Q2LKW6

EV
Gene name
Nlrp1b
Protein name
NACHT, LRR and PYD domains-containing protein 1b allele 1
Names
Species
Mus musculus (Mouse)
KEGG Pathway
EC number
Protein Class
NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 1 (PTHR46985)

Descriptions

Nlrp1b is a receptor that detects the reduction of cellular ATP. Upon activation, this receptor recruits procaspase-1, which promotes cytokine processing and a proinflammatory form of cell death termed pyroptosis. The leucine-rich repeat (LRR) domain in Nlrp1b, interacting with NACHT domain within the same protein, is involved in autoinhibition and mutations within the LRR domain activates the protein.

Autoinhibitory domains (AIDs)

625-709 (Leucine-rich repeat) EV

Target domain

126-435 (NACHT domain)

Relief mechanism

Cleavage

Assay

Mutagenesis experiment, Deletion assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q2LKW6

Entry ID Method Resolution Chain Position Source
AF-Q2LKW6-F1 Predicted AlphaFoldDB

No variants for Q2LKW6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2LKW6

No associated diseases with Q2LKW6

4 regional properties for Q2LKW6

Type Name Position InterPro Accession
domain Protein kinase domain 16 - 269 IPR000719
active_site Serine/threonine-protein kinase, active site 135 - 147 IPR008271
domain Ubiquitin-associated domain 291 - 334 IPR015940
binding_site Protein kinase, ATP binding site 22 - 45 IPR017441

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytosol
  • Membrane
  • ;
PANTHER Family PTHR46985 NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 1
PANTHER Subfamily PTHR46985:SF5 NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 1B ALLELE 2
PANTHER Protein Class defense/immunity protein
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
inflammasome complex A cytosolic protein complex that is capable of activating caspase-1.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
NLRP1 inflammasome complex An inflammasome complex that consists of two components, NLRP1 (NALP1) and caspase-1 or caspase-5. The exact mechanisms of NLRP1 activation remain obscure, but potassium ion efflux appears to be essential.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
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.

9 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
cysteine-type endopeptidase activator activity Binds to and increases the activity of a cysteine-type endopeptidase.
double-stranded DNA binding Binding to double-stranded DNA.
double-stranded RNA binding Binding to double-stranded RNA.
endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
enzyme binding Binding to an enzyme, a protein with catalytic activity.
peptidase activity Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
protein domain specific binding Binding to a specific domain of a protein.
protein self-association Binding to a domain within the same polypeptide.

12 GO annotations of biological process

Name Definition
activation of cysteine-type endopeptidase activity involved in apoptotic process Any process that initiates the activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process.
antiviral innate immune response A defense response against viruses mediated through an innate immune response. An innate immune response is mediated by germline encoded components that directly recognize components of potential pathogens.
defense response to virus Reactions triggered in response to the presence of a virus that act to protect the cell or organism.
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.
neuron apoptotic process Any apoptotic process in a neuron, the basic cellular unit of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the nervous system.
NLRP1 inflammasome complex assembly The aggregation, arrangement and bonding together of a set of components to form a NLRP1 inflammasome complex.
positive regulation of interleukin-1 beta production Any process that activates or increases the frequency, rate, or extent of interleukin-1 beta production.
protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
protein homooligomerization The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
pyroptosis A caspase-1-dependent cell death subroutine that is associated with the generation of pyrogenic mediators such as IL-1beta and IL-18.
regulation of apoptotic process Any process that modulates the occurrence or rate of cell death by apoptotic process.
self proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEESPPKQKS NTKVAQHEGQ QDLNTTRHMN VELKHRPKLE RHLKLGMIPV VYMKQGEEIL
70 80 90 100 110 120
YPAQSLREEN LIQNFTSLLL LQKLCPKDPE NMIRKSWASC VPEEGGHMIN IQDLFGPNIG
130 140 150 160 170 180
TQKEPQLVII EGAAGIGKST LARLVKRAWK EGQLYRDHFQ HVFFFSCREL AQCKKLSLAE
190 200 210 220 230 240
LIAQGQEVPT APINQILSHP EKLLFILDGI DEPAWVLADQ NPELCLHWSQ RQPVHTLLGS
250 260 270 280 290 300
LLGKSILPEA FFLLTTRTTA LQKFIPSLPM PCQVEVLGFS GIERENYFYK YFANQRHAIT
310 320 330 340 350 360
AFMMVESNPV LLTLCEVPWV CWLVCTCLKK QMEQGRVLSL KSQTTTALCL KYLSLTIPDK
370 380 390 400 410 420
HRRTQVKALC SLAAEGIWKR RTLFSESDLC KQGLDEDAVA TFLKTGVLQK QASSLSYSFA
430 440 450 460 470 480
HLCLQEFFAA ISCILEDSEE RHGNMEMDRI VETLVERYGR QNLFEAPTVR FLFGLLGKEG
490 500 510 520 530 540
VKGMEKLFSC SLHGKTNLKL LWHILVKSQP HQPPCLGLLH CLYENQDMEL LTHVMHDLQG
550 560 570 580 590 600
TIVPGPNDTA HTVLQTNVKH LVVQTDMELM VATFCIQFYC HVRTLQLNME KQQGYALISP
610 620 630 640 650 660
RMVLYRWTPI TNASWEILFY NLKFTRNLEG LDLSGNSLRY SVVQSLCNTL RYPGCQLKTL
670 680 690 700 710 720
WLVKCGLTSR YCSLLASVLS AHSSLTELYL QLNDLGDDGV RMLCEGLRNP VCNLSILWLD
730 740 750 760 770 780
LSSLSAQVIT ELRTLEEKNP KLYIRSIWMP HMMVPTENMD EEAILTTLKQ QRQESGDKPM
790 800 810 820 830 840
EILGTEEDFW GPTGPVATEL VDRVRNLYRM PQMMVPTENM DEEDILTSFK QQRQQSGANP
850 860 870 880 890 900
MEILGTEEDF WGPIGPVATE VVYRERNLYR VQLPMAGSYH CPSTRLHFVV TRAVTIEIEF
910 920 930 940 950 960
CAWSQFLDKT PLQQSHMVVG PLFDIKAEQG AVTAVYLPHF VSLKDTKAST FDFKVAHFQE
970 980 990 1000 1010 1020
HGMVLETPDR VKPGYTVLKN PSFSPMGVVL RIIPAARHFI PITSITLIYY RVNQEEVTLH
1030 1040 1050 1060 1070 1080
LYLVPNDCTI QKAIDDEEMK FQFVRINKPP PVDNLFIGSR YIVSGSENLE ITPKELELCY
1090 1100 1110 1120 1130 1140
RSSKEFQLFS EIYVGNMGSE IKLQIKNKKH MKLIWEALLK PGDLRPALPR IAQALKDAPS
1150 1160 1170 1180 1190 1200
LLHFMDQHRE QLVARVTSVD PLLDKLHGLV LNEESYEAVR AENTNQDKMR KLFNLSRSWS
1210 1220 1230
RACKDLFYQA LKETHPHLVM DLLEKSGGVS LGS