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   24-JAN-2024, entry version 161.
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=3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-
CC         octadecenoyl)-1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 3-(9Z-
CC         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}.
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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; 31.
DR   IntAct; Q9BV23; 11.
DR   STRING; 9606.ENSP00000295962; -.
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   SwissPalm; Q9BV23; -.
DR   BioMuta; ABHD6; -.
DR   DMDM; 74733280; -.
DR   EPD; Q9BV23; -.
DR   jPOST; Q9BV23; -.
DR   MassIVE; Q9BV23; -.
DR   MaxQB; Q9BV23; -.
DR   PaxDb; 9606-ENSP00000420315; -.
DR   PeptideAtlas; Q9BV23; -.
DR   ProteomicsDB; 79154; -.
DR   Pumba; Q9BV23; -.
DR   Antibodypedia; 2562; 139 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   AGR; HGNC:21398; -.
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; NAMWQYS; -.
DR   OrthoDB; 45773at2759; -.
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; 16 hits in 1158 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 178 other cell types or tissues.
DR   ExpressionAtlas; Q9BV23; baseline and differential.
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:0031902; C:late endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C: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:0045211; C:postsynaptic membrane; IEA:Ensembl.
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   GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; IEA:Ensembl.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR   PANTHER; PTHR43798:SF5; MONOACYLGLYCEROL LIPASE ABHD6; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   Genevisible; Q9BV23; HS.
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
//