ABHD5_RAT
ID ABHD5_RAT Reviewed; 351 AA.
AC Q6QA69;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
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|RGD:1303237};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PLIN AND ADRP, SUBCELLULAR
RP LOCATION, INDUCTION, AND MUTAGENESIS OF GLU-9; GLN-132 AND GLU-262.
RX PubMed=15136565; DOI=10.1074/jbc.m403920200;
RA Yamaguchi T., Omatsu N., Matsushita S., Osumi T.;
RT "CGI-58 interacts with perilipin and is localized to lipid droplets.
RT Possible involvement of CGI-58 mislocalization in Chanarin-Dorfman
RT syndrome.";
RL J. Biol. Chem. 279:30490-30497(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP INTERACTION WITH PLIN5.
RX PubMed=23408028; DOI=10.1152/ajpregu.00418.2012;
RA MacPherson R.E., Ramos S.V., Vandenboom R., Roy B.D., Peters S.J.;
RT "Skeletal muscle PLIN proteins, ATGL and CGI-58, interactions at rest and
RT following stimulated contraction.";
RL Am. J. Physiol. 304:R644-R650(2013).
CC -!- FUNCTION: Coenzyme A-dependent lysophosphatidic acid acyltransferase
CC that catalyzes the transfert of an acyl group on a lysophosphatidic
CC acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid
CC followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-
CC lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid
CC acceptor. Functions preferentially with arachidonoyl-CoA followed by
CC oleoyl-CoA as acyl group donors (By similarity). Functions in
CC phosphatidic acid biosynthesis (By similarity). May regulate the
CC cellular storage of triacylglycerol through activation of the
CC phospholipase PNPLA2 (By similarity). Involved in keratinocyte
CC differentiation (By similarity). Regulates lipid droplet fusion (By
CC similarity). {ECO:0000250|UniProtKB:Q8WTS1,
CC ECO:0000250|UniProtKB:Q9DBL9}.
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:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37452;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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:0000250|UniProtKB:Q9DBL9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456;
CC Evidence={ECO:0000250|UniProtKB:Q9DBL9};
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:0000250|UniProtKB:Q9DBL9}.
CC -!- SUBUNIT: Interacts with ADRP and PLIN. Interacts with PNPLA2 (By
CC similarity). Interacts with PLIN5; promotes interaction with PNPLA2.
CC {ECO:0000250, ECO:0000269|PubMed:15136565,
CC ECO:0000269|PubMed:23408028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15136565}. Lipid
CC droplet {ECO:0000269|PubMed:15136565}. Note=Colocalized with PLIN and
CC ADRP on the surface of lipid droplets. The localization is dependent
CC upon the metabolic status of the adipocytes and the activity of PKA.
CC -!- INDUCTION: Increased in the early stage of adipocyte differentiation.
CC {ECO:0000269|PubMed:15136565}.
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.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY550934; AAS57860.1; -; mRNA.
DR RefSeq; NP_997689.1; NM_212524.1.
DR AlphaFoldDB; Q6QA69; -.
DR SMR; Q6QA69; -.
DR STRING; 10116.ENSRNOP00000000239; -.
DR ESTHER; ratno-abhd5; CGI-58_ABHD5_ABHD4.
DR MEROPS; S33.975; -.
DR iPTMnet; Q6QA69; -.
DR PhosphoSitePlus; Q6QA69; -.
DR jPOST; Q6QA69; -.
DR PaxDb; Q6QA69; -.
DR PRIDE; Q6QA69; -.
DR GeneID; 316122; -.
DR KEGG; rno:316122; -.
DR UCSC; RGD:1303237; rat.
DR CTD; 51099; -.
DR RGD; 1303237; Abhd5.
DR VEuPathDB; HostDB:ENSRNOG00000000221; -.
DR eggNOG; KOG4409; Eukaryota.
DR HOGENOM; CLU_017361_0_0_1; -.
DR InParanoid; Q6QA69; -.
DR OMA; SCDPGAQ; -.
DR OrthoDB; 1555935at2759; -.
DR TreeFam; TF314196; -.
DR PRO; PR:Q6QA69; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000000221; Expressed in esophagus and 18 other tissues.
DR Genevisible; Q6QA69; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:RGD.
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; IDA:MGI.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; ISO:RGD.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; ISO:RGD.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISS: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 Acyltransferase; Cytoplasm; Differentiation; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..351
FT /note="1-acylglycerol-3-phosphate O-acyltransferase ABHD5"
FT /id="PRO_0000080870"
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:0007744|PubMed:22673903"
FT MUTAGEN 9
FT /note="E->K: Colocalized to the lipid droplets with PLIN
FT and ADPR."
FT /evidence="ECO:0000269|PubMed:15136565"
FT MUTAGEN 132
FT /note="Q->P: Exhibits a diffuse cytoplasmic distribution
FT without colocalization to lipid droplets with PLIN and
FT ADPR. Loss of binding to PLIN."
FT /evidence="ECO:0000269|PubMed:15136565"
FT MUTAGEN 262
FT /note="E->K: Exhibits a diffuse cytoplasmic distribution
FT without colocalization to lipid droplets with PLIN and
FT ADPR. Loss of binding to PLIN."
FT /evidence="ECO:0000269|PubMed:15136565"
SQ SEQUENCE 351 AA; 39104 MW; DDC5BBA54D8D5ACD CRC64;
MKAMAAEEEV DSADAGGGSG WLTGWLPTWC PTSTSHLKEA EEKMLKCVPC TYKKEPVRIS
NGNSIWTLMF SHNMSSKTPL 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
