Nod1
entrez
107607
canonical
uniprot
Q8BHB0
canonical
ensembl
ENSMUSG00000038058
resolver
ensp
ENSMUSP00000055747
resolver
ensp
ENSMUSP00000130487
resolver
ensp
ENSMUSP00000321161
resolver
enst
ENSMUST00000060655
resolver
enst
ENSMUST00000168172
resolver
genesymbol
Nod1
resolver
genesymbol_syn
Card4
resolver
uniprot
Q540J8
resolver
uniprot
Q8BUT6
resolver
uniprot_entry
NOD1_MOUSE
resolver
uniprot_entry
Q540J8_MOUSE
resolver
uniprot_sec
Q8BUT6
resolver
amino_acid_sequence
MEEHGHHEMEGTPLGCHSHIKLLKINREHLVTNIRNTQCLVDNLLENGYFSAEDAEIVCACPTKPDKVRKILDLVQSKGEEVSEFFLYVLQQLEDAYVDLRLWLSEIGFSPSQLIRTKTIVNTDPVSRYTQQLRHQLGRDSKFMLCYAQKEDLLLEETYMDTLMELVGFNNENLGSLGGLDCLLDHSTGVLNEHGETVFVFGDAGVGKSMLLQRLQSLWASGRLTSTAKFFFHFRCRMFSCFKESDMLSLQDLLFKHFCYPEQDPEEVFSFLLRFPHTALFTFDGLDELHSDFDLSRVPDSCCPWEPAHPLVLLANLLSGRLLKGAGKLLTARTGVEVPRQLLRKKVLLRGFSPSHLRAYARRMFPERTAQEHLLQQLDANPNLCSLCGVPLFCWIIFRCFQHFQTVFEGSSSQLPDCAVTLTDVFLLVTEVHLNRPQPSSLVQRNTRSPAETLRAGWRTLHALGEVAHRGTDKSLFVFGQEEVQASKLQEGDLQLGFLRALPDVGPEQGQSYEFFHLTLQAFFTAFFLVADDKVSTRELLRFFREWTSPGEATSSSCHSSFFSFQCLGGRSRLGPDPFRNKDHFQFTNLFLCGLLAKARQKLLRQLVPKAILRRKRKALWAHLFASLRSYLKSLPRVQSGGFNQVHAMPTFLWMLRCIYETQSQKVGRLAARGISADYLKLAFCNACSADCSALSFVLHHFHRQLALDLDNNNLNDYGVQELQPCFSRLTVIRLSVNQITDTGVKVLCEELTKYKIVTFLGLYNNQITDIGARYVAQILDECRGLKHLKLGKNRITSEGGKCVALAVKNSTSIVDVGMWGNQIGDEGAKAFAEALKDHPSLTTLSLAFNGISPEGGKSLAQALKQNTTLTVIWLTKNELNDESAECFAEMLRVNQTLRHLWLIQNRITAKGTAQLARALQKNTAITEICLNGNLIKPEEAKVFENEKRIICF
uniprot
proteins
function
FUNCTION: Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and thus participates in both innate and adaptive immune responses (PubMed:12796777, PubMed:21715553). Specifically recognizes and binds gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP), a dipeptide present in peptidoglycan of Gram-negative bacteria (PubMed:12796777, PubMed:16211083). Preferentially binds iE-DAP in tetrapeptide-containing muropeptides (MurNAc-TetraDAP or TetraDAP) (PubMed:16211083). Ligand binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2 (By similarity). 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 (By similarity). This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (By similarity). 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 (By similarity). Also acts as a regulator of autophagy via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry (PubMed:19898471). 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). In addition, plays a role in insulin trafficking in beta cells in a cell-autonomous manner (PubMed:21715553, PubMed:31201384). Mechanistically, upon recognizing cognate ligands, NOD1 and RIPK2 localize to insulin vesicles where they recruit RAB1A to direct insulin trafficking through the cytoplasm (PubMed:31201384). {ECO:0000250|UniProtKB:Q9Y239, ECO:0000269|PubMed:12796777, ECO:0000269|PubMed:16211083, ECO:0000269|PubMed:19898471, ECO:0000269|PubMed:21715553, ECO:0000269|PubMed:27007849, ECO:0000269|PubMed:31201384}.
uniprot
proteins
mass_dalton
107740
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF34 promotes proteasomal degradation and thereby negatively regulates NOD1 for instance in NF-kappa-B activation. {ECO:0000250|UniProtKB:Q9Y239}.; PTM: Palmitoylated. Palmitoylation is required for proper recruitment to the bacterial entry site and hence for proper signaling upon cognate peptidoglycan detection. {ECO:0000250|UniProtKB:Q9Y239}.; PTM: Degraded via selective autophagy following interaction with Irgm1. Irgm1 promotes NOD1-RIPK2 RIPosome recruitment to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation. {ECO:0000250|UniProtKB:Q9Y239}.
uniprot
proteins
protein_family
NOD1-NOD2 family
uniprot
proteins
pubmed
12796777
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16211083
uniprot
proteins
pubmed
19898471
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21715553
uniprot
proteins
pubmed
27007849
uniprot
proteins
pubmed
31201384
uniprot
proteins
sequence_length
953
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y239}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Y239}. Apical cell membrane {ECO:0000250|UniProtKB:Q9Y239}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9Y239}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y239}. Note=Detected in the cytoplasm and at the cell membrane. Following bacterial infection, localizes to bacterial entry sites in the cell membrane. Recruited to the basolateral and apical membranes in polarized epithelial cells. {ECO:0000250|UniProtKB:Q9Y239}.
uniprot
proteins