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Protein

1-acylglycerol-3-phosphate O-acyltransferase ABHD5

Gene

Abhd5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Lysophosphatidic acid acyltransferase which functions in phosphatidic acid biosynthesis. May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2. Involved in keratinocyte differentiation. Regulates lipid droplet fusion.By similarity

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Differentiation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Protein family/group databases

ESTHERiratno-abhd5. CGI-58_ABHD5_ABHD4.
MEROPSiS33.975.

Names & Taxonomyi

Protein namesi
Recommended name:
1-acylglycerol-3-phosphate O-acyltransferase ABHD5 (EC:2.3.1.51)
Alternative name(s):
Abhydrolase domain-containing protein 5
Lipid droplet-binding protein CGI-58
Short name:
Protein CGI-58
Gene namesi
Name:Abhd5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi1303237. Abhd5.

Subcellular locationi

  • Cytoplasm 1 Publication
  • 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.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lipid droplet

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91E → K: Colocalized to the lipid droplets with PLIN and ADPR. 1 Publication
Mutagenesisi132 – 1321Q → P: Exhibits a diffuse cytoplasmic disribution without colocalization to lipid droplets with PLIN and ADPR. Loss of binding to PLIN. 1 Publication
Mutagenesisi262 – 2621E → K: Exhibits a diffuse cytoplasmic disribution without colocalization to lipid droplets with PLIN and ADPR. Loss of binding to PLIN. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3513511-acylglycerol-3-phosphate O-acyltransferase ABHD5PRO_0000080870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ6QA69.
PRIDEiQ6QA69.

PTM databases

iPTMnetiQ6QA69.

Expressioni

Inductioni

Increased in the early stage of adipocyte differentiation.1 Publication

Gene expression databases

GenevisibleiQ6QA69. RN.

Interactioni

Subunit structurei

Interacts with ADRP and PLIN. Interacts with PNPLA2 (By similarity). Interacts with PLIN5; promotes interaction with PNPLA2.By similarity2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000239.

Structurei

3D structure databases

ProteinModelPortaliQ6QA69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi329 – 3346HXXXXD motif

Domaini

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4409. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00390000016277.
HOVERGENiHBG054445.
InParanoidiQ6QA69.
KOiK13699.
OMAiWTLKFSH.
OrthoDBiEOG751NG1.
TreeFamiTF314196.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6QA69-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:351
Mass (Da):39,104
Last modified:July 5, 2004 - v1
Checksum:iDDC5BBA54D8D5ACD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY550934 mRNA. Translation: AAS57860.1.
RefSeqiNP_997689.1. NM_212524.1.
UniGeneiRn.12459.

Genome annotation databases

EnsembliENSRNOT00000000239; ENSRNOP00000000239; ENSRNOG00000000221.
GeneIDi316122.
KEGGirno:316122.
UCSCiRGD:1303237. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY550934 mRNA. Translation: AAS57860.1.
RefSeqiNP_997689.1. NM_212524.1.
UniGeneiRn.12459.

3D structure databases

ProteinModelPortaliQ6QA69.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000239.

Protein family/group databases

ESTHERiratno-abhd5. CGI-58_ABHD5_ABHD4.
MEROPSiS33.975.

PTM databases

iPTMnetiQ6QA69.

Proteomic databases

PaxDbiQ6QA69.
PRIDEiQ6QA69.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000239; ENSRNOP00000000239; ENSRNOG00000000221.
GeneIDi316122.
KEGGirno:316122.
UCSCiRGD:1303237. rat.

Organism-specific databases

CTDi51099.
RGDi1303237. Abhd5.

Phylogenomic databases

eggNOGiKOG4409. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00390000016277.
HOVERGENiHBG054445.
InParanoidiQ6QA69.
KOiK13699.
OMAiWTLKFSH.
OrthoDBiEOG751NG1.
TreeFamiTF314196.

Miscellaneous databases

PROiQ6QA69.

Gene expression databases

GenevisibleiQ6QA69. RN.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CGI-58 interacts with perilipin and is localized to lipid droplets. Possible involvement of CGI-58 mislocalization in Chanarin-Dorfman syndrome."
    Yamaguchi T., Omatsu N., Matsushita S., Osumi T.
    J. Biol. Chem. 279:30490-30497(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PLIN AND ADRP, SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS OF GLU-9; GLN-132 AND GLU-262.
    Strain: ZDF.
  2. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. "Skeletal muscle PLIN proteins, ATGL and CGI-58, interactions at rest and following stimulated contraction."
    MacPherson R.E., Ramos S.V., Vandenboom R., Roy B.D., Peters S.J.
    Am. J. Physiol. 304:R644-R650(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLIN5.

Entry informationi

Entry nameiABHD5_RAT
AccessioniPrimary (citable) accession number: Q6QA69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.