NLRP1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0006919Biological processactivation of cysteine-type endopeptidase activity involved in apoptotic process
GO_0051260Biological processprotein homooligomerization
GO_0002221Biological processpattern recognition receptor signaling pathway
GO_0032495Biological processresponse to muramyl dipeptide
GO_0007165Biological processsignal transduction
GO_0051607Biological processdefense response to virus
GO_0070269Biological processpyroptotic inflammatory response
GO_0050727Biological processregulation of inflammatory response
GO_0071493Biological processcellular response to UV-B
GO_0032731Biological processpositive regulation of interleukin-1 beta production
GO_0051402Biological processneuron apoptotic process
GO_0042981Biological processregulation of apoptotic process
GO_0097264Biological processself proteolysis
GO_0042742Biological processdefense response to bacterium
GO_1904784Biological processNLRP1 inflammasome complex assembly
GO_0006915Biological processapoptotic process
GO_0050729Biological processpositive regulation of inflammatory response
GO_0140374Biological processantiviral innate immune response
GO_0072558Cellular componentNLRP1 inflammasome complex
GO_0005730Cellular componentnucleolus
GO_0005654Cellular componentnucleoplasm
GO_0005829Cellular componentcytosol
GO_0005737Cellular componentcytoplasm
GO_0061702Cellular componentcanonical inflammasome complex
GO_0005634Cellular componentnucleus
GO_0019899Molecular functionenzyme binding
GO_0008233Molecular functionpeptidase activity
GO_0038187Molecular functionpattern recognition receptor activity
GO_0019904Molecular functionprotein domain specific binding
GO_0003690Molecular functiondouble-stranded DNA binding
GO_0008656Molecular functioncysteine-type endopeptidase activator activity involved in apoptotic process
GO_0035591Molecular functionsignaling adaptor activity
GO_0140693Molecular functionmolecular condensate scaffold activity
GO_0005524Molecular functionATP binding
GO_0140608Molecular functioncysteine-type endopeptidase activator activity
GO_0005515Molecular functionprotein binding
GO_0016887Molecular functionATP hydrolysis activity
GO_0003725Molecular functiondouble-stranded RNA binding

IV. Literature review

[source]
Gene nameNLRP1
Protein nameNACHT, LRR and PYD domains-containing protein 1
NLRP1 protein
NLR family pyrin domain containing 1
NACHT, LRR and PYD domains-containing protein 1 (EC 3.4.-.-) (EC 3.6.4.-) (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1, C-terminus (NLRP1-CT); NACHT, LRR and PYD domains-containing protein 1, N-terminus (NLRP1-NT)]
SynonymsNAC
KIAA0926
CARD7
NALP1
DEFCAP
DescriptionFUNCTION: Acts as the sensor component of the NLRP1 inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis . Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation . Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as cleavage by some human enteroviruses and rhinoviruses, double-stranded RNA, UV-B irradiation, or Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex composed of NLRP1, CASP1 and PYCARD/ASC . In response to pathogen-associated signals, the N-terminal part of NLRP1 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes and associates with PYCARD/ASC to initiate the formation of the inflammasome complex: the NLRP1 inflammasome recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis . In the absence of GSDMD expression, the NLRP1 inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) . Activation of NLRP1 inflammasome is also required for HMGB1 secretion; the active cytokines and HMGB1 stimulate inflammatory responses . Binds ATP and shows ATPase activity . Plays an important role in antiviral immunity and inflammation in the human airway epithelium . Specifically recognizes a number of pathogen-associated signals: upon infection by human rhinoviruses 14 and 16 (HRV-14 and HRV-16), NLRP1 is cleaved and activated which triggers NLRP1-dependent inflammasome activation and IL18 secretion . Positive-strand RNA viruses, such as Semliki forest virus and long dsRNA activate the NLRP1 inflammasome, triggering IL1B release in a NLRP1-dependent fashion . Acts as a direct sensor for long dsRNA and thus RNA virus infection . May also be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner . The NLRP1 inflammasome is also activated in response to UV-B irradiation causing ribosome collisions: ribosome collisions cause phosphorylation and activation of NLRP1 in a MAP3K20-dependent manner, leading to pyroptosis . .; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1]: Constitutes the precursor of the NLRP1 inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. .; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1, N-terminus]: Regulatory part that prevents formation of the NLRP1 inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of NLRP1 (NACHT, LRR and PYD domains-containing protein 1, C-terminus), preventing activation of the NLRP1 inflammasome . In response to pathogen-associated signals, this part is ubiquitinated and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the NLRP1 inflammasome . .; FUNCTION: [NACHT, LRR and PYD domains-containing protein 1, C-terminus]: Constitutes the active part of the NLRP1 inflammasome . In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of NLRP1 (NACHT, LRR and PYD domains-containing protein 1, N-terminus), preventing activation of the NLRP1 inflammasome . In response to pathogen-associated signals, the N-terminal part of NLRP1 is degraded by the proteasome, releasing this form, which polymerizes and associates with PYCARD/ASC to form of the NLRP1 inflammasome complex: the NLRP1 inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis . .; FUNCTION: [Isoform 2]: It is unclear whether is involved in inflammasome formation. It is not cleaved within the FIIND domain, does not assemble into specks, nor promote IL1B release . However, in an vitro cell-free system, it has been shown to be activated by MDP . .

AccessionsENST00000699713.1
A0A8V8TNJ2
A0A8V8TP02
A0A8V8TPC6
A0A8V8TP07
ENST00000572272.6 [Q9C000-1]
ENST00000699613.1
ENST00000699801.1
ENST00000699644.1
ENST00000699707.1
A0A8V8TQB8
ENST00000699775.1
ENST00000699800.1
ENST00000699630.1
ENST00000699625.1
ENST00000699645.1
A0A8V8TQ83
ENST00000699615.1
Q9C000
A0A8V8TNG2
ENST00000699622.1
ENST00000699804.1
ENST00000699634.1
A0A8V8TNH7
A0A8V8TQ99
A0A8V8TP94
A0A8V8TQ85
ENST00000699771.1
ENST00000544378.7 [Q9C000-5]
A0A8V8TNV8
ENST00000699776.1
ENST00000576905.5
A0A8V8TQI5
ENST00000699712.1
ENST00000699586.1
ENST00000699808.1
ENST00000354411.8 [Q9C000-4]
ENST00000617618.5 [Q9C000-1]
ENST00000699632.1
A0A8V8TP36
ENST00000699773.1
ENST00000699806.1
A0A8V8TP42
Q96AM0
A0A8V8TP48
ENST00000699777.1
A0A8V8TNN3
ENST00000699633.1
A0A8V8TQ79
ENST00000699809.1
ENST00000699612.1
A0A8V8TNK6
ENST00000699710.1
ENST00000699805.1
ENST00000699772.1
A0A8V8TNR1
A0A8V8TNV2
ENST00000699774.1
ENST00000699807.1
ENST00000699629.1
ENST00000571451.7 [Q9C000-2]
A0A8V8TNS7
ENST00000699623.1
ENST00000572143.2
ENST00000571307.2
ENST00000699709.1 [Q9C000-1]
A0A8V8TPW2
A0A8V8TNP3
ENST00000262467.11 [Q9C000-5]
ENST00000699614.1
A0A8V8TQ17
A0A8V8TPB9
A0A8V8TQB3
ENST00000699643.1
A0A8V8TNS2
A0A8V8TP14
A0A8V8TQE6
A0A8V8TQ11
ENST00000699626.1
ENST00000699802.1
ENST00000269280.9 [Q9C000-2]
A0A8V8TQK4
A0A8V8TPB4
A0A8V8TNP9
I3L0S2
A0A8V8TNR8
ENST00000699708.1
ENST00000577119.5 [Q9C000-3]
ENST00000699665.1
ENST00000576905.6 [Q9C000-2]
A0A8V8TNV1
A0A8V8TQL0
ENST00000699642.1
ENST00000699711.1
A0A8V8TP05
A0A8V8TQA8
A0A8V8TP12
ENST00000699705.1
A0A8V8TQ55
A0A8V8TNU7
ENST00000699803.1
ENST00000699810.1
ENST00000699706.1