ABD12_MOUSE
ID ABD12_MOUSE Reviewed; 398 AA.
AC Q99LR1; A2ANB4; Q99M06;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Lysophosphatidylserine lipase ABHD12 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:23297193};
DE AltName: Full=2-arachidonoylglycerol hydrolase ABHD12 {ECO:0000305};
DE AltName: Full=Abhydrolase domain-containing protein 12 {ECO:0000305};
DE AltName: Full=Monoacylglycerol lipase ABHD12 {ECO:0000305};
DE EC=3.1.1.23 {ECO:0000269|PubMed:18096503};
DE AltName: Full=Oxidized phosphatidylserine lipase ABHD12 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000269|PubMed:30643283};
GN Name=Abhd12 {ECO:0000303|PubMed:23297193, ECO:0000312|MGI:MGI:1923442};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC 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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP GLYCOSYLATION.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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 [6]
RP SUBCELLULAR LOCATION.
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23297193; DOI=10.1073/pnas.1217121110;
RA Blankman J.L., Long J.Z., Trauger S.A., Siuzdak G., Cravatt B.F.;
RT "ABHD12 controls brain lysophosphatidylserine pathways that are deregulated
RT in a murine model of the neurodegenerative disease PHARC.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1500-1505(2013).
RN [8]
RP FUNCTION.
RX PubMed=25580854; DOI=10.1038/nchembio.1721;
RA Kamat S.S., Camara K., Parsons W.H., Chen D.H., Dix M.M., Bird T.D.,
RA Howell A.R., Cravatt B.F.;
RT "Immunomodulatory lysophosphatidylserines are regulated by ABHD16A and
RT ABHD12 interplay.";
RL Nat. Chem. Biol. 11:164-171(2015).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=30237167; DOI=10.1074/jbc.ra118.005640;
RA Joshi A., Shaikh M., Singh S., Rajendran A., Mhetre A., Kamat S.S.;
RT "Biochemical characterization of the PHARC-associated serine hydrolase
RT ABHD12 reveals its preference for very-long-chain lipids.";
RL J. Biol. Chem. 293:16953-16963(2018).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=30420694; DOI=10.1038/s41589-018-0155-8;
RA Ogasawara D., Ichu T.A., Vartabedian V.F., Benthuysen J., Jing H., Reed A.,
RA Ulanovskaya O.A., Hulce J.J., Roberts A., Brown S., Rosen H., Teijaro J.R.,
RA Cravatt B.F.;
RT "Selective blockade of the lyso-PS lipase ABHD12 stimulates immune
RT responses in vivo.";
RL Nat. Chem. Biol. 14:1099-1108(2018).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30643283; DOI=10.1038/s41589-018-0195-0;
RA Kelkar D.S., Ravikumar G., Mehendale N., Singh S., Joshi A., Sharma A.K.,
RA Mhetre A., Rajendran A., Chakrapani H., Kamat S.S.;
RT "A chemical-genetic screen identifies ABHD12 as an oxidized-
RT phosphatidylserine lipase.";
RL Nat. Chem. Biol. 15:169-178(2019).
CC -!- FUNCTION: Lysophosphatidylserine (LPS) lipase that mediates the
CC hydrolysis of lysophosphatidylserine, a class of signaling lipids that
CC regulates immunological and neurological processes (PubMed:23297193,
CC PubMed:25580854, PubMed:30420694). Represents a major
CC lysophosphatidylserine lipase in the brain, thereby playing a key role
CC in the central nervous system (PubMed:23297193). Also able to hydrolyze
CC oxidized phosphatidylserine; oxidized phosphatidylserine is produced in
CC response to severe inflammatory stress and constitutes a proapoptotic
CC 'eat me' signal (PubMed:30643283). Also has monoacylglycerol (MAG)
CC lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby
CC acting as a regulator of endocannabinoid signaling pathways
CC (PubMed:18096503). Has a strong preference for very-long-chain lipid
CC substrates; substrate specificity is likely due to improved catalysis
CC and not improved substrate binding (PubMed:30237167).
CC {ECO:0000269|PubMed:18096503, ECO:0000269|PubMed:23297193,
CC ECO:0000269|PubMed:25580854, ECO:0000269|PubMed:30237167,
CC ECO:0000269|PubMed:30420694, ECO:0000269|PubMed:30643283}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000269|PubMed:23297193};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000269|PubMed:23297193};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-(1'-sn-
CC glycerol); Xref=Rhea:RHEA:44584, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64717,
CC ChEBI:CHEBI:72828; Evidence={ECO:0000269|PubMed:23297193};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44585;
CC Evidence={ECO:0000269|PubMed:23297193};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) +
CC H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-1D-myo-
CC inositol; Xref=Rhea:RHEA:44588, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:58444, ChEBI:CHEBI:78762;
CC Evidence={ECO:0000269|PubMed:23297193};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44589;
CC Evidence={ECO:0000269|PubMed:23297193};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:40895, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74971, ChEBI:CHEBI:143890;
CC Evidence={ECO:0000269|PubMed:23297193};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40896;
CC Evidence={ECO:0000269|PubMed:23297193};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:41091, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:75757, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000269|PubMed:23297193};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41092;
CC Evidence={ECO:0000269|PubMed:23297193};
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:23297193};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC Evidence={ECO:0000269|PubMed:23297193};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H2O = H(+) +
CC hexadecanoate + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:44552,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64765, ChEBI:CHEBI:75020;
CC Evidence={ECO:0000269|PubMed:23297193};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44553;
CC Evidence={ECO:0000269|PubMed:23297193};
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=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000269|PubMed:18096503};
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:Q8N2K0};
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:Q8N2K0};
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:Q8N2K0};
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:Q8N2K0};
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:30237167};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000269|PubMed:30237167};
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:Q8N2K0};
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:30237167};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44729;
CC Evidence={ECO:0000269|PubMed:30237167};
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:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:69081; Evidence={ECO:0000269|PubMed:30237167};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960;
CC Evidence={ECO:0000269|PubMed:30237167};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoylglycerol + H2O = glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:38363, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:75555; Evidence={ECO:0000269|PubMed:30237167};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38364;
CC Evidence={ECO:0000269|PubMed:30237167};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9,10-epoxyoctadecanoyl)-sn-glycero-3-
CC phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine +
CC 9,10-epoxyoctadecanoate + H(+); Xref=Rhea:RHEA:59364,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467,
CC ChEBI:CHEBI:85195, ChEBI:CHEBI:143087;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3-
CC phospho-L-serine + H2O = 1-octadecanoyl-sn-glycero-3-phosphoserine +
CC 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59368,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84467,
CC ChEBI:CHEBI:143088, ChEBI:CHEBI:143089;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(10-hydroxyoctadecanoyl)-sn-glycero-3-
CC phospho-L-serine + H2O = 1-hexadecanoyl-sn-glycero-3-phospho-L-serine
CC + 10-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:59372,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:143089, ChEBI:CHEBI:143094;
CC Evidence={ECO:0000250|UniProtKB:Q8N2K0};
CC -!- ACTIVITY REGULATION: Selectively inhibited by DO264 (N-3-pyridyl-N'-(1-
CC [3-chloro-4-{2-chloro-4-(trifluoromethoxy)phenoxy}pyridine-2-
CC yl]piperidin-4-yl)thiourea). {ECO:0000269|PubMed:30420694}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:30237167}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:20657592}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99LR1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99LR1-2; Sequence=VSP_057493;
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:18096503}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and were born at the expected
CC Mendelian frequency (PubMed:23297193). Young mice (less than 6 months
CC old) are mostly normal in their behavior; however, as these animals
CC age, they develop an array of phenotypes, including defective auditory
CC and motor behavior, with concomitant cellular pathology indicative of a
CC neuroinflammatory response (PubMed:23297193). Mice show heightened
CC immunological responses (PubMed:30420694). Metabolomic characterization
CC of brain tissue show striking elevations in a series of
CC lysophosphatidylserine (LPS) lipids that occur before the onset of
CC neuroinflammatory and behavioral defects (PubMed:23297193). Brain
CC tissues accumulate oxidized phosphatidylserine lipids in response to
CC severe inflammatory stress (PubMed:30643283).
CC {ECO:0000269|PubMed:23297193, ECO:0000269|PubMed:30420694,
CC ECO:0000269|PubMed:30643283}.
CC -!- SIMILARITY: Belongs to the serine esterase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02138.1; 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; AL808125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28584.1; -; Genomic_DNA.
DR EMBL; BC002138; AAH02138.1; ALT_INIT; mRNA.
DR EMBL; BC002263; AAH02263.1; -; mRNA.
DR CCDS; CCDS50742.1; -. [Q99LR1-1]
DR RefSeq; NP_077785.2; NM_024465.3. [Q99LR1-1]
DR AlphaFoldDB; Q99LR1; -.
DR SMR; Q99LR1; -.
DR BioGRID; 218015; 1.
DR IntAct; Q99LR1; 1.
DR STRING; 10090.ENSMUSP00000053558; -.
DR BindingDB; Q99LR1; -.
DR ChEMBL; CHEMBL5972; -.
DR SwissLipids; SLP:000001041; -.
DR ESTHER; mouse-abd12; ABHD12-PHARC.
DR MEROPS; S09.939; -.
DR GlyConnect; 2513; 3 N-Linked glycans (1 site).
DR GlyGen; Q99LR1; 1 site, 3 N-linked glycans (1 site).
DR iPTMnet; Q99LR1; -.
DR PhosphoSitePlus; Q99LR1; -.
DR SwissPalm; Q99LR1; -.
DR EPD; Q99LR1; -.
DR MaxQB; Q99LR1; -.
DR PaxDb; Q99LR1; -.
DR PeptideAtlas; Q99LR1; -.
DR PRIDE; Q99LR1; -.
DR ProteomicsDB; 285823; -. [Q99LR1-1]
DR ProteomicsDB; 285824; -. [Q99LR1-2]
DR Antibodypedia; 10033; 182 antibodies from 28 providers.
DR DNASU; 76192; -.
DR Ensembl; ENSMUST00000056149; ENSMUSP00000053558; ENSMUSG00000032046. [Q99LR1-1]
DR GeneID; 76192; -.
DR KEGG; mmu:76192; -.
DR UCSC; uc008muo.2; mouse. [Q99LR1-1]
DR CTD; 26090; -.
DR MGI; MGI:1923442; Abhd12.
DR VEuPathDB; HostDB:ENSMUSG00000032046; -.
DR eggNOG; KOG1552; Eukaryota.
DR GeneTree; ENSGT00940000160517; -.
DR HOGENOM; CLU_029375_1_0_1; -.
DR InParanoid; Q99LR1; -.
DR OMA; YELHNCL; -.
DR OrthoDB; 691954at2759; -.
DR PhylomeDB; Q99LR1; -.
DR TreeFam; TF315122; -.
DR Reactome; R-MMU-426048; Arachidonate production from DAG.
DR BioGRID-ORCS; 76192; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Abhd12; mouse.
DR PRO; PR:Q99LR1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99LR1; protein.
DR Bgee; ENSMUSG00000032046; Expressed in urinary bladder urothelium and 246 other tissues.
DR ExpressionAtlas; Q99LR1; baseline and differential.
DR Genevisible; Q99LR1; MM.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; ISO:MGI.
DR GO; GO:0046464; P:acylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; ISO:MGI.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0006660; P:phosphatidylserine catabolic process; IMP:MGI.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:UniProtKB.
DR GO; GO:0002084; P:protein depalmitoylation; IDA:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0010996; P:response to auditory stimulus; IMP:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR026605; ABHD12.
DR InterPro; IPR022742; Hydrolase_4.
DR PANTHER; PTHR12277:SF61; PTHR12277:SF61; 1.
DR Pfam; PF12146; Hydrolase_4; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Lipid metabolism; Membrane; Mitochondrion; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="Lysophosphatidylserine lipase ABHD12"
FT /id="PRO_0000079414"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18096503"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:18096503"
FT TOPO_DOM 96..398
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:18096503"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 246
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 333
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q8N2K0"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..219
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057493"
FT CONFLICT 386
FT /note="R -> W (in Ref. 3; AAH02138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45270 MW; B8B23FA97DB4FF45 CRC64;
MRKRTEPVTL EHERCAASGS SSSGSAAAAL DADCSLKQNL RLAGKGTAEP HSASDAGMKR
ALGRRKSLWF RLRKILLCVL GFYIAIPFLV KLCPGIQAKL IFLNFVRVPY FIDLKKPQDQ
GLNHTCNYYL QPEDDVTIGV WHTIPSVWWK NAQGKDQMWY EDALASNHAI ILYLHGNAGT
RGGDHRVELY KVLSSLGYHV VTFDYRGWGD SVGTPSERGM TYDALHVFDW IKARSGDNPV
YIWGHSLGTG VATNLVRRLC ERETPPDALI LESPFTNIRE EAKSHPFSVI YRYFPGFDWF
FLDPITSSGI KFANDENMKH ISCPLLILHA EDDPVVPFHL GRKLYNIAAP SRSFRDFKVQ
FIPFHSDLGY RHKYIYKSPE LPRILREFLG KSEPERQH
