NLRP12

From Wikipedia, the free encyclopedia

NLR family, pyrin domain containing 12

Identifiers

NLRP12; CLR19.3; Monarch1; NALP12; PAN6; PYPAF7; RNO; RNO2

External IDs

Gene ontology
Molecular Function:	• nucleotide binding • protein binding • ATP binding • caspase activator activity
Cellular Component:	• cytoplasm
Biological Process:	• caspase activation • signal transduction • release of cytoplasmic sequestered NF-kappaB • negative regulation of protein amino acid 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 interleukin-1 secretion • positive regulation of interleukin-1 beta secretion • positive regulation of inflammatory response

Orthologs

Human

Mouse

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Refseq

NM_033297 (mRNA)
NP_150639 (protein)

n/a (mRNA)
n/a (protein)

Location

Chr 19: 58.99 - 59.02 Mb

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Pubmed search

[1]

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NLR family, pyrin domain containing 12, also known as NLRP12, is a human gene.^[1]

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]^[1]

[edit] References

^ ^a ^b Entrez Gene: NLRP12 NLR family, pyrin domain containing 12.

[edit] Further reading

Tschopp J, Martinon F, Burns K (2003). "NALPs: a novel protein family involved in inflammation.". Nat. Rev. Mol. Cell Biol. 4 (2): 95-104. doi:10.1038/nrm1019. PMID 12563287.
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. PMID 11167794.
Wang L, Manji GA, Grenier JM, et al. (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.
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. 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. 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. 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. 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.