ABHD5_MOUSE
ID ABHD5_MOUSE Reviewed; 351 AA.
AC Q9DBL9; Q9CTY3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase ABHD5 {ECO:0000305};
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q8WTS1};
DE AltName: Full=Abhydrolase domain-containing protein 5;
DE AltName: Full=Lipid droplet-binding protein CGI-58;
DE Short=Protein CGI-58;
GN Name=Abhd5 {ECO:0000312|MGI:MGI:1914719};
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=Liver;
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; TISSUE=Colon, and Mammary gland;
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 INTERACTION WITH PLIN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15292255; DOI=10.1074/jbc.m407462200;
RA Subramanian V., Rothenberg A., Gomez C., Cohen A.W., Garcia A.,
RA Bhattacharyya S., Shapiro L., Dolios G., Wang R., Lisanti M.P.,
RA Brasaemle D.L.;
RT "Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in
RT 3T3-L1 adipocytes.";
RL J. Biol. Chem. 279:42062-42071(2004).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH PLIN AND PNPLA2.
RX PubMed=16679289; DOI=10.1016/j.cmet.2006.03.005;
RA Lass A., Zimmermann R., Haemmerle G., Riederer M., Schoiswohl G.,
RA Schweiger M., Kienesberger P., Strauss J.G., Gorkiewicz G., Zechner R.;
RT "Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is
RT activated by CGI-58 and defective in Chanarin-Dorfman Syndrome.";
RL Cell Metab. 3:309-319(2006).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18832586; DOI=10.2353/ajpath.2008.080005;
RA Akiyama M., Sakai K., Takayama C., Yanagi T., Yamanaka Y., McMillan J.R.,
RA Shimizu H.;
RT "CGI-58 is an alpha/beta-hydrolase within lipid transporting lamellar
RT granules of differentiated keratinocytes.";
RL Am. J. Pathol. 173:1349-1360(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=18606822; DOI=10.1074/jbc.m801783200;
RA Ghosh A.K., Ramakrishnan G., Chandramohan C., Rajasekharan R.;
RT "CGI-58, the causative gene for Chanarin-Dorfman syndrome, mediates
RT acylation of lysophosphatidic acid.";
RL J. Biol. Chem. 283:24525-24533(2008).
RN [7]
RP INTERACTION WITH PLIN5.
RX PubMed=19064991; DOI=10.1074/jbc.m808251200;
RA Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z.;
RT "Functional interactions between Mldp (LSDP5) and Abhd5 in the control of
RT intracellular lipid accumulation.";
RL J. Biol. Chem. 284:3049-3057(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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 [9]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=19801371; DOI=10.1194/jlr.m001917;
RA Montero-Moran G., Caviglia J.M., McMahon D., Rothenberg A., Subramanian V.,
RA Xu Z., Lara-Gonzalez S., Storch J., Carman G.M., Brasaemle D.L.;
RT "CGI-58/ABHD5 is a coenzyme A-dependent lysophosphatidic acid
RT acyltransferase.";
RL J. Lipid Res. 51:709-719(2010).
RN [10]
RP INTERACTION WITH PLIN5.
RX PubMed=21148142; DOI=10.1074/jbc.m110.180711;
RA Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z., Zhou L.;
RT "Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase.";
RL J. Biol. Chem. 286:5126-5135(2011).
RN [11]
RP FUNCTION.
RX PubMed=26083785; DOI=10.1371/journal.pgen.1005284;
RA Xie M., Roy R.;
RT "The causative gene in Chanarian Dorfman syndrome regulates lipid droplet
RT homeostasis in C. elegans.";
RL PLoS Genet. 11:E1005284-E1005284(2015).
RN [12]
RP ERRATUM OF PUBMED:26083785.
RX PubMed=28002418; DOI=10.1371/journal.pgen.1006524;
RA Xie M., Roy R.;
RL PLoS Genet. 12:E1006524-E1006524(2016).
CC -!- FUNCTION: Coenzyme A-dependent lysophosphatidic acid acyltransferase
CC that catalyzes the transfert of an acyl group on a lysophosphatidic
CC acid (PubMed:19801371). Functions preferentially with 1-oleoyl-
CC lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-
CC stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid
CC as lipid acceptor (PubMed:19801371). Functions preferentially with
CC arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors
CC (PubMed:19801371). Functions in phosphatidic acid biosynthesis (By
CC similarity). May regulate the cellular storage of triacylglycerol
CC through activation of the phospholipase PNPLA2 (PubMed:16679289).
CC Involved in keratinocyte differentiation (By similarity). Regulates
CC lipid droplet fusion (PubMed:26083785). {ECO:0000250|UniProtKB:Q8WTS1,
CC ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:19801371,
CC ECO:0000269|PubMed:26083785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000250|UniProtKB:Q8WTS1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000250|UniProtKB:Q8WTS1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000269|PubMed:19801371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:19801371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74551;
CC Evidence={ECO:0000269|PubMed:19801371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000305|PubMed:19801371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA
CC = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74552;
CC Evidence={ECO:0000269|PubMed:19801371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000305|PubMed:19801371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74928; Evidence={ECO:0000269|PubMed:19801371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000305|PubMed:19801371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA =
CC 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37451, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74937;
CC Evidence={ECO:0000269|PubMed:19801371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37452;
CC Evidence={ECO:0000305|PubMed:19801371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000269|PubMed:19801371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000305|PubMed:19801371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate
CC = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37163, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000269|PubMed:19801371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000305|PubMed:19801371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37455,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74938,
CC ChEBI:CHEBI:74941; Evidence={ECO:0000269|PubMed:19801371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456;
CC Evidence={ECO:0000305|PubMed:19801371};
CC -!- ACTIVITY REGULATION: Acyltransferase activity is inhibited by
CC detergents such as Triton X-100 and 3-[(3-
CC cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS).
CC Acyltransferase activity is inhibited by the presence of magnesium and
CC calcium. {ECO:0000269|PubMed:19801371}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.8 uM for oleoyl-CoA {ECO:0000269|PubMed:19801371};
CC KM=18 uM for 1-oleoyl-lysophosphatidic acid
CC {ECO:0000269|PubMed:19801371};
CC Vmax=6.1 nmol/min/mg enzyme toward oleoyl-CoA
CC {ECO:0000269|PubMed:19801371};
CC Vmax=7.6 nmol/min/mg enzyme toward 1-oleoyl-lysophosphatidic acid
CC {ECO:0000269|PubMed:19801371};
CC pH dependence:
CC Optimum pH is 7-8.5. {ECO:0000269|PubMed:19801371};
CC Temperature dependence:
CC Preincubation of the enzyme for 10 min at temperatures above 35
CC degrees Celsius decreases acyltransferase activity subsequently
CC measured at 30 degrees Celsius. Acyltransferase activity is reduced
CC by approximately 60% following 10 min preincubation at47 degrees
CC Celsius. {ECO:0000269|PubMed:19801371};
CC -!- SUBUNIT: Interacts with ADRP (By similarity). Interacts with PLIN.
CC Interacts with and PNPLA2. Interacts with PLIN5; promotes interaction
CC with PNPLA2. {ECO:0000250, ECO:0000269|PubMed:15292255,
CC ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:19064991,
CC ECO:0000269|PubMed:21148142}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Lipid droplet
CC {ECO:0000269|PubMed:18606822}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:18606822}. Note=Colocalized with PLIN and ADRP on
CC the surface of lipid droplets. The localization is dependent upon the
CC metabolic status of the adipocytes and the activity of PKA.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DBL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DBL9-2; Sequence=VSP_015345;
CC -!- TISSUE SPECIFICITY: Highly expressed in the adipose tissue and testes.
CC Weakly expressed in the liver, muscle, kidney, and heart. Expressed by
CC upper epidermal layers and dermal fibroblasts in skin, hepatocytes and
CC hypothalamus in brain (at protein level). {ECO:0000269|PubMed:15292255,
CC ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:18832586}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK004873; BAB23632.1; -; mRNA.
DR EMBL; AK019488; BAB31755.2; -; mRNA.
DR EMBL; AK050377; BAC34220.1; -; mRNA.
DR EMBL; BC037063; AAH37063.1; -; mRNA.
DR CCDS; CCDS23646.1; -. [Q9DBL9-1]
DR CCDS; CCDS90688.1; -. [Q9DBL9-2]
DR RefSeq; NP_080455.1; NM_026179.2. [Q9DBL9-1]
DR RefSeq; XP_006512308.1; XM_006512245.3.
DR PDB; 5A4H; NMR; -; A=10-43.
DR PDBsum; 5A4H; -.
DR AlphaFoldDB; Q9DBL9; -.
DR SMR; Q9DBL9; -.
DR BioGRID; 212211; 4.
DR DIP; DIP-61642N; -.
DR IntAct; Q9DBL9; 1.
DR STRING; 10090.ENSMUSP00000122274; -.
DR ChEMBL; CHEMBL3259509; -.
DR SwissLipids; SLP:000000283; -.
DR ESTHER; mouse-abhd5; CGI-58_ABHD5_ABHD4.
DR MEROPS; S33.975; -.
DR iPTMnet; Q9DBL9; -.
DR PhosphoSitePlus; Q9DBL9; -.
DR SwissPalm; Q9DBL9; -.
DR EPD; Q9DBL9; -.
DR jPOST; Q9DBL9; -.
DR MaxQB; Q9DBL9; -.
DR PaxDb; Q9DBL9; -.
DR PeptideAtlas; Q9DBL9; -.
DR PRIDE; Q9DBL9; -.
DR ProteomicsDB; 286052; -. [Q9DBL9-1]
DR ProteomicsDB; 286053; -. [Q9DBL9-2]
DR Antibodypedia; 29395; 348 antibodies from 33 providers.
DR DNASU; 67469; -.
DR Ensembl; ENSMUST00000111497; ENSMUSP00000107123; ENSMUSG00000032540. [Q9DBL9-2]
DR Ensembl; ENSMUST00000156520; ENSMUSP00000122274; ENSMUSG00000032540. [Q9DBL9-1]
DR GeneID; 67469; -.
DR KEGG; mmu:67469; -.
DR UCSC; uc009sew.1; mouse. [Q9DBL9-1]
DR UCSC; uc009sey.1; mouse. [Q9DBL9-2]
DR CTD; 51099; -.
DR MGI; MGI:1914719; Abhd5.
DR VEuPathDB; HostDB:ENSMUSG00000032540; -.
DR eggNOG; KOG4409; Eukaryota.
DR GeneTree; ENSGT00390000016277; -.
DR HOGENOM; CLU_017361_0_0_1; -.
DR InParanoid; Q9DBL9; -.
DR OMA; SCDPGAQ; -.
DR OrthoDB; 1555935at2759; -.
DR PhylomeDB; Q9DBL9; -.
DR TreeFam; TF314196; -.
DR BRENDA; 2.3.1.51; 3474.
DR BioGRID-ORCS; 67469; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Abhd5; mouse.
DR PRO; PR:Q9DBL9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DBL9; protein.
DR Bgee; ENSMUSG00000032540; Expressed in spermatid and 258 other tissues.
DR ExpressionAtlas; Q9DBL9; baseline and differential.
DR Genevisible; Q9DBL9; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; ISO:MGI.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IMP:CACAO.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:MGI.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Alternative splicing; Cytoplasm;
KW Differentiation; Fatty acid metabolism; Lipid biosynthesis; Lipid droplet;
KW Lipid metabolism; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..351
FT /note="1-acylglycerol-3-phosphate O-acyltransferase ABHD5"
FT /id="PRO_0000080867"
FT DOMAIN 79..184
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT MOTIF 329..334
FT /note="HXXXXD motif"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6QA69"
FT VAR_SEQ 19..171
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015345"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:5A4H"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:5A4H"
SQ SEQUENCE 351 AA; 39155 MW; 04068BFB77D33E67 CRC64;
MKAMAAEEEV DSADAGGGSG WLTGWLPTWC PTSTSHLKEA EEKMLKCVPC TYKKEPVRIS
NGNRIWTLMF SHNISSKTPL VLLHGFGGGL GLWALNFEDL STDRPVYAFD LLGFGRSSRP
RFDSDAEEVE NQFVESIEEW RCALRLDKMI LLGHNLGGFL AAAYSLKYPS RVSHLILVEP
WGFPERPDLA DQERPIPVWI RALGAALTPF NPLAGLRIAG PFGLSLVQRL RPDFKRKYSS
MFEDDTVTEY IYHCNVQTPS GETAFKNMTI PYGWAKRPML QRIGGLHPDI PVSVIFGARS
CIDGNSGTSI QSLRPKSYVK TIAILGAGHY VYADQPEEFN QKVKEICHTV D
