B0FPE9

SS
Gene name
NLRP3
Protein name
NACHT, LRR and PYD domains-containing protein 3
Names
Species
Macaca mulatta (Rhesus macaque)
KEGG Pathway
mcc:701278
EC number
Protein Class

Descriptions

PYPAF1 (PYRIN-containing Apaf1-like protein 1) is a novel PYRIN-containing signaling protein that belongs to the nucleotide-binding site/leucine-rich repeat (NBS/LRR) family of signaling proteins. C-terminal leucine-rich repeats (LRRs) may function as a negative regulator of PYPAF1 activity. PYPAF1 and ASC function to regulate the activation of NF-B.

Autoinhibitory domains (AIDs)

741-990 (Leucine-rich repeats) SS

Target domain

1-93 (PYRIN domain)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B0FPE9

Entry ID Method Resolution Chain Position Source
AF-B0FPE9-F1 Predicted AlphaFoldDB

No variants for B0FPE9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0FPE9

No associated diseases with B0FPE9

10 regional properties for B0FPE9

Type Name Position InterPro Accession
repeat Leucine-rich repeat 739 - 761 IPR001611-1
repeat Leucine-rich repeat 795 - 818 IPR001611-2
repeat Leucine-rich repeat 853 - 871 IPR001611-3
repeat Leucine-rich repeat 909 - 932 IPR001611-4
repeat Leucine-rich repeat 967 - 989 IPR001611-5
domain DAPIN domain 1 - 93 IPR004020
domain NACHT nucleoside triphosphatase 220 - 536 IPR007111
domain NACHT-associated domain 139 - 210 IPR029495
domain NOD2, winged helix domain 466 - 520 IPR041075
domain NACHT, LRR and PYD domains-containing protein, helical domain HD2 522 - 645 IPR041267

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytosol
  • Inflammasome
  • Cytoplasm, cytoskeleton, microtubule organizing center
  • Golgi apparatus membrane
  • Endoplasmic reticulum
  • Mitochondrion
  • Secreted
  • Nucleus
  • In macrophages, under resting conditions, mainly located in the cytosol and on membranes of various organelles, such as endoplasmic reticulum, mitochondria and Golgi: forms an inactive double-ring cage that is primarily localized on membranes
  • Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes for the formation of an active inflammasome complex
  • Recruited to dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P)
  • After the induction of pyroptosis, inflammasome specks are released into the extracellular space where they can further promote IL1B processing and where they can be engulfed by macrophages
  • Phagocytosis induces lysosomal damage and inflammasome activation in the recipient cells
  • In the Th2 subset of CD4(+) helper T-cells, mainly located in the nucleus
  • Nuclear localization depends upon KPNA2
  • In the Th1 subset of CD4(+) helper T-cells, mainly cytoplasmic
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
NLRP3 inflammasome complex An inflammasome complex that consists of three components, NLRP3 (NALP3), PYCARD and caspase-1. It is activated upon exposure to whole pathogens, as well as a number of structurally diverse pathogen- and danger-associated molecular patterns (PAMPs and DAMPs) and environmental irritants. Whole pathogens demonstrated to activate the NLRP3 inflammasome complex include the fungi Candida albicans and Saccharomyces cerevisiae, bacteria that produce pore-forming toxins, including Listeria monocytogenes and Staphylococcus aureus, and viruses such as Sendai virus, adenovirus, and influenza virus.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA-binding transcription factor binding Binding to a DNA-binding transcription factor, a protein that interacts with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription.
sequence-specific DNA binding Binding to DNA of a specific nucleotide composition, e.g. GC-rich DNA binding, or with a specific sequence motif or type of DNA e.g. promotor binding or rDNA binding.

9 GO annotations of biological process

Name Definition
inflammatory response The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages.
innate immune response Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens.
negative regulation of NIK/NF-kappaB signaling Any process that stops, prevents or reduces the frequency, rate or extent of NIK/NF-kappaB signaling.
positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Any process that activates or increases the activity of a cysteine-type endopeptidase involved in the apoptotic process.
positive regulation of interleukin-4 production Any process that activates or increases the frequency, rate, or extent of interleukin-4 production.
positive regulation of T-helper 2 cell cytokine production Any process that activates or increases the frequency, rate or extent of T-helper 2 cell cytokine production.
positive regulation of T-helper 2 cell differentiation Any process that activates or increases the frequency, rate or extent of T-helper 2 cell differentiation.
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.
positive regulation of type 2 immune response Any process that activates or increases the frequency, rate, or extent of a type 2 immune response.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A6QLE5 NLRP3 NACHT, LRR and PYD domains-containing protein 3 Bos taurus (Bovine) SS
Q96P20 NLRP3 NACHT, LRR and PYD domains-containing protein 3 Homo sapiens (Human) EV
E9Q5R7 Nlrp12 NACHT, LRR and PYD domains-containing protein 12 Mus musculus (Mouse) SS
Q8R4B8 Nlrp3 NACHT, LRR and PYD domains-containing protein 3 Mus musculus (Mouse) SS
D4A523 Nlrp3 NACHT, LRR and PYD domains-containing protein 3 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MKMASTRCKL ARYLEDLEDV DLKKFKMHLE DYPPQKGCIS LPRGQTEKAD HVDLATLMID
70 80 90 100 110 120
FNGEEKAWAM AVWIFAAINR RDLYEKAKRD EPKWGSDNAR VSNPTVICQE DSIEEEWMGL
130 140 150 160 170 180
LEYLSRISIC KKKKDYCKKY RKYVRSRFQC IEDRNARLGE SVSLNKRYTR LRLIKEHRSQ
190 200 210 220 230 240
QEREHELLAI GKTKTWESPV SPIKMELLFD PDDEHSEPVH TVVFQGAAGI GKTILARKIM
250 260 270 280 290 300
LDWASGTLYQ DRFDYLFYIH CREVSLVTQR SLGDLIMSCC PDPNPPIRKI VSKPSRILFL
310 320 330 340 350 360
MDGFDELQGA FDEHIGPLCT DWQKAERGDI LLSSLIRKKL LPEASLLITT RPVALEKLQH
370 380 390 400 410 420
LLDHPRHVEI LGFSEAKRKE YFFKYFSDEA QARAAFSLIQ ENEVLFTMCF IPLVCWIVCT
430 440 450 460 470 480
GLKQQMESGK SLAQTSKTTT AVYTFFLSSL LQPRGGSQEH RLCAHLWGLC SLAADGIWNQ
490 500 510 520 530 540
KILFEESDLR NHGLQKADVS AFLRMNLFQK EVDCEKFYSF IHMTFQEFFA AMYYLLEEEK
550 560 570 580 590 600
EGRTNVPGSC LKLPSRDVTV LLENYGKFEK GYLIFVVRFL FGLVNQERTC YLEKKLSCKI
610 620 630 640 650 660
SQQIRLELLK WIEVKAKAKK LQIQPSQLEL FYCLYEMQEE DFVQRAMDYF PKIEINLSTR
670 680 690 700 710 720
MDHVVSSFCI ENCHRVESLS LGFLHNMPKE EEEEEKEGRH LDMVQCVLPG SHAACSHRLV
730 740 750 760 770 780
NSHLTSSFCR GLFSVLSTSQ SLTELDLSDN SLGDPGMRVL CETLQHPDCN IRRLWLGRCG
790 800 810 820 830 840
LSHECCFDIS LVLSSNQKLV ELDLSDNALG DFGIRLLCVG LKHLLCNLKK LWLVSCCLTS
850 860 870 880 890 900
ACCQDLASVL STSRSLTRLY VGENALGDAG VAILCEKAKN PQCNLQKLGL VNSGLTSACC
910 920 930 940 950 960
SALSSVLSTN QNLTHLYLRG NTLGDKGIKL LCEGLLHPDC KLQVLELDNC NLTSHCCWDL
970 980 990 1000 1010 1020
STLLTSSQSL RKLSLGNNDL GDLGVMMFCE VLKQQSCLLQ NLGLSEMYFN YETKSALETL
1030
QEEKPELTIV FEPSW