41 AND LYS-208Mammary glandComplete sequencing and characterization of 21,243 full-length human cDNAs.Ota T.Suzuki Y.Nishikawa T.Otsuki T.Sugiyama T.Irie R.Wakamatsu A.Hayashi K.Sato H.Nagai K.Kimura K.Makita H.Sekine M.Obayashi M.Nishi T.Shibahara T.Tanaka T.Ishii S.Yamamoto J.Saito K.Kawai Y.Isono Y.Nakamura Y.Nagahari K.Murakami K.Yasuda T.Iwayanagi T.Wagatsuma M.Shiratori A.Sudo H.Hosoiri T.Kaku Y.Kodaira H.Kondo H.Sugawara M.Takahashi M.Kanda K.Yokoi T.Furuya T.Kikkawa E.Omura Y.Abe K.Kamihara K.Katsuta N.Sato K.Tanikawa M.Yamazaki M.Ninomiya K.Ishibashi T.Yamashita H.Murakawa K.Fujimori K.Tanai H.Kimata M.Watanabe M.Hiraoka S.Chiba Y.Ishida S.Ono Y.Takiguchi S.Watanabe S.Yosida M.Hotuta T.Kusano J.Kanehori K.Takahashi-Fujii A.Hara H.Tanase T.-O.Nomura Y.Togiya S.Komai F.Hara R.Takeuchi K.Arita M.Imose N.Musashino K.Yuuki H.Oshima A.Sasaki N.Aotsuka S.Yoshikawa Y.Matsunawa H.Ichihara T.Shiohata N.Sano S.Moriya S.Momiyama H.Satoh N.Takami S.Terashima Y.Suzuki O.Nakagawa S.Senoh A.Mizoguchi H.Goto Y.Shimizu F.Wakebe H.Hishigaki H.Watanabe T.Sugiyama A.Takemoto M.Kawakami B.Yamazaki M.'Watanabe K.Kumagai A.Itakura S.Fukuzumi Y.Fujimori Y.Komiyama M.Tashiro H.Tanigami A.Fujiwara T.Ono T.Yamada K.Fujii Y.Ozaki K.Hirao M.Ohmori Y.Kawabata A.Hikiji T.Kobatake N.Inagaki H.Ikema Y.Okamoto S.Okitani R.Kawakami T.Noguchi S.Itoh T.Shigeta K.Senba T.Matsumura K.Nakajima Y.Mizuno T.Morinaga M.Sasaki M.Togashi T.Oyama M.Hata H.Watanabe M.'Komatsu T.Mizushima-Sugano J.Satoh T.Shirai Y.Takahashi Y.Nakagawa K.Okumura K.Nagase T.Nomura N.Kikuchi H.Masuho Y.Yamashita R.Nakai K.Yada T.Nakamura Y.'Ohara O.Isogai T.Sugano S.doi:10.1038/ng12852004Nat. Genet.3640-45NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)PlacentaThe DNA sequence of human chromosome 7.Hillier L.W.Fulton R.S.Fulton L.A.Graves T.A.Pepin K.H.Wagner-McPherson C.Layman D.Maas J.Jaeger S.Walker R.Wylie K.Sekhon M.Becker M.C.O'Laughlin M.D.Schaller M.E.Fewell G.A.Delehaunty K.D.Miner T.L.Nash W.E.Cordes M.Du H.Sun H.Edwards J.Bradshaw-Cordum H.Ali J.Andrews S.Isak A.Vanbrunt A.Nguyen C.Du F.Lamar B.Courtney L.Kalicki J.Ozersky P.Bielicki L.Scott K.Holmes A.Harkins R.Harris A.Strong C.M.Hou S.Tomlinson C.Dauphin-Kohlberg S.Kozlowicz-Reilly A.Leonard S.Rohlfing T.Rock S.M.Tin-Wollam A.-M.Abbott A.Minx P.Maupin R.Strowmatt C.Latreille P.Miller N.Johnson D.Murray J.Woessner J.P.Wendl M.C.Yang S.-P.Schultz B.R.Wallis J.W.Spieth J.Bieri T.A.Nelson J.O.Berkowicz N.Wohldmann P.E.Cook L.L.Hickenbotham M.T.Eldred J.Williams D.Bedell J.A.Mardis E.R.Clifton S.W.Chissoe S.L.Marra M.A.Raymond C.Haugen E.Gillett W.Zhou Y.James R.Phelps K.Iadanoto S.Bubb K.Simms E.Levy R.Clendenning J.Kaul R.Kent W.J.Furey T.S.Baertsch R.A.Brent M.R.Keibler E.Flicek P.Bork P.Suyama M.Bailey J.A.Portnoy M.E.Torrents D.Chinwalla A.T.Gish W.R.Eddy S.R.McPherson J.D.Olson M.V.Eichler E.E.Green E.D.Waterston R.H.Wilson R.K.doi:10.1038/nature017822003Nature424157-164NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)VARIANT HIS-447LymphAn induced proximity model for NF-kappa B activation in the Nod1/RICK and RIP signaling pathways.Inohara N.Koseki T.Lin J.del Peso L.Lucas P.C.Chen F.F.Ogura Y.Nunez G.doi:10.1074/jbc.m0034152002000J. Biol. Chem.27527823-27831FUNCTIONSUBUNITINTERACTION WITH RIPK2Human Nod1 confers responsiveness to bacterial lipopolysaccharides.Inohara N.Ogura Y.Chen F.F.Muto A.Nunez G.doi:10.1074/jbc.m0097282002001J. Biol. Chem.2762551-2554FUNCTIONPeptidoglycan molecular requirements allowing detection by Nod1 and Nod2.Girardin S.E.Travassos L.H.Herve M.Blanot D.Boneca I.G.Philpott D.J.Sansonetti P.J.Mengin-Lecreulx D.doi:10.1074/jbc.m3071982002003J. Biol. Chem.27841702-41708FUNCTIONAn essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid.Chamaillard M.Hashimoto M.Horie Y.Masumoto J.Qiu S.Saab L.Ogura Y.Kawasaki A.Fukase K.Kusumoto S.Valvano M.A.Foster S.J.Mak T.W.Nunez G.Inohara N.doi:10.1038/ni9452003Nat. Immunol.4702-707FUNCTIONNod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan.Girardin S.E.Boneca I.G.Carneiro L.A.Antignac A.Jehanno M.Viala J.Tedin K.Taha M.K.Labigne A.Zaehringer U.Coyle A.J.DiStefano P.S.Bertin J.Sansonetti P.J.Philpott D.J.doi:10.1126/science.10846772003Science3001584-1587FUNCTIONRegulatory regions and critical residues of NOD2 involved in muramyl dipeptide recognition.Tanabe T.Chamaillard M.Ogura Y.Zhu L.Qiu S.Masumoto J.Ghosh P.Moran A.Predergast M.M.Tromp G.Williams C.J.Inohara N.Nunez G.doi:10.1038/sj.emboj.76001752004EMBO J.231587-1597FUNCTIONMUTAGENESIS OF LYS-208 AND ASP-284Murine Nod1 but not its human orthologue mediates innate immune detection of tracheal cytotoxin.Magalhaes J.G.Philpott D.J.Nahori M.A.Jehanno M.Fritz J.Le Bourhis L.Viala J.Hugot J.P.Giovannini M.Bertin J.Lepoivre M.Mengin-Lecreulx D.Sansonetti P.J.Girardin S.E.doi:10.1038/sj.embor.74005522005EMBO Rep.61201-1207FUNCTIONIdentification of the critical residues involved in peptidoglycan detection by Nod1.Girardin S.E.Jehanno M.Mengin-Lecreulx D.Sansonetti P.J.Alzari P.M.Philpott D.J.doi:10.1074/jbc.m5095372002005J. Biol. Chem.28038648-38656FUNCTIONFUNCTION (ISOFORM 3)DOMAINMUTAGENESIS OF HIS-788; LYS-790; GLY-792; GLU-816; GLY-818; TRP-820 AND TRP-874The pattern-recognition molecule Nod1 is localized at the plasma membrane at sites of bacterial interaction.Kufer T.A.Kremmer E.Adam A.C.Philpott D.J.Sansonetti P.J.doi:10.1111/j.1462-5822.2007.01062.x2008Cell. Microbiol.10477-486SUBCELLULAR LOCATIONMUTAGENESIS OF LYS-208; ASP-711; HIS-788; GLY-792 AND GLN-877GEF-H1 mediated control of NOD1 dependent NF-kappaB activation by Shigella effectors.Fukazawa A.Alonso C.Kurachi K.Gupta S.Lesser C.F.McCormick B.A.Reinecker H.C.doi:10.1371/journal.ppat.10002282008PLoS Pathog.4E1000228FUNCTIONSUBCELLULAR LOCATIONINTERACTION WITH ARHGEF2NLRP10 enhances Shigella-induced pro-inflammatory responses.Lautz K.Damm A.Menning M.Wenger J.Adam A.C.Zigrino P.Kremmer E.Kufer T.A.doi:10.1111/j.1462-5822.2012.01822.x2012Cell. Microbiol.141568-1583FUNCTIONINTERACTION WITH NLRP10MUTAGENESIS OF LYS-208 AND ASP-287Ubiquitin regulates caspase recruitment domain-mediated signaling by nucleotide-binding oligomerization domain-containing proteins NOD1 and NOD2.Ver Heul A.M.Fowler C.A.Ramaswamy S.Piper R.C.doi:10.1074/jbc.m112.4137812013J. Biol. Chem.2886890-6902UBIQUITIN-BINDINGINTERACTION WITH RIPK2MUTAGENESIS OF ARG-69 AND 84-GLU--TYR-88The E3 ligase RNF34 is a novel negative regulator of the NOD1 pathway.Zhang R.Zhao J.Song Y.Wang X.Wang L.Xu J.Song C.Liu F.doi:10.1159/0003629722014Cell. Physiol. Biochem.331954-1962UBIQUITINATION BY RNF34NOD1 Participates in the Innate Immune Response Triggered by Hepatitis C Virus Polymerase.Vegna S.Gregoire D.Moreau M.Lassus P.Durantel D.Assenat E.Hibner U.Simonin Y.doi:10.1128/jvi.03230-152016J. Virol.906022-6035FUNCTIONNOD1 and NOD2 signalling links ER stress with inflammation.Keestra-Gounder A.M.Byndloss M.X.Seyffert N.Young B.M.Chavez-Arroyo A.Tsai A.Y.Cevallos S.A.Winter M.G.Pham O.H.Tiffany C.R.de Jong M.F.Kerrinnes T.Ravindran R.Luciw P.A.McSorley S.J.Baeumler A.J.Tsolis R.M.doi:10.1038/nature176312016Nature532394-397FUNCTIONStructural basis of RIP2 activation and signaling.Gong Q.Long Z.Zhong F.L.Teo D.E.T.Jin Y.Yin Z.Boo Z.Z.Zhang Y.Zhang J.Yang R.Bhushan S.Reversade B.Li Z.Wu B.doi:10.1038/s41467-018-07447-92018Nat. Commun.94993INTERACTION WITH RIPK2Palmitoylation of NOD1 and NOD2 is required for bacterial sensing.Lu Y.Zheng Y.Coyaud E.Zhang C.Selvabaskaran A.Yu Y.Xu Z.Weng X.Chen J.S.Meng Y.Warner N.Cheng X.Liu Y.Yao B.Hu H.Xia Z.Muise A.M.Klip A.Brumell J.H.Girardin S.E.Ying S.Fairn G.D.Raught B.Sun Q.Neculai D.doi:10.1126/science.aau63912019Science366460-467PALMITOYLATION AT CYS-558; CYS-567 AND CYS-952SUBCELLULAR LOCATIONMUTAGENESIS OF CYS-558; CYS-567 AND CYS-952NOD1 Promotes Antiviral Signaling by Binding Viral RNA and Regulating the Interaction of MDA5 and MAVS.Wu X.M.Zhang J.Li P.W.Hu Y.W.Cao L.Ouyang S.Bi Y.H.Nie P.Chang M.X.doi:10.4049/jimmunol.19006672020J. Immunol.2042216-2231FUNCTIONINTERACTION WITH IFIH1SUBCELLULAR LOCATIONCellular stress promotes NOD1/2-dependent inflammation via the endogenous metabolite sphingosine-1-phosphate.Pei G.Zyla J.He L.Moura-Alves P.Steinle H.Saikali P.Lozza L.Nieuwenhuizen N.Weiner J.Mollenkopf H.J.Ellwanger K.Arnold C.Duan M.Dagil Y.Pashenkov M.Boneca I.G.Kufer T.A.Dorhoi A.Kaufmann S.H.doi:10.15252/embj.20201062722021EMBO J.40e106272FUNCTIONMUTAGENESIS OF HIS-517Selective autophagy of RIPosomes maintains innate immune homeostasis during bacterial infection.Mehto S.Jena K.K.Yadav R.Priyadarsini S.Samal P.Krishna S.Dhar K.Jain A.Chauhan N.R.Murmu K.C.Bal R.Sahu R.Jaiswal P.Sahoo B.S.Patnaik S.Kufer T.A.Rusten T.E.Chauhan S.Prasad P.Chauhan S.'doi:10.15252/embj.20221112892022EMBO J.41e111289INTERACTION WITH IRGMPROTEIN DEGRADATIONSolution structure of the CARD domain in human caspase recruitment domain protein 4 (NOD1 protein).RIKEN structural genomics initiative (RSGI)2006-12PDBSTRUCTURE BY NMR OF 14-110Crystal structure of the Nod1 caspase activation and recruitment domain.Coussens N.P.Mowers J.C.McDonald C.Nunez G.Ramaswamy S.doi:10.1016/j.bbrc.2006.11.1222007Biochem. Biophys. Res. Commun.3531-5X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-108SUBUNITSolution structure of NOD1 CARD and mutational analysis of its interaction with the CARD of downstream kinase RICK.Manon F.Favier A.Nunez G.Simorre J.P.Cusack S.doi:10.1016/j.jmb.2006.09.0672007J. Mol. Biol.365160-174STRUCTURE BY NMR OF 15-138FUNCTIONINTERACTION WITH RIPK2MUTAGENESIS OF VAL-41; LEU-44; ASP-48; GLU-53; ASP-54; GLU-56 AND ARG-69Monomer/dimer transition of the caspase-recruitment domain of human Nod1.Srimathi T.Robbins S.L.Dubas R.L.Hasegawa M.Inohara N.Park Y.C.doi:10.1021/bi70166022008Biochemistry471319-1325X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 9-106SUBUNITCrystal structure of a complex of NOD1 CARD and ubiquitin.Ver Heul A.M.Gakhar L.Piper R.C.Subramanian R.doi:10.1371/journal.pone.01040172014PLoS ONE9e104017X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 16-108 IN COMPLEX WITH UBIQUITINSUBUNITA=15-138A=17-1102.00A=16-1081.90A/B=9-1062.15A/B/C/D/E/F=2-1382.90A=16-10831351 site, 1 O-linked glycan (1 site)441 antibodies from 37 providershumanNOD1Low tissue specificitygeneEukaryotaNOD1/2 Signaling PathwayTAK1-dependent IKK and NF-kappa-B activationactivated TAK1 mediates p38 MAPK activationJNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1Ovarian tumor domain proteasesInterleukin-1 signalingSARS-CoV-2 activates/modulates innate and adaptive immune responses10 hits in 1153 CRISPR screenshumanTchemProteinExpressed in sural nerve and 150 other cell types or tissuesbaseline and differentialCARD_NOD1_CARD4Death Domain, FasP-loop containing nucleotide triphosphate hydrolasesRibonuclease InhibitorCARDDEATH-like_dom_sfLeu-rich_rptLRR_dom_sfNACHT_NTPaseNLRP_HD2NOD2_WHP-loop_NTPaseNACHT, LRR AND CARD DOMAINS-CONTAININGRNI-LIKE SUPERFAMILY PROTEINCARDLRR_6NACHTNLRC4_HD2NOD2_WHLRR_RIDEATH domainRNI-likeCARDNACHTHSNucleotide-binding oligomerization domain-containing protein 1hNod1Caspase recruitment domain-containing protein 4NOD1CARD4Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and thus participates in both innate and adaptive immune responses (PubMed:11058605, PubMed:12796777, PubMed:12791997, PubMed:15044951, PubMed:16172124, PubMed:19043560, PubMed:22672233, PubMed:27099311). Specifically recognizes and binds gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP), a dipeptide present in peptidoglycan of Gram-negative bacteria (PubMed:12871942, PubMed:12796777, PubMed:12791997, PubMed:16211083, PubMed:16172124). Preferentially binds iE-DAP in tripeptide-containing muropeptides (MurNAc-TriDAP or TriDAP) (PubMed:16211083). Ligand binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2 (PubMed:12796777, PubMed:12791997, PubMed:17054981). Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (PubMed:10880512, PubMed:12791997, PubMed:19043560). This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (PubMed:10880512, PubMed:19043560). Also acts as a regulator of antiviral response elicited by dsRNA and the expression of RLR pathway members by targeting IFIH1 and TRAF3 to modulate the formation of IFIH1-MAVS and TRAF3-MAVS complexes leading to increased transcription of type I IFNs (PubMed:32169843). Also acts as a regulator of autophagy via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry (By similarity). Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling (PubMed:27007849, PubMed:33942347). In addition, plays a role in insulin trafficking in beta cells in a cell-autonomous manner (By similarity). Mechanistically, upon recognizing cognate ligands, NOD1 and RIPK2 localize to insulin vesicles where they recruit RAB1A to direct insulin trafficking through the cytoplasm (By similarity).In contrast to isoform 1, does not efficiently recognize and bind gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP) ligand.Homooligomer: homooligomerizes following ligand-binding, promoting RIPK2 recruitment (PubMed:10880512). Interacts (via CARD domain) with RIPK2 (via CARD domain) (PubMed:10880512, PubMed:30478312, PubMed:23300079, PubMed:17054981). Following RIPK2 recruitment, RIPK2 homooligomerizes via its CARD domain and forms long filaments named RIPosomes (PubMed:30478312). Interacts with ARHGEF2 (PubMed:19043560). Interacts (via CARD domain) with ubiquitin; inhibiting interaction with RIPK2 (PubMed:23300079, PubMed:25127239). Interacts with NLRP10 and recruits it to the cell membrane following invasive bacterial infection (PubMed:22672233). Interacts with IFIH1; this interaction promotes transcription of antiviral genes and inhibition of viral replication (PubMed:32169843). Interacts with IRGM; promoting NOD1 degradation (PubMed:36221902). Interacts with ATG16L1 (By similarity).Detected in the cytoplasm and at the cell membrane (PubMed:31649195). Following bacterial infection, localizes to bacterial entry sites in the cell membrane (PubMed:31649195). Recruited to the basolateral and apical membranes in polarized epithelial cells (PubMed:19043560).Highly expressed in adult heart, skeletal muscle, pancreas, spleen and ovary (PubMed:10224040). Also detected in placenta, lung, liver, kidney, thymus, testis, small intestine and colon (PubMed:10224040).The LRR repeats recognize and bind gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).Palmitoylated. Palmitoylation is required for proper recruitment to the bacterial entry site and hence for proper signaling upon cognate peptidoglycan detection.Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF34 promotes proteasomal degradation and thereby negatively regulates NOD1 for instance in NF-kappa-B activation.Degraded via selective autophagy following interaction with IRGM (PubMed:36221902). IRGM promotes NOD1-RIPK2 RIPosome recruitment to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation (PubMed:36221902).Belongs to the NOD1-NOD2 family.Human and mouse NOD1 bind gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP) in a different context (PubMed:16211083). do not detect the same muropeptide from bacterial peptidoglycan: while human NOD1 detects a tripeptide-containing muropeptide (MurNAc-TriDAP or TriDAP), mouse Nod1 needs a tetrapeptide structure for efficient sensing (MurNAc-tetraDAP or TetraDAP) (PubMed:16211083).Nucleotide-binding oligomerization domain-containing protein 11076911953CARD15105NACHT196531LRR 1632656LRR 2702725LRR 3727750LRR 4755778LRR 5783806LRR 6839862LRR 7867891LRR 8895918LRR 9923946202209S-palmitoyl cysteine558S-palmitoyl cysteine567S-palmitoyl cysteine952In isoform 2.AASRKVTGCVCRTCSSSTTATQSGTPRRCLPSCCASPTWPSSPSMAWTSCTRTWT195249In isoform 2.250In isoform 3.819846K266N372H447W605T610Abolishes interaction with RIPK2/RICK.A41Abolishes caspase-9 activation.QAbolishes activation of NF-kappa-B. No effect on interaction with RIPK2.A44Abolishes activation of NF-kappa-B. No effect on interaction with RIPK2.K48No effect on activation of NF-kappa-B. Abolishes interaction with RIPK2.K53Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2.K54Abolishes activation of NF-kappa-B. Abolishes interaction with RIPK2.K56Abolishes activation of NF-kappa-B. Abolished interaction with ubiquitin and RIPK2.E69Abolished interaction with ubiquitin without affecting interaction with RIPK2.AFFLR8488Reduces caspase-9 activation. Reduced binding affinity for NLRP10. Does not associate with cell membrane. Reduced NF-kappa-B activation in response to ligand binding.R208Reduced NF-kappa-B activation in response to ligand binding.A284Reduced binding affinity for NLRP10.A287Loss of activation by sphingosine-1-phosphate.A517Strongly reduced palmitoylation and localization to the cell membrane; when associated with S-567 and S-952.SStrongly reduced palmitoylation and localization to the cell membrane; when associated with S-558 and S-952.SDoes not associate with cell membrane.S711No effect on association with cell membrane. Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).S788Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).T790Does not associate with cell membrane. Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).S792Increased binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP) in tetrapeptide-containing muropeptides (MurNAc-TetraDAP or TetraDAP).D816Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).SReduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).S818Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).S820Reduced binding to gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP).S874Does not associate with cell membrane.S877Strongly reduced palmitoylation and localization to the cell membrane; when associated with S-558 and S-567.S182527333846525961636478809598100101false3false3false3false9false3false3false2false2false3false3false5true4NOD1CRYAAGFAPGLE1HTTKLK6LMNAOLFM4PAK1SPRED1SUGT1sspH21999-11-011107691a4bd7261a6578bb7ad9869c952b816b11AlphaMEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAYARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRGYLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAKVYEDEKRIICF2MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQAASRKVTGCVCRTCSSSTTATQSGTPRRCLPSCCASPTWPSSPSMAWTSCTRTWT3Betadelta10MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAYARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRGYLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAKVYEDEKRIICFtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue