UniProtKB - Q6QA69 (ABHD5_RAT)
1-acylglycerol-3-phosphate O-acyltransferase ABHD5
Abhd5
Functioni
Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors (By similarity).
Functions in phosphatidic acid biosynthesis (By similarity).
May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (By similarity).
Involved in keratinocyte differentiation (By similarity).
Regulates lipid droplet fusion (By similarity).
By similarityCatalytic activityi
- a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoABy similarityEC:2.3.1.51By similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + eicosanoyl-CoA = 1-(9Z)-octadecenoyl-2-eicosanoyl-sn-glycero-3-phosphate + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
Activity regulationi
GO - Molecular functioni
- 1-acylglycerol-3-phosphate O-acyltransferase activity Source: UniProtKB
- carboxylic ester hydrolase activity Source: GO_Central
- lysophosphatidic acid acyltransferase activity Source: RGD
GO - Biological processi
- cell differentiation Source: UniProtKB-KW
- fatty acid metabolic process Source: UniProtKB-KW
- lipid homeostasis Source: GO_Central
- lipid metabolic process Source: MGI
- negative regulation of sequestering of triglyceride Source: UniProtKB
- phosphatidic acid biosynthetic process Source: UniProtKB
- positive regulation of lipid catabolic process Source: RGD
- positive regulation of lipoprotein lipase activity Source: RGD
- positive regulation of triglyceride catabolic process Source: UniProtKB
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Differentiation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism |
Protein family/group databases
ESTHERi | ratno-abhd5, CGI-58_ABHD5_ABHD4 |
MEROPSi | S33.975 |
Names & Taxonomyi
Protein namesi | Recommended name: 1-acylglycerol-3-phosphate O-acyltransferase ABHD5Curated (EC:2.3.1.51By similarity)Alternative name(s): Abhydrolase domain-containing protein 5 Lipid droplet-binding protein CGI-58 Short name: Protein CGI-58 |
Gene namesi | Name:Abhd5Imported |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 1303237, Abhd5 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Other locations
- Lipid droplet 1 Publication
Note: Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA.
Cytosol
- cytosol Source: UniProtKB
Mitochondrion
- mitochondrion Source: GO_Central
Nucleus
- nucleoplasm Source: Ensembl
Other locations
- lipid droplet Source: BHF-UCL
Keywords - Cellular componenti
Cytoplasm, Lipid dropletPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 9 | E → K: Colocalized to the lipid droplets with PLIN and ADPR. 1 Publication | 1 | |
Mutagenesisi | 132 | Q → P: Exhibits a diffuse cytoplasmic distribution without colocalization to lipid droplets with PLIN and ADPR. Loss of binding to PLIN. 1 Publication | 1 | |
Mutagenesisi | 262 | E → K: Exhibits a diffuse cytoplasmic distribution without colocalization to lipid droplets with PLIN and ADPR. Loss of binding to PLIN. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000080870 | 1 – 351 | 1-acylglycerol-3-phosphate O-acyltransferase ABHD5Add BLAST | 351 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 124 | PhosphoserineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
jPOSTi | Q6QA69 |
PaxDbi | Q6QA69 |
PTM databases
iPTMneti | Q6QA69 |
PhosphoSitePlusi | Q6QA69 |
Expressioni
Inductioni
Gene expression databases
Bgeei | ENSRNOG00000000221, Expressed in esophagus and 20 other tissues |
Genevisiblei | Q6QA69, RN |
Interactioni
Subunit structurei
Interacts with ADRP and PLIN.
Interacts with PNPLA2 (By similarity).
Interacts with PLIN5; promotes interaction with PNPLA2.
By similarity2 PublicationsProtein-protein interaction databases
STRINGi | 10116.ENSRNOP00000000239 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 79 – 184 | AB hydrolase-1Sequence analysisAdd BLAST | 106 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 329 – 334 | HXXXXD motif | 6 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG4409, Eukaryota |
GeneTreei | ENSGT00390000016277 |
HOGENOMi | CLU_017361_0_0_1 |
InParanoidi | Q6QA69 |
OMAi | SCDPGAQ |
OrthoDBi | 1555935at2759 |
TreeFami | TF314196 |
Family and domain databases
Gene3Di | 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR000073, AB_hydrolase_1 |
Pfami | View protein in Pfam PF00561, Abhydrolase_1, 1 hit |
PRINTSi | PR00111, ABHYDROLASE |
SUPFAMi | SSF53474, SSF53474, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MKAMAAEEEV DSADAGGGSG WLTGWLPTWC PTSTSHLKEA EEKMLKCVPC
60 70 80 90 100
TYKKEPVRIS NGNSIWTLMF SHNMSSKTPL VLLHGFGGGL GLWALNFEDL
110 120 130 140 150
STDRPVYAFD LLGFGRSSRP RFDSDAEEVE NQFVESIEEW RCALRLDKMI
160 170 180 190 200
LLGHNLGGFL AAAYSLKYPS RVSHLILVEP WGFPERPDLA DQERPIPVWI
210 220 230 240 250
RALGAALTPF NPLAGLRIAG PFGLSLVQRL RPDFKRKYSS MFEDDTVTEY
260 270 280 290 300
IYHCNVQTPS GETAFKNMTI PYGWAKRPML QRIGGLHPDI PVSVIFGARS
310 320 330 340 350
CIDGNSGTSI QSLRPKSYVK TIAILGAGHY VYADQPEEFN QKVKEICHTV
D
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY550934 mRNA Translation: AAS57860.1 |
RefSeqi | NP_997689.1, NM_212524.1 |
Genome annotation databases
Ensembli | ENSRNOT00000000239; ENSRNOP00000000239; ENSRNOG00000000221 |
GeneIDi | 316122 |
KEGGi | rno:316122 |
UCSCi | RGD:1303237, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY550934 mRNA Translation: AAS57860.1 |
RefSeqi | NP_997689.1, NM_212524.1 |
3D structure databases
SMRi | Q6QA69 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000000239 |
Protein family/group databases
ESTHERi | ratno-abhd5, CGI-58_ABHD5_ABHD4 |
MEROPSi | S33.975 |
PTM databases
iPTMneti | Q6QA69 |
PhosphoSitePlusi | Q6QA69 |
Proteomic databases
jPOSTi | Q6QA69 |
PaxDbi | Q6QA69 |
Genome annotation databases
Ensembli | ENSRNOT00000000239; ENSRNOP00000000239; ENSRNOG00000000221 |
GeneIDi | 316122 |
KEGGi | rno:316122 |
UCSCi | RGD:1303237, rat |
Organism-specific databases
CTDi | 51099 |
RGDi | 1303237, Abhd5 |
Phylogenomic databases
eggNOGi | KOG4409, Eukaryota |
GeneTreei | ENSGT00390000016277 |
HOGENOMi | CLU_017361_0_0_1 |
InParanoidi | Q6QA69 |
OMAi | SCDPGAQ |
OrthoDBi | 1555935at2759 |
TreeFami | TF314196 |
Miscellaneous databases
PROi | PR:Q6QA69 |
Gene expression databases
Bgeei | ENSRNOG00000000221, Expressed in esophagus and 20 other tissues |
Genevisiblei | Q6QA69, RN |
Family and domain databases
Gene3Di | 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR000073, AB_hydrolase_1 |
Pfami | View protein in Pfam PF00561, Abhydrolase_1, 1 hit |
PRINTSi | PR00111, ABHYDROLASE |
SUPFAMi | SSF53474, SSF53474, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ABHD5_RAT | |
Accessioni | Q6QA69Primary (citable) accession number: Q6QA69 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 30, 2005 |
Last sequence update: | July 5, 2004 | |
Last modified: | February 23, 2022 | |
This is version 127 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families