NLRP12

NLRP12
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2L6A, 4XHS
Identifiers
Aliases	NLRP12, CLR19.3, FCAS2, NALP12, PAN6, PYPAF7, RNO, RNO2, NLR family, pyrin domain containing 12, NLR family pyrin domain containing 12
External IDs	MGI: 2676630 HomoloGene: 16972 GeneCards: NLRP12
Gene ontology Molecular function • nucleotide binding • cysteine-type endopeptidase activator activity involved in apoptotic process • ATP binding • protein binding Cellular component • cytoplasm • nucleus Biological process • regulation of interleukin-18 biosynthetic process • dendritic cell migration • positive regulation of interleukin-1 beta secretion • negative regulation of interleukin-1 secretion • regulation of cysteine-type endopeptidase activity involved in apoptotic process • release of cytoplasmic sequestered NF-kappaB • regulation of I-kappaB kinase/NF-kappaB signaling • activation of cysteine-type endopeptidase activity involved in apoptotic process • negative regulation of Toll signaling pathway • signal transduction • negative regulation of NIK/NF-kappaB signaling • negative regulation of inflammatory response • cellular response to cytokine stimulus • negative regulation of I-kappaB kinase/NF-kappaB signaling • positive regulation of inflammatory response • negative regulation of protein autophosphorylation • positive regulation of MHC class I biosynthetic process • negative regulation of interleukin-6 biosynthetic process • negative regulation of ERK1 and ERK2 cascade • negative regulation of cytokine secretion • negative regulation of NF-kappaB transcription factor activity • negative regulation of signal transduction Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	91662	378425
Ensembl	ENSG00000142405	n/a
UniProt	P59046	E9Q5R7
RefSeq (mRNA)	NM_001277126 NM_001277129 NM_033297 NM_144687	NM_001033431
RefSeq (protein)	NP_001264055.1 NP_001264058.1 NP_653288.1	NP_001028603.1
Location (UCSC)	Chr 19: 53.79 – 53.82 Mb	Chr 7: 3.22 – 3.25 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

NACHT, LRR and PYD domains-containing protein 12 is a protein that in humans is encoded by the NLRP12 gene.^[3][4][5]

NALPs are cytoplasmic proteins that form a subfamily within the larger CATERPILLER protein family. Most short NALPs, such as NALP12, have an N-terminal pyrin (MEFV; MIM 608107) domain (PYD), followed by a NACHT domain, a NACHT-associated domain (NAD), and a C-terminal leucine-rich repeat (LRR) region. The long NALP, NALP1 (MIM 606636), also has a C-terminal extension containing a function to find domain (FIIND) and a caspase recruitment domain (CARD). NALPs are implicated in the activation of proinflammatory caspases (e.g., CASP1; MIM 147678) via their involvement in multiprotein complexes called inflammasomes (Tschopp et al., 2003).[supplied by OMIM]^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Tschopp J, Martinon F, Burns K (Feb 2003). "NALPs: a novel protein family involved in inflammation". Nat Rev Mol Cell Biol. 4 (2): 95–104. doi:10.1038/nrm1019. PMID 12563287.
4. Wang L, Manji GA, Grenier JM, Al-Garawi A, Merriam S, Lora JM, Geddes BJ, Briskin M, DiStefano PS, Bertin J (Aug 2002). "PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates activation of NF-kappa B and caspase-1-dependent cytokine processing". J Biol Chem. 277 (33): 29874–80. doi:10.1074/jbc.M203915200. PMID 12019269.
5. "Entrez Gene: NLRP12 NLR family, pyrin domain containing 12".

Further reading

• Shami PJ, Kanai N, Wang LY, et al. (2001). "Identification and characterization of a novel gene that is upregulated in leukaemia cells by nitric oxide.". Br. J. Haematol. 112 (1): 138–47. doi:10.1046/j.1365-2141.2001.02491.x. PMID 11167794.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Williams KL, Taxman DJ, Linhoff MW, et al. (2003). "Cutting edge: Monarch-1: a pyrin/nucleotide-binding domain/leucine-rich repeat protein that controls classical and nonclassical MHC class I genes.". J. Immunol. 170 (11): 5354–8. doi:10.4049/jimmunol.170.11.5354. PMID 12759408.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Williams KL, Lich JD, Duncan JA, et al. (2006). "The CATERPILLER protein monarch-1 is an antagonist of toll-like receptor-, tumor necrosis factor alpha-, and Mycobacterium tuberculosis-induced pro-inflammatory signals.". J. Biol. Chem. 280 (48): 39914–24. doi:10.1074/jbc.M502820200. PMID 16203735.
• Lich JD, Williams KL, Moore CB, et al. (2007). "Monarch-1 suppresses non-canonical NF-kappaB activation and p52-dependent chemokine expression in monocytes.". J. Immunol. 178 (3): 1256–60. doi:10.4049/jimmunol.178.3.1256. PMID 17237370.
• Arthur JC, Lich JD, Aziz RK, et al. (2007). "Heat shock protein 90 associates with monarch-1 and regulates its ability to promote degradation of NF-kappaB-inducing kinase.". J. Immunol. 179 (9): 6291–6. doi:10.4049/jimmunol.179.9.6291. PMID 17947705.