ABHD6_HUMAN
ID ABHD6_HUMAN Reviewed; 337 AA.
AC Q9BV23; B2R7Y9; Q6ZMF7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Monoacylglycerol lipase ABHD6 {ECO:0000305};
DE EC=3.1.1.23 {ECO:0000269|PubMed:22969151};
DE AltName: Full=2-arachidonoylglycerol hydrolase {ECO:0000250|UniProtKB:Q8R2Y0};
DE AltName: Full=Abhydrolase domain-containing protein 6 {ECO:0000312|HGNC:HGNC:21398};
GN Name=ABHD6 {ECO:0000312|HGNC:HGNC:21398};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum, Hepatoma, and Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
RP SER-148.
RX PubMed=22969151; DOI=10.1194/jlr.m030411;
RA Navia-Paldanius D., Savinainen J.R., Laitinen J.T.;
RT "Biochemical and pharmacological characterization of human alpha/beta-
RT hydrolase domain containing 6 (ABHD6) and 12 (ABHD12).";
RL J. Lipid Res. 53:2413-2424(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 43-337 IN COMPLEX WITH
RP (9Z)-OCTADECENOATE.
RA Nawrotek A., Talagas A., Vuillard L., Miallau L.;
RT "Crystal structure of human monoacylglycerol lipase ABHD6 in complex with
RT oleic acid and octyl glucoside.";
RL Submitted (JUN-2021) to the PDB data bank.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, VARIANTS HIS-113; CYS-148; LEU-204; PRO-206
RP AND VAL-231, AND CHARACTERIZATION OF VARIANTS HIS-113; CYS-148; LEU-204;
RP PRO-206 AND VAL-231.
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:22969151).
CC Through 2-arachidonoylglycerol degradation may regulate endocannabinoid
CC signaling pathways (By similarity). Also has a lysophosphatidyl lipase
CC activity with a preference for lysophosphatidylglycerol among other
CC lysophospholipids (By similarity). Also able to degrade
CC bis(monoacylglycero)phosphate (BMP) and constitutes the major enzyme
CC for BMP catabolism (PubMed:26491015). BMP, also known as
CC lysobisphosphatidic acid, is enriched in late endosomes and lysosomes
CC and plays a key role in the formation of intraluminal vesicles and in
CC lipid sorting (PubMed:26491015). {ECO:0000250|UniProtKB:Q8R2Y0,
CC ECO:0000269|PubMed:22969151, 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:22969151};
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:0000269|PubMed:22969151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44329;
CC Evidence={ECO:0000269|PubMed:22969151};
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:0000269|PubMed:22969151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44321;
CC Evidence={ECO:0000269|PubMed:22969151};
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:0000269|PubMed:22969151};
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:0000269|PubMed:22969151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44313;
CC Evidence={ECO:0000269|PubMed:22969151};
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:0000269|PubMed:22969151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964;
CC Evidence={ECO:0000269|PubMed:22969151};
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:0000269|PubMed:22969151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC Evidence={ECO:0000269|PubMed:22969151};
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:22969151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000269|PubMed:22969151};
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:0000269|PubMed:22969151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44733;
CC Evidence={ECO:0000269|PubMed:22969151};
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:22969151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC Evidence={ECO:0000269|PubMed:22969151};
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:0000269|PubMed:22969151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44729;
CC Evidence={ECO:0000269|PubMed:22969151};
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:0000269|PubMed:22969151};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48429;
CC Evidence={ECO:0000269|PubMed:22969151};
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:0000250|UniProtKB:Q8R2Y0};
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:0000250|UniProtKB:Q8R2Y0};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=159 uM for 2-arachidonoyglycerol {ECO:0000269|PubMed:22969151};
CC Vmax=45 nmol/min/mg enzyme toward 2-arachidonoyglycerol
CC {ECO:0000269|PubMed:22969151};
CC pH dependence:
CC Optimum pH is 7.2-9 with 2-arachidonoyglycerol as substrate.
CC {ECO:0000269|PubMed:22969151};
CC -!- INTERACTION:
CC Q9BV23; Q9Y3D6: FIS1; NbExp=3; IntAct=EBI-3916106, EBI-3385283;
CC Q9BV23; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-3916106, EBI-10244780;
CC Q9BV23; Q969E2: SCAMP4; NbExp=3; IntAct=EBI-3916106, EBI-4403649;
CC Q9BV23; Q9NYZ1: TVP23B; NbExp=3; IntAct=EBI-3916106, EBI-11343401;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8R2Y0};
CC Single-pass type II membrane protein {ECO:0000255}. Mitochondrion
CC membrane {ECO:0000250|UniProtKB:Q8R2Y0}; Single-pass type II membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {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; AK122983; BAG53832.1; -; mRNA.
DR EMBL; AK172797; BAD18771.1; -; mRNA.
DR EMBL; AK313168; BAG35986.1; -; mRNA.
DR EMBL; AC098479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65360.1; -; Genomic_DNA.
DR EMBL; BC001698; AAH01698.1; -; mRNA.
DR CCDS; CCDS2887.1; -.
DR RefSeq; NP_001307055.1; NM_001320126.1.
DR RefSeq; NP_065727.4; NM_020676.6.
DR PDB; 7OTS; X-ray; 1.79 A; A/B=43-337.
DR PDBsum; 7OTS; -.
DR AlphaFoldDB; Q9BV23; -.
DR SMR; Q9BV23; -.
DR BioGRID; 121508; 30.
DR IntAct; Q9BV23; 11.
DR STRING; 9606.ENSP00000420315; -.
DR BindingDB; Q9BV23; -.
DR ChEMBL; CHEMBL2189127; -.
DR DrugCentral; Q9BV23; -.
DR GuidetoPHARMACOLOGY; 2919; -.
DR SwissLipids; SLP:000001042; -.
DR ESTHER; human-ABHD6; ABHD6-Lip.
DR MEROPS; S33.997; -.
DR iPTMnet; Q9BV23; -.
DR MetOSite; Q9BV23; -.
DR PhosphoSitePlus; Q9BV23; -.
DR BioMuta; ABHD6; -.
DR DMDM; 74733280; -.
DR EPD; Q9BV23; -.
DR jPOST; Q9BV23; -.
DR MassIVE; Q9BV23; -.
DR MaxQB; Q9BV23; -.
DR PaxDb; Q9BV23; -.
DR PeptideAtlas; Q9BV23; -.
DR PRIDE; Q9BV23; -.
DR ProteomicsDB; 79154; -.
DR Antibodypedia; 2562; 127 antibodies from 27 providers.
DR DNASU; 57406; -.
DR Ensembl; ENST00000295962.8; ENSP00000295962.4; ENSG00000163686.15.
DR Ensembl; ENST00000478253.6; ENSP00000420315.1; ENSG00000163686.15.
DR GeneID; 57406; -.
DR KEGG; hsa:57406; -.
DR MANE-Select; ENST00000478253.6; ENSP00000420315.1; NM_001320126.2; NP_001307055.1.
DR UCSC; uc003djs.4; human.
DR CTD; 57406; -.
DR DisGeNET; 57406; -.
DR GeneCards; ABHD6; -.
DR HGNC; HGNC:21398; ABHD6.
DR HPA; ENSG00000163686; Tissue enhanced (liver).
DR neXtProt; NX_Q9BV23; -.
DR OpenTargets; ENSG00000163686; -.
DR PharmGKB; PA134916787; -.
DR VEuPathDB; HostDB:ENSG00000163686; -.
DR eggNOG; KOG1454; Eukaryota.
DR GeneTree; ENSGT00510000047225; -.
DR InParanoid; Q9BV23; -.
DR OMA; VYILENC; -.
DR OrthoDB; 1285824at2759; -.
DR PhylomeDB; Q9BV23; -.
DR TreeFam; TF331946; -.
DR PathwayCommons; Q9BV23; -.
DR Reactome; R-HSA-426048; Arachidonate production from DAG.
DR SignaLink; Q9BV23; -.
DR BioGRID-ORCS; 57406; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; ABHD6; human.
DR GenomeRNAi; 57406; -.
DR Pharos; Q9BV23; Tchem.
DR PRO; PR:Q9BV23; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BV23; protein.
DR Bgee; ENSG00000163686; Expressed in ileal mucosa and 176 other tissues.
DR ExpressionAtlas; Q9BV23; baseline and differential.
DR Genevisible; Q9BV23; HS.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IEA:Ensembl.
DR GO; GO:0046464; P:acylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; TAS:Reactome.
DR GO; GO:0060292; P:long-term synaptic depression; IEA:Ensembl.
DR GO; GO:2001311; P:lysobisphosphatidic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:Ensembl.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IEA:Ensembl.
DR GO; GO:2000124; P:regulation of endocannabinoid signaling pathway; IEA:Ensembl.
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; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endosome; Hydrolase; Lipid metabolism; Lysosome; Membrane;
KW Mitochondrion; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..337
FT /note="Monoacylglycerol lipase ABHD6"
FT /id="PRO_0000281575"
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..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 72..313
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 148
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q99685,
FT ECO:0000305|PubMed:22969151"
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 BINDING 80
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:7OTS"
FT BINDING 149
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:7OTS"
FT BINDING 306
FT /ligand="(9Z)-octadecenoate"
FT /ligand_id="ChEBI:CHEBI:30823"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PDB:7OTS"
FT VARIANT 113
FT /note="R -> H (decreased bis(monoacylglycero)phosphate
FT (BMP) hydrolase activity; dbSNP:rs200333190)"
FT /evidence="ECO:0000269|PubMed:26491015"
FT /id="VAR_081595"
FT VARIANT 148
FT /note="S -> C (loss of bis(monoacylglycero)phosphate (BMP)
FT hydrolase activity; dbSNP:rs11544004)"
FT /evidence="ECO:0000269|PubMed:26491015"
FT /id="VAR_081596"
FT VARIANT 204
FT /note="P -> L (loss of bis(monoacylglycero)phosphate (BMP)
FT hydrolase activity; dbSNP:rs199678322)"
FT /evidence="ECO:0000269|PubMed:26491015"
FT /id="VAR_081597"
FT VARIANT 206
FT /note="T -> P (loss of lipase activity; dbSNP:rs199696239)"
FT /evidence="ECO:0000269|PubMed:26491015"
FT /id="VAR_081598"
FT VARIANT 231
FT /note="G -> V (decreased bis(monoacylglycero)phosphate
FT (BMP) hydrolase activity; dbSNP:rs745824058)"
FT /evidence="ECO:0000269|PubMed:26491015"
FT /id="VAR_081599"
FT MUTAGEN 148
FT /note="S->A: Loss of 2-arachidonoyglycerol hydrolase
FT activity."
FT /evidence="ECO:0000269|PubMed:22969151"
FT CONFLICT 11
FT /note="I -> T (in Ref. 1; BAD18771)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="L -> P (in Ref. 1; BAD18771)"
FT /evidence="ECO:0000305"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:7OTS"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:7OTS"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:7OTS"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:7OTS"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:7OTS"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:7OTS"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:7OTS"
FT TURN 253..257
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:7OTS"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:7OTS"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 285..292
FT /evidence="ECO:0007829|PDB:7OTS"
FT STRAND 293..303
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:7OTS"
FT HELIX 313..334
FT /evidence="ECO:0007829|PDB:7OTS"
SQ SEQUENCE 337 AA; 38331 MW; D87CEE8316F94910 CRC64;
MDLDVVNMFV IAGGTLAIPI LAFVASFLLW PSALIRIYYW YWRRTLGMQV RYVHHEDYQF
CYSFRGRPGH KPSILMLHGF SAHKDMWLSV VKFLPKNLHL VCVDMPGHEG TTRSSLDDLS
IDGQVKRIHQ FVECLKLNKK PFHLVGTSMG GQVAGVYAAY YPSDVSSLCL VCPAGLQYST
DNQFVQRLKE LQGSAAVEKI PLIPSTPEEM SEMLQLCSYV RFKVPQQILQ GLVDVRIPHN
NFYRKLFLEI VSEKSRYSLH QNMDKIKVPT QIIWGKQDQV LDVSGADMLA KSIANCQVEL
LENCGHSVVM ERPRKTAKLI IDFLASVHNT DNNKKLD
