ABHD6_MOUSE
ID ABHD6_MOUSE Reviewed; 336 AA.
AC Q8R2Y0; Q3TGD2; Q9DCD4;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Monoacylglycerol lipase ABHD6 {ECO:0000305};
DE EC=3.1.1.23 {ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:24095738};
DE AltName: Full=2-arachidonoylglycerol hydrolase {ECO:0000303|PubMed:18096503};
DE AltName: Full=Abhydrolase domain-containing protein 6 {ECO:0000312|MGI:MGI:1913332};
GN Name=Abhd6 {ECO:0000312|MGI:MGI:1913332};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Amnion, Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18096503; DOI=10.1016/j.chembiol.2007.11.006;
RA Blankman J.L., Simon G.M., Cravatt B.F.;
RT "A comprehensive profile of brain enzymes that hydrolyze the
RT endocannabinoid 2-arachidonoylglycerol.";
RL Chem. Biol. 14:1347-1356(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20657592; DOI=10.1038/nn.2601;
RA Marrs W.R., Blankman J.L., Horne E.A., Thomazeau A., Lin Y.H., Coy J.,
RA Bodor A.L., Muccioli G.G., Hu S.S., Woodruff G., Fung S., Lafourcade M.,
RA Alexander J.P., Long J.Z., Li W., Xu C., Moller T., Mackie K.,
RA Manzoni O.J., Cravatt B.F., Stella N.;
RT "The serine hydrolase ABHD6 controls the accumulation and efficacy of 2-AG
RT at cannabinoid receptors.";
RL Nat. Neurosci. 13:951-957(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP SER-148, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=24095738; DOI=10.1016/j.celrep.2013.08.047;
RA Thomas G., Betters J.L., Lord C.C., Brown A.L., Marshall S., Ferguson D.,
RA Sawyer J., Davis M.A., Melchior J.T., Blume L.C., Howlett A.C.,
RA Ivanova P.T., Milne S.B., Myers D.S., Mrak I., Leber V., Heier C.,
RA Taschler U., Blankman J.L., Cravatt B.F., Lee R.G., Crooke R.M.,
RA Graham M.J., Zimmermann R., Brown H.A., Brown J.M.;
RT "The serine hydrolase ABHD6 is a critical regulator of the metabolic
RT syndrome.";
RL Cell Rep. 5:508-520(2013).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26491015; DOI=10.1074/jbc.m115.669168;
RA Pribasnig M.A., Mrak I., Grabner G.F., Taschler U., Knittelfelder O.,
RA Scherz B., Eichmann T.O., Heier C., Grumet L., Kowaliuk J., Romauch M.,
RA Holler S., Anderl F., Wolinski H., Lass A., Breinbauer R., Marsche G.,
RA Brown J.M., Zimmermann R.;
RT "alpha/beta hydrolase domain-containing 6 (ABHD6) degrades the late
RT endosomal/lysosomal lipid bis(monoacylglycero)phosphate.";
RL J. Biol. Chem. 290:29869-29881(2015).
CC -!- FUNCTION: Lipase that preferentially hydrolysis medium-chain saturated
CC monoacylglycerols including 2-arachidonoylglycerol (PubMed:18096503,
CC PubMed:20657592). Through 2-arachidonoylglycerol degradation may
CC regulate endocannabinoid signaling pathways (PubMed:18096503,
CC PubMed:20657592). Also has a lysophosphatidyl lipase activity with a
CC preference for lysophosphatidylglycerol among other lysophospholipids
CC (PubMed:24095738). Also able to degrade bis(monoacylglycero)phosphate
CC (BMP) and constitutes the major enzyme for BMP catabolism
CC (PubMed:26491015). BMP, also known as lysobisphosphatidic acid, is
CC enriched in late endosomes and lysosomes and plays a key role in the
CC formation of intraluminal vesicles and in lipid sorting
CC (PubMed:26491015). {ECO:0000269|PubMed:18096503,
CC ECO:0000269|PubMed:20657592, ECO:0000269|PubMed:24095738,
CC ECO:0000269|PubMed:26491015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000269|PubMed:18096503,
CC ECO:0000269|PubMed:24095738};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000269|PubMed:18096503};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC Evidence={ECO:0000269|PubMed:18096503};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octanoylglycerol + H2O = glycerol + H(+) + octanoate;
CC Xref=Rhea:RHEA:44328, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:25646, ChEBI:CHEBI:85241;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-decanoylglycerol + H2O = decanoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:27689, ChEBI:CHEBI:75547;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:18262, ChEBI:CHEBI:75539;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:75562; Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:75455; Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:26491015};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000269|PubMed:26491015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:44732,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75457;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:44728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:75612;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z,12Z-octadecadienoyl)-glycerol + H2O = (9Z,12Z)-
CC octadecadienoate + glycerol + H(+); Xref=Rhea:RHEA:48428,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75568;
CC Evidence={ECO:0000250|UniProtKB:Q9BV23};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S,S)-3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-
CC octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-3-
CC (9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+);
CC Xref=Rhea:RHEA:55712, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:139150, ChEBI:CHEBI:139152;
CC Evidence={ECO:0000269|PubMed:26491015};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55713;
CC Evidence={ECO:0000269|PubMed:26491015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S,S)-2-(9Z-octadecenoyl)-sn-glycero-1-phospho-(2'-(9Z-
CC octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + (S,S)-2-
CC (9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) + H(+);
CC Xref=Rhea:RHEA:55716, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:139156, ChEBI:CHEBI:139157;
CC Evidence={ECO:0000269|PubMed:26491015};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55717;
CC Evidence={ECO:0000269|PubMed:26491015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(2'-(9Z-
CC octadecenoyl)-3'-sn-glycerol) + H2O = (9Z)-octadecenoate + (R,R)-2-
CC (9Z-octadecenoyl)-sn-glycero-3-phospho-(3'-sn-glycerol) + H(+);
CC Xref=Rhea:RHEA:55804, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:139228, ChEBI:CHEBI:139230;
CC Evidence={ECO:0000269|PubMed:26491015};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55805;
CC Evidence={ECO:0000269|PubMed:26491015};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 uM for 1(3)-monoolein {ECO:0000269|PubMed:24095738};
CC KM=0.75 uM for 1-oleoyl lysophosphatidylglycerol (in presence of 5M
CC CHAPS) {ECO:0000269|PubMed:24095738};
CC KM=0.98 mM for (R,R)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(2'-
CC (9Z-octadecenoyl)-3'-sn-glycerol) {ECO:0000269|PubMed:26491015};
CC KM=0.9 mM for racemic monoolein {ECO:0000269|PubMed:26491015};
CC KM=1.1 mM for lysophosphatidylglycerol {ECO:0000269|PubMed:26491015};
CC Vmax=478.6 umol/h/mg enzyme toward 1(3)-monoolein
CC {ECO:0000269|PubMed:24095738};
CC Vmax=93.2 umol/h/mg enzyme toward 1-oleoyl lysophosphatidylglycerol
CC {ECO:0000269|PubMed:24095738};
CC Vmax=89 umol/h/mg enzyme toward lysophosphatidylglycerol
CC {ECO:0000269|PubMed:26491015};
CC Vmax=348 umol/h/mg enzyme toward (R,R)-2-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho-(2'-(9Z-octadecenoyl)-3'-sn-glycerol)
CC {ECO:0000269|PubMed:26491015};
CC Vmax=806 umol/h/mg enzyme toward 1-(9Z-octadecenoyl)-glycerol
CC {ECO:0000269|PubMed:26491015};
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:26491015};
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:26491015}; Single-pass type II membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:26491015}; Single-
CC pass type II membrane protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000269|PubMed:20657592}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R2Y0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R2Y0-2; Sequence=VSP_024012;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in small
CC intestine, liver and brown adipose tissue (PubMed:24095738). In brain,
CC expressed postsynaptically in cortical neurons but not detected in
CC microglia (at protein level) (PubMed:20657592).
CC {ECO:0000269|PubMed:20657592, ECO:0000269|PubMed:24095738}.
CC -!- INDUCTION: Up-regulated in small intestine and liver by high-fat diet.
CC {ECO:0000269|PubMed:24095738}.
CC -!- DISRUPTION PHENOTYPE: Abhd6 partial knockdown inducing a stronger
CC depletion in liver, kidney and white adipose tissues protects mice
CC against hight-fat diet-induced metabolic disorder and obesity. De novo
CC lipogenesis in liver is reduced and associated with a reduced
CC expression of lipogenic genes. Accumulation of phospholipids and
CC lysophospholipds in the liver is also observed.
CC {ECO:0000269|PubMed:24095738}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE40616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE40616.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK002883; BAB22430.1; -; mRNA.
DR EMBL; AK076105; BAC36186.1; -; mRNA.
DR EMBL; AK090076; BAC41081.1; -; mRNA.
DR EMBL; AK168782; BAE40616.1; ALT_INIT; mRNA.
DR EMBL; BC027011; AAH27011.1; -; mRNA.
DR CCDS; CCDS26808.1; -. [Q8R2Y0-1]
DR CCDS; CCDS88563.1; -. [Q8R2Y0-2]
DR RefSeq; NP_001317993.1; NM_001331064.1. [Q8R2Y0-1]
DR RefSeq; NP_001317994.1; NM_001331065.1. [Q8R2Y0-2]
DR RefSeq; NP_079617.2; NM_025341.4. [Q8R2Y0-1]
DR RefSeq; XP_006518136.1; XM_006518073.2. [Q8R2Y0-1]
DR AlphaFoldDB; Q8R2Y0; -.
DR SMR; Q8R2Y0; -.
DR STRING; 10090.ENSMUSP00000129169; -.
DR BindingDB; Q8R2Y0; -.
DR ChEMBL; CHEMBL5010; -.
DR GuidetoPHARMACOLOGY; 2919; -.
DR SwissLipids; SLP:000001860; -.
DR ESTHER; mouse-ABHD6; ABHD6-Lip.
DR MEROPS; S33.977; -.
DR iPTMnet; Q8R2Y0; -.
DR PhosphoSitePlus; Q8R2Y0; -.
DR SwissPalm; Q8R2Y0; -.
DR EPD; Q8R2Y0; -.
DR jPOST; Q8R2Y0; -.
DR MaxQB; Q8R2Y0; -.
DR PaxDb; Q8R2Y0; -.
DR PeptideAtlas; Q8R2Y0; -.
DR PRIDE; Q8R2Y0; -.
DR ProteomicsDB; 285827; -. [Q8R2Y0-1]
DR ProteomicsDB; 285828; -. [Q8R2Y0-2]
DR Antibodypedia; 2562; 127 antibodies from 27 providers.
DR DNASU; 66082; -.
DR Ensembl; ENSMUST00000166497; ENSMUSP00000129169; ENSMUSG00000025277. [Q8R2Y0-1]
DR Ensembl; ENSMUST00000225234; ENSMUSP00000153068; ENSMUSG00000025277. [Q8R2Y0-2]
DR GeneID; 66082; -.
DR KEGG; mmu:66082; -.
DR UCSC; uc007sen.1; mouse. [Q8R2Y0-1]
DR CTD; 57406; -.
DR MGI; MGI:1913332; Abhd6.
DR VEuPathDB; HostDB:ENSMUSG00000025277; -.
DR eggNOG; KOG1454; Eukaryota.
DR GeneTree; ENSGT00510000047225; -.
DR HOGENOM; CLU_020336_13_9_1; -.
DR InParanoid; Q8R2Y0; -.
DR OMA; VYILENC; -.
DR OrthoDB; 1285824at2759; -.
DR PhylomeDB; Q8R2Y0; -.
DR TreeFam; TF331946; -.
DR Reactome; R-MMU-426048; Arachidonate production from DAG.
DR BioGRID-ORCS; 66082; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Abhd6; mouse.
DR PRO; PR:Q8R2Y0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8R2Y0; protein.
DR Bgee; ENSMUSG00000025277; Expressed in placenta labyrinth and 233 other tissues.
DR ExpressionAtlas; Q8R2Y0; baseline and differential.
DR Genevisible; Q8R2Y0; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IDA:UniProtKB.
DR GO; GO:0046464; P:acylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0060292; P:long-term synaptic depression; IMP:MGI.
DR GO; GO:2001311; P:lysobisphosphatidic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:2000124; P:regulation of endocannabinoid signaling pathway; IMP:MGI.
DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; EXP:SynGO.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endosome; Hydrolase; Lipid metabolism; Lysosome;
KW Membrane; Mitochondrion; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..336
FT /note="Monoacylglycerol lipase ABHD6"
FT /id="PRO_0000281576"
FT TOPO_DOM 1..8
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 148
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:24095738"
FT ACT_SITE 278
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q99685"
FT ACT_SITE 306
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q99685"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024012"
FT MUTAGEN 148
FT /note="S->A: Loss of the lipid hydrolase activity."
FT /evidence="ECO:0000269|PubMed:24095738"
FT CONFLICT 85
FT /note="D -> G (in Ref. 1; BAB22430)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="P -> A (in Ref. 1; BAB22430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 38205 MW; 4C207C66DBE41FE4 CRC64;
MDLDVVNMFV IAGGTLAIPI LAFVASFLLW PSALIRIYYW YWRRTLGMQV RYAHHEDYQF
CYSFRGRPGH KPSILMLHGF SAHKDMWLSV VKFLPKNLHL VCVDMPGHEG TTRSSLDDLS
IVGQVKRIHQ FVECLKLNKK PFHLIGTSMG GHVAGVYAAY YPSDVCSLSL VCPAGLQYST
DNPFVQRLKE LEESAAIQKI PLIPSTPEEM SEMLQLCSYV RFKVPQQILQ GLVDVRIPHN
SFYRKLFLEI VNEKSRYSLH ENMDKIKVPT QIIWGKQDQV LDVSGADILA KSISNSQVEV
LENCGHSVVM ERPRKTAKLI VDFLASVHNT DNKKLN
