ABHD12

ABHD12
Identifiers
Aliases	ABHD12, ABHD12A, BEM46L2, C20orf22, PHARC, dJ965G21.2, abhydrolase domain containing 12, habhydrolase domain containing 12, lysophospholipase
External IDs	OMIM: 613599; MGI: 1923442; HomoloGene: 22910; GeneCards: ABHD12; OMA:ABHD12 - orthologs
Gene location (Human)
Chr.	Chromosome 20 (human)
End	25,390,835 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	150,746,661 bp
RNA expression pattern
	Top expressed in
	C1 segment; ; prefrontal cortex; ; body of pancreas; ; left lobe of thyroid gland; ; right lobe of thyroid gland; ; right frontal lobe; ; cingulate gyrus; ; anterior cingulate cortex; ; nucleus accumbens; ; Brodmann area 9;
	Top expressed in
	transitional epithelium of urinary bladder; ; superior frontal gyrus; ; primary visual cortex; ; primary motor cortex; ; seminal vesicula; ; dentate gyrus of hippocampal formation granule cell; ; lateral hypothalamus; ; dorsomedial hypothalamic nucleus; ; pontine nuclei; ; cerebellar cortex;
	More reference expression data
	n/a
Gene ontology
Molecular function	hydrolase activity; lysophospholipase activity; acylglycerol lipase activity; palmitoyl-(protein) hydrolase activity;
Cellular component	integral component of membrane; plasma membrane; AMPA glutamate receptor complex; membrane; cytoplasm; dendrite cytoplasm;
Biological process	acylglycerol catabolic process; phosphatidylserine catabolic process; adult walking behavior; response to auditory stimulus; monoacylglycerol catabolic process; glycerophospholipid catabolic process; protein depalmitoylation;
	Sources:Amigo / QuickGO
Orthologs
	26090
	76192
	ENSG00000100997
	ENSMUSG00000032046
	Q8N2K0
	Q99LR1
	NM_001042472; NM_015600
	NM_024465; NM_001356549; NM_001356550
	NP_001035937; NP_056415
	NP_077785; NP_001343478; NP_001343479
	Wikidata
View/Edit Human	View/Edit Mouse

alpha/beta-Hydrolase domain containing 12 (ABHD12) is a serine hydrolase encoded by the ABHD12 gene that participates in the breakdown of the endocannabinoid neurotransmitter 2-arachidonylglycerol (2-AG) in the central nervous system.^[5] It is responsible for about 9% of brain 2-AG hydrolysis.^[5] Together, ABHD12 along with two other enzymes, monoacylglycerol lipase (MAGL) and ABHD6, control 99% of 2-AG hydrolysis in the brain.^[5]^[6] ABHD12 also serves as a lysophospholipase and metabolizes lysophosphatidylserine (LPS).^[7]

Inhibitors

Inhibitors of ABHD12 have been identified.^[7] Orlistat (tetrahydrolipstatin; THL) and methyl arachidonyl fluorophosphonate (MAFP), so-called "universal lipase/serine hydrolase inhibitors" that are extremely non-selective enzyme inhibitors, were found to inhibit ABHD12.^[7] Selective reversible inhibitors have also been identified, including betulinic acid, maslinic acid, oleanolic acid, and ursolic acid.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000100997 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000032046 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b ^c Cannabinoid Receptors—Advances in Research and Application: 2012 Edition: ScholarlyBrief. ScholarlyEditions. 26 December 2012. pp. 68–. ISBN 978-1-4816-0672-1.
^ 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 Physiol (Oxf). 204 (2): 267–76. doi:10.1111/j.1748-1716.2011.02280.x. PMC 3320662. PMID 21418147.
^ ^a ^b ^c ^d Bogyo, Matthew; Parkkari, Teija; Haavikko, Raisa; Laitinen, Tuomo; Navia-Paldanius, Dina; Rytilahti, Roosa; Vaara, Miia; Lehtonen, Marko; Alakurtti, Sami; Yli-Kauhaluoma, Jari; Nevalainen, Tapio; Savinainen, Juha R.; Laitinen, Jarmo T. (2014). "Discovery of Triterpenoids as Reversible Inhibitors of α/β-hydrolase Domain Containing 12 (ABHD12)". PLoS ONE. 9 (5): e98286. doi:10.1371/journal.pone.0098286. ISSN 1932-6203. PMC 4045134. PMID 24879289.{{cite journal}}: CS1 maint: unflagged free DOI (link)

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000100997 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000032046 – 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.

[ScholarlyEditions2012-5] Cannabinoid Receptors—Advances in Research and Application: 2012 Edition: ScholarlyBrief. ScholarlyEditions. 26 December 2012. pp. 68–. ISBN 978-1-4816-0672-1.

[pmid21418147-6] 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 Physiol (Oxf). 204 (2): 267–76. doi:10.1111/j.1748-1716.2011.02280.x. PMC 3320662. PMID 21418147.

[BogyoParkkari2014-7] Bogyo, Matthew; Parkkari, Teija; Haavikko, Raisa; Laitinen, Tuomo; Navia-Paldanius, Dina; Rytilahti, Roosa; Vaara, Miia; Lehtonen, Marko; Alakurtti, Sami; Yli-Kauhaluoma, Jari; Nevalainen, Tapio; Savinainen, Juha R.; Laitinen, Jarmo T. (2014). "Discovery of Triterpenoids as Reversible Inhibitors of α/β-hydrolase Domain Containing 12 (ABHD12)". PLoS ONE. 9 (5): e98286. doi:10.1371/journal.pone.0098286. ISSN 1932-6203. PMC 4045134. PMID 24879289.{{cite journal}}: CS1 maint: unflagged free DOI (link)

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Inhibitors

See also

References