ABHD5_PIG
ID ABHD5_PIG Reviewed; 349 AA.
AC Q5EE05;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xia T., Yang Z.Q.;
RT "Mapping of porcine CGI-58 gene.";
RL Submitted (JAN-2005) 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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY902463; AAW82452.1; -; mRNA.
DR RefSeq; NP_001012407.1; NM_001012407.1.
DR AlphaFoldDB; Q5EE05; -.
DR SMR; Q5EE05; -.
DR STRING; 9823.ENSSSCP00000012044; -.
DR ESTHER; pig-abhd5; CGI-58_ABHD5_ABHD4.
DR MEROPS; S33.975; -.
DR PaxDb; Q5EE05; -.
DR PeptideAtlas; Q5EE05; -.
DR PRIDE; Q5EE05; -.
DR Ensembl; ENSSSCT00005064321; ENSSSCP00005039743; ENSSSCG00005039875.
DR GeneID; 497624; -.
DR KEGG; ssc:497624; -.
DR CTD; 51099; -.
DR eggNOG; KOG4409; Eukaryota.
DR InParanoid; Q5EE05; -.
DR OrthoDB; 1555935at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
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:0010891; P:negative regulation of sequestering of triglyceride; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
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; Reference proteome;
KW 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_0000080868"
FT DOMAIN 77..185
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"
SQ SEQUENCE 349 AA; 39004 MW; DE85BD529EE16854 CRC64;
MAAEEEEMDS TDACERSGWL TGWLPTWCPT STSHLKEAEE KILKCVPCIY KKGPVRISNG
NKIWTLKLSH NISNKIPLVL LHGFGGGLGL WALNFGDLCT NRPVYAFDLL GFGRSSRPRF
DTDAEEVENQ FVESIEEWRC ALGLDKVILL GHNLGGFLAA AYSLKYPSRV SHLILVEPWG
FPERPDLADQ ERPIPVWIRA LGAALTPFNP LAGLRIAGPF GLSLVQRLRP DFKRKYSSMF
EDDTVTEYIY HCNVQTPSGE TAFKNMTIPY GWAKRPMLHR IGKMNPDIPV SVIYGARSCI
DGNSGTSIQS LRPHSYVKTI AILGAGHYVY ADQPEDFNLK VKEICDTVD
