ABHD6
Identifiers
AliasesABHD6, abhydrolase domain containing 6, abhydrolase domain containing 6, acylglycerol lipase
External IDsOMIM: 616966 MGI: 1913332 HomoloGene: 23246 GeneCards: ABHD6
Orthologs
SpeciesHumanMouse
Entrez

57406

66082

Ensembl

ENSG00000163686

ENSMUSG00000025277

UniProt

Q9BV23

Q8R2Y0

RefSeq (mRNA)

NM_020676
NM_001320126

NM_025341
NM_001331064
NM_001331065

RefSeq (protein)

NP_001307055
NP_065727
NP_065727.4
NP_001307055.1

NP_001317993
NP_001317994
NP_079617

Location (UCSC)Chr 3: 58.24 – 58.3 MbChr 14: 14.41 – 14.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

alpha/beta-Hydrolase domain containing 6 (ABHD6), also known as monoacylglycerol lipase ABHD6 or 2-arachidonoylglycerol hydrolase is an enzyme that in humans is encoded by the ABHD6 gene.

Function

ABHD6 is a serine hydrolyzing enzyme that possesses typical α/β-hydrolase family domains. ABHD6 was first studied because of its over-expression in certain forms of tumours.[5]

ABHD6 has been linked to regulation of the endocannabinoid system as it controls the accumulation of 2-arachidonoylglycerol (2-AG) at the cannabinoid receptors.[6]

ABHD6 accounts for about 4% of 2-AG brain hydrolysis.[7] Together, monoacylglycerol lipase (MAGL), ABHD12, and ABHD6 control about 99% of 2-AG signalling in the brain,[7][8] and each enzyme exhibits a distinct subcellular distribution, suggesting that they regulate distinct pools of 2-AG in the nervous system.[9]

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000163686 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025277 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Li F, Fei X, Xu J, Ji C (April 2009). "An unannotated alpha/beta hydrolase superfamily member, ABHD6 differentially expressed among cancer cell lines". Molecular Biology Reports. 36 (4): 691–6. doi:10.1007/s11033-008-9230-7. PMID 18360779. S2CID 6795598.
  6. ↑ Marrs WR, Blankman JL, Horne EA, Thomazeau A, Lin YH, Coy J, Bodor AL, Muccioli GG, Hu SS, Woodruff G, Fung S, Lafourcade M, Alexander JP, Long JZ, Li W, Xu C, Möller T, Mackie K, Manzoni OJ, Cravatt BF, Stella N (August 2010). "The serine hydrolase ABHD6 controls the accumulation and efficacy of 2-AG at cannabinoid receptors". Nature Neuroscience. 13 (8): 951–7. doi:10.1038/nn.2601. PMC 2970523. PMID 20657592.
  7. 1 2 Cannabinoid Receptors—Advances in Research and Application: 2012 Edition: ScholarlyBrief. ScholarlyEditions. 26 December 2012. pp. 68–. ISBN 978-1-4816-0672-1.
  8. ↑ Savinainen JR, Saario SM, Laitinen JT (February 2012). "The serine hydrolases MAGL, ABHD6 and ABHD12 as guardians of 2-arachidonoylglycerol signalling through cannabinoid receptors". Acta Physiologica. 204 (2): 267–76. doi:10.1111/j.1748-1716.2011.02280.x. PMC 3320662. PMID 21418147.
  9. ↑ Blankman JL, Simon GM, Cravatt BF (December 2007). "A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol". Chemistry & Biology. 14 (12): 1347–56. doi:10.1016/j.chembiol.2007.11.006. PMC 2692834. PMID 18096503.
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