NLRP12

NLR family, pyrin domain containing 12
Identifiers
Symbols	NLRP12; CLR19.3; FCAS2; NALP12; PAN6; PYPAF7; RNO; RNO2
External IDs	OMIM: 609648 HomoloGene: 16972 GeneCards: NLRP12 Gene
Gene Ontology Molecular function • nucleotide binding • protein binding • ATP binding • caspase activator activity Cellular component • cytoplasm Biological process • activation of caspase activity • signal transduction • release of cytoplasmic sequestered NF-kappaB • negative regulation of signal transduction • negative regulation of protein autophosphorylation • negative regulation of I-kappaB kinase/NF-kappaB cascade • regulation of interleukin-18 biosynthetic process • negative regulation of interleukin-6 biosynthetic process • negative regulation of Toll signaling pathway • negative regulation of cytokine secretion • negative regulation of interleukin-1 secretion • positive regulation of interleukin-1 beta secretion • positive regulation of inflammatory response Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	91662	378425
Ensembl	ENSG00000142405	ENSMUSG00000078817
UniProt	P59046	n/a
RefSeq (mRNA)	NM_033297.2	NM_001033431.1
RefSeq (protein)	NP_150639.1	NP_001028603.1
Location (UCSC)	Chr 19: 54.3 – 54.33 Mb	Chr 7: 3.22 – 3.25 Mb
PubMed search	[1]	[2]

NACHT, LRR and PYD domains-containing protein 12 is a protein that in humans is encoded by the NLRP12 gene.^[1][2][3]

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]^[3]

References

1. ^ 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. 
2. ^ 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. 
3. ^ ^{a b} "Entrez Gene: NLRP12 NLR family, pyrin domain containing 12". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=91662. 

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. 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. PMID 17947705.