ABHD5_PONAB
ID ABHD5_PONAB Reviewed; 349 AA.
AC Q5RBI4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase ABHD5 {ECO:0000250|UniProtKB:Q8WTS1};
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q8WTS1};
DE AltName: Full=Abhydrolase domain-containing protein 5;
GN Name=ABHD5 {ECO:0000250|UniProtKB:Q8WTS1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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, PLIN and PNPLA2. Interacts with PLIN5;
CC promotes interaction with PNPLA2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Lipid droplet
CC {ECO:0000250}. Note=Colocalized with PLIN and ADRP on the surface of
CC lipid droplets. The localization is dependent upon the metabolic status
CC of the adipocytes and the activity of PKA (By similarity).
CC {ECO:0000250}.
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; CR858663; CAH90876.1; -; mRNA.
DR RefSeq; NP_001127344.1; NM_001133872.1.
DR AlphaFoldDB; Q5RBI4; -.
DR SMR; Q5RBI4; -.
DR STRING; 9601.ENSPPYP00000015621; -.
DR ESTHER; ponab-abhd5; CGI-58_ABHD5_ABHD4.
DR MEROPS; S33.975; -.
DR Ensembl; ENSPPYT00000016242; ENSPPYP00000015621; ENSPPYG00000013964.
DR GeneID; 100174407; -.
DR KEGG; pon:100174407; -.
DR CTD; 51099; -.
DR eggNOG; KOG4409; Eukaryota.
DR GeneTree; ENSGT00390000016277; -.
DR HOGENOM; CLU_017361_0_0_1; -.
DR InParanoid; Q5RBI4; -.
DR OMA; SCDPGAQ; -.
DR OrthoDB; 1555935at2759; -.
DR TreeFam; TF314196; -.
DR Proteomes; UP000001595; Chromosome 3.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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:0051006; P:positive regulation of lipoprotein lipase activity; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Cytoplasm; Differentiation;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WTS1"
FT CHAIN 2..349
FT /note="1-acylglycerol-3-phosphate O-acyltransferase ABHD5"
FT /id="PRO_0000080869"
FT DOMAIN 77..184
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT MOTIF 327..332
FT /note="HXXXXD motif"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WTS1"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6QA69"
SQ SEQUENCE 349 AA; 39065 MW; 49A6A8EC49A6023B CRC64;
MAAEEEEVDS ADTGERSGWL TGWLPTWCPT STSHLKEAEE KMLKCVPCTY KKEPVHISNG
NKIWTLKFSH NISNKTPLVL LHGFGGGLGL WALNFGDLCT NRPVYAFDLL GFGRSSRPRF
DSDAEEVENQ FVESIEEWRC ALGLDKMILL GHNLGGFLAA AYSLKYPSRV NHLILVEPWG
FPERPDLADQ DRPIPVWIRA LGAALTPFNP LAGLRIAGPF GLSLVQRLRP DFKRKYSSMF
EDDTVTEYIY HCNVQTPSGE TAFKNMTIPY GWAKRPMLQR IGKMHPDIPV SVIFGARSCI
DGNSGTSIQS LRPHSYVKTI AILGAGHYVY ADQPEEFNQK VKEICDTVD
