ABHD3_MOUSE
ID ABHD3_MOUSE Reviewed; 411 AA.
AC Q91ZH7; Q3UNF7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Phospholipase ABHD3 {ECO:0000305};
DE EC=3.1.1.32 {ECO:0000269|PubMed:21926997};
DE EC=3.1.1.4 {ECO:0000269|PubMed:21926997};
DE AltName: Full=Abhydrolase domain-containing protein 3 {ECO:0000312|MGI:MGI:2147183};
DE AltName: Full=Lung alpha/beta hydrolase 3 {ECO:0000303|PubMed:11922611};
DE Short=MmLABH3 {ECO:0000303|PubMed:11922611};
GN Name=Abhd3 {ECO:0000312|MGI:MGI:2147183};
GN Synonyms=Labh3 {ECO:0000303|PubMed:11922611};
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=11922611; DOI=10.1006/bbrc.2002.6692;
RA Edgar A.J., Polak J.M.;
RT "Cloning and tissue distribution of three murine alpha/beta hydrolase fold
RT protein cDNAs.";
RL Biochem. Biophys. Res. Commun. 292:617-625(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Liver;
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, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP SER-220.
RX PubMed=21926997; DOI=10.1038/nchembio.659;
RA Long J.Z., Cisar J.S., Milliken D., Niessen S., Wang C., Trauger S.A.,
RA Siuzdak G., Cravatt B.F.;
RT "Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain
RT phospholipids.";
RL Nat. Chem. Biol. 7:763-765(2011).
CC -!- FUNCTION: Phospholipase that may play a role in phospholipids
CC remodeling. May selectively cleave myristate (C14)-containing
CC phosphatidylcholines through its predominant phospholipase 1 activity,
CC cleaving preferentially acyl groups in sn1 position. In parallel, may
CC have a minor phospholipase 2 activity acting on acyl groups in position
CC sn2. In addition to (C14)-containing phosphatidylcholines, may also act
CC on other medium-chain-containing and oxidatively truncated
CC phospholipids. {ECO:0000269|PubMed:21926997}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H(+) + tetradecanoate; Xref=Rhea:RHEA:54388,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:76084, ChEBI:CHEBI:86094;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54389;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-tetradecanoyl-
CC sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:54392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:64489, ChEBI:CHEBI:86094;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54393;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:76079, ChEBI:CHEBI:86102;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54397;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphocholine + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:76085, ChEBI:CHEBI:86162;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54401;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 2-
CC tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:131738;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54405;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC octadecanoyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:54408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:73858, ChEBI:CHEBI:75220;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54409;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-ditetradecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC tetradecanoyl-sn-glycero-3-phosphocholine + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:54456, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:45240, ChEBI:CHEBI:64489;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54457;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-pentanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + pentanoate;
CC Xref=Rhea:RHEA:54460, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31011, ChEBI:CHEBI:73858, ChEBI:CHEBI:138211;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54461;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-hexanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexanoate;
CC Xref=Rhea:RHEA:54464, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:73858, ChEBI:CHEBI:138212;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54465;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-octanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + octanoate;
CC Xref=Rhea:RHEA:54468, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25646, ChEBI:CHEBI:73858, ChEBI:CHEBI:138213;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54469;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-nonanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+) + nonanoate;
CC Xref=Rhea:RHEA:54472, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32361, ChEBI:CHEBI:73858, ChEBI:CHEBI:138214;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54473;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O =
CC 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+) + nonanedioate;
CC Xref=Rhea:RHEA:54552, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64496, ChEBI:CHEBI:78208, ChEBI:CHEBI:138269;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54553;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine + H2O =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + nonanedioate;
CC Xref=Rhea:RHEA:41388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:78207, ChEBI:CHEBI:78208;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41389;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine +
CC H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 9-oxononanoate +
CC H(+); Xref=Rhea:RHEA:41179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:61042, ChEBI:CHEBI:72998, ChEBI:CHEBI:77812;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41180;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine
CC + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 5-oxopentanoate
CC + H(+); Xref=Rhea:RHEA:40483, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16120, ChEBI:CHEBI:72998, ChEBI:CHEBI:77890;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40484;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + glutarate + H(+);
CC Xref=Rhea:RHEA:41159, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30921, ChEBI:CHEBI:72998, ChEBI:CHEBI:77756;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41160;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000269|PubMed:21926997};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000305|PubMed:21926997};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91ZH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91ZH7-2; Sequence=VSP_023564;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in liver.
CC {ECO:0000269|PubMed:11922611}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos from 7 dpc to 17 dpc.
CC {ECO:0000269|PubMed:11922611}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Abhd3 are viable, fertile and have
CC normal behavior. {ECO:0000269|PubMed:21926997}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 4
CC family. {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; AF429302; AAL27565.1; -; mRNA.
DR EMBL; AK134676; BAE22236.1; -; mRNA.
DR EMBL; AK144238; BAE25790.1; -; mRNA.
DR EMBL; BC026770; AAH26770.1; -; mRNA.
DR CCDS; CCDS29057.1; -. [Q91ZH7-1]
DR RefSeq; NP_598891.1; NM_134130.1. [Q91ZH7-1]
DR AlphaFoldDB; Q91ZH7; -.
DR STRING; 10090.ENSMUSP00000002549; -.
DR SwissLipids; SLP:000001752; -.
DR ESTHER; mouse-abhd3; abh_upf0017.
DR iPTMnet; Q91ZH7; -.
DR PhosphoSitePlus; Q91ZH7; -.
DR SwissPalm; Q91ZH7; -.
DR jPOST; Q91ZH7; -.
DR MaxQB; Q91ZH7; -.
DR PaxDb; Q91ZH7; -.
DR PRIDE; Q91ZH7; -.
DR ProteomicsDB; 296435; -. [Q91ZH7-1]
DR ProteomicsDB; 296436; -. [Q91ZH7-2]
DR Antibodypedia; 2532; 127 antibodies from 24 providers.
DR DNASU; 106861; -.
DR Ensembl; ENSMUST00000117726; ENSMUSP00000112768; ENSMUSG00000002475. [Q91ZH7-2]
DR Ensembl; ENSMUST00000117828; ENSMUSP00000113137; ENSMUSG00000002475. [Q91ZH7-1]
DR GeneID; 106861; -.
DR KEGG; mmu:106861; -.
DR UCSC; uc008eba.1; mouse. [Q91ZH7-1]
DR CTD; 171586; -.
DR MGI; MGI:2147183; Abhd3.
DR VEuPathDB; HostDB:ENSMUSG00000002475; -.
DR eggNOG; KOG1838; Eukaryota.
DR GeneTree; ENSGT00950000182902; -.
DR InParanoid; Q91ZH7; -.
DR OMA; RNDPFVP; -.
DR OrthoDB; 1162019at2759; -.
DR PhylomeDB; Q91ZH7; -.
DR TreeFam; TF313195; -.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR BioGRID-ORCS; 106861; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Abhd3; mouse.
DR PRO; PR:Q91ZH7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91ZH7; protein.
DR Bgee; ENSMUSG00000002475; Expressed in cerebellar nuclear complex and 216 other tissues.
DR ExpressionAtlas; Q91ZH7; baseline and differential.
DR Genevisible; Q91ZH7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008126; F:acetylesterase activity; IBA:GO_Central.
DR GO; GO:0047372; F:acylglycerol lipase activity; IBA:GO_Central.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; ISS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000952; AB_hydrolase_4_CS.
DR InterPro; IPR012020; ABHD4.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01133; UPF0017; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Lipid metabolism; Membrane;
KW Phospholipid metabolism; Reference proteome; Serine esterase;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..411
FT /note="Phospholipase ABHD3"
FT /id="PRO_0000280209"
FT TRANSMEM 25..45
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 140..233
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 375
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT VAR_SEQ 353..356
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023564"
FT MUTAGEN 220
FT /note="S->A: Loss of phospholipase activity."
FT /evidence="ECO:0000269|PubMed:21926997"
FT CONFLICT 88
FT /note="E -> A (in Ref. 2; BAE25790)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="Y -> H (in Ref. 2; BAE25790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46232 MW; A9B89D164214CC24 CRC64;
MQRLAMDLRV LSRELALYLE HQVRVGFFGS GVGLSLILGF SVAYACYYLS SIAKKPQLVI
GGESFSRFLQ DHCPVVTETY YPTVWCWESR GQTLLRPFIT SKPPVQYRNE LIKTADGGQI
SLDWFDNNNS AYYVDASTRP TILLLPGLTG TSKESYILHM IHLSEELGYR CVVFNNRGVA
GESLLTPRTY CCANTEDLEA VVHHVHSLYP GAPFLAAGVS MGGMLLLNYL GKIGSKTPLM
AAATFSVGWN TFACSESLER PLNWLLFNYY LTTCLQSSVK KHRHMFVEQI DMDQVMKAKS
IREFDKRFTA VMFGYRTLDD YYTDASPNRR LKSVGIPVLC LNATDDVFSP SHAIPIETAK
QNPNVALVLT AYGGHIGFLE GIWPRQCTYM DRVFKQFVQA MVEHGHELSN M
