Descriptions

NOD2, a NOD-like receptor (NLR), is an intracellular sensor of bacterial muramyl dipeptide (MDP) that promotes secretion of the proinflammatory cytokine IL-1β. NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger IL-1β processing and secretion in MDP-stimulated macrophages, wherease the C-terminal leucine-rich repeats (LRR) of NOD2 prevent caspase-1 activation in non-stimulated cells. Removal of the LRR rendered NOD2 a constitutive activator of pro-IL-1β processing and caspase-1.

Autoinhibitory domains (AIDs)

Target domain

26-218 (CARD domains)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q53B88

Entry ID Method Resolution Chain Position Source
AF-Q53B88-F1 Predicted AlphaFoldDB

No variants for Q53B88

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q53B88

No associated diseases with Q53B88

5 regional properties for Q53B88

Type Name Position InterPro Accession
domain CARD domain 26 - 120 IPR001315-1
domain CARD domain 134 - 218 IPR001315-2
domain NACHT nucleoside triphosphatase 293 - 462 IPR007111
domain NOD2, winged helix domain 546 - 587 IPR041075
domain NACHT, LRR and PYD domains-containing protein, helical domain HD2 603 - 757 IPR041267

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane ; Lipid-anchor
  • Basolateral cell membrane
  • Cytoplasm
  • Mitochondrion
  • Palmitoylation promotes localization to the cell membrane, where it detects bacterial invasion at the point of entry
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
basolateral plasma membrane The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis.
cell surface The external part of the cell wall and/or plasma membrane.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
vesicle Any small, fluid-filled, spherical organelle enclosed by membrane.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
CARD domain binding Binding to a CARD (N-terminal caspase recruitment) domain, a protein-protein interaction domain that belongs to the death domain-fold superfamily. These protein molecule families are similar in structure with each consisting of six or seven anti-parallel alpha-helices that form highly specific homophilic interactions between signaling partners. CARD exists in the N-terminal prodomains of several caspases and in apoptosis-regulatory proteins and mediates the assembly of CARD-containing proteins that participate in activation or suppression of CARD carrying members of the caspase family.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
muramyl dipeptide binding Interacting selectively and non-covalently, in a non-covalent manner, with muramyl dipeptide; muramyl dipeptide is derived from peptidoglycan.
peptidoglycan binding Interacting selectively and non-covalently, in a non-covalent manner, with peptidoglycan, any of a class of glycoconjugates found in bacterial cell walls.
protein kinase binding Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.

16 GO annotations of biological process

Name Definition
cellular response to lipopolysaccharide Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria.
cellular response to muramyl dipeptide Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a muramyl dipeptide stimulus. Muramyl dipeptide is derived from peptidoglycan.
defense response to bacterium Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.
detection of bacterium The series of events in which a stimulus from a bacterium is received and converted into a molecular signal.
detection of muramyl dipeptide The series of events in which a muramyl dipeptide stimulus is received by a cell and converted into a molecular signal. Muramyl dipeptide is derived from peptidoglycan.
innate immune response Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens.
intracellular signal transduction The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell.
nucleotide-binding oligomerization domain containing 2 signaling pathway The series of molecular signals initiated by the binding of a ligand (such as a bacterial peptidoglycan) to a cytoplasmic nucleotide-binding oligomerization domain containing 2 (NOD2) protein receptor, and ending with regulation of a downstream cellular process.
positive regulation of cytokine production involved in immune response Any process that activates or increases the frequency, rate, or extent of cytokine production that contributes to an immune response.
positive regulation of I-kappaB kinase/NF-kappaB signaling Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
positive regulation of interleukin-1 beta production Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
positive regulation of interleukin-17 production Any process that activates or increases the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
positive regulation of NF-kappaB transcription factor activity Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB.
positive regulation of transcription by RNA polymerase II Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.
regulation of apoptotic process Any process that modulates the occurrence or rate of cell death by apoptotic process.
response to muramyl dipeptide Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a muramyl dipeptide stimulus. Muramyl dipeptide is derived from peptidoglycan.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGEEGGSVSH DEEERASVLL GQYLGCEMCS QEAFQAQRSQ LVELLVSGSL EGFESVLDWL
70 80 90 100 110 120
LSWEVLSWED YEGFHLLGQP LSHLARRLLD TVWNKGTWAC QKLIAAAQEA QADSQSPKLH
130 140 150 160 170 180
GCWDPHSLHP ARDLQSHRPA IVRRLHSHVE GVLDLAWERG FVSQYECDEI RLPIFTPSQR
190 200 210 220 230 240
ARRLLDLATV KANGLAAFLL QHVQELPVPL ALPLEAATCR KYMAKLRTTV SAQSRFLSTY
250 260 270 280 290 300
DGAETLCLED IYTENVLEVW ADVGTAGPPP KSPATLGLEE LFSTPGHLND DADTVLVVGE
310 320 330 340 350 360
AGSGKSTLLQ RLHLLWAAGR DFQEFLFVFP FSCRQLQCMA KPLSVRTLLF EHCCWPDVGQ
370 380 390 400 410 420
EDIFQLLLDH PDRVLLTFDG FDEFKFRFTD RERHCSPTDP TSVQTLLFNL LQGNLLKNAR
430 440 450 460 470 480
KVVTSRPAAV SAFLRKYIRT EFNLKGFSEQ GIELYLRKRH REPGVADRLI RLLQATSALH
490 500 510 520 530 540
GLCHLPVFSW MVSKCHQELL LQEGGSPKTT TDMYLLILQH FLLHAIPPDS ASQGLGPSLL
550 560 570 580 590 600
RGRLPTLLHL GRLALWGLGM CCYVFSAQQL QAAQVSPDDI SLGFLVRAKG VVPGSTAPLE
610 620 630 640 650 660
FLHITFQCFF AAFYLALSAD VPPALLRHLF NCGRPGNSPV ARLLPTLCIQ GSEGKDSSVA
670 680 690 700 710 720
ALLQKAEPHN LQITAAFLAG LLSREHWGLL AECQTSEKAL LRRQACARWC LARSLRKHFH
730 740 750 760 770 780
SIPPAAPGEA KSMHAMPGFI WLIRSLYEMQ EERLARKAAR GLNVGHLKLT FCSVGPAECA
790 800 810 820 830 840
ALAFVLQHLR RPVALQLDYN SVGDIGVEQL LPCLGVCKAL YLRDNNISDR GICKLIECAL
850 860 870 880 890 900
HCEQLQKLVL FNNKLTDGCA HSMAKLLACR QNFLALRLGN NHITPAGAQV LAEGLRGNTS
910 920 930 940 950 960
LQFLGFWGNR VGDEGAQALA EALGDHQSLR WLSLVGNNIG SVGAQALALM LAKNVMLEEL
970 980 990 1000 1010 1020
CLEENHIQDE GVCSLAEGLK KNSSLKILKL SNNCITYLGA KALLQALERN DTILEVWLRG
1030
NIFSLEEVDK LGCRDIRLLL