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Protein

1-acylglycerol-3-phosphate O-acyltransferase ABHD5

Gene

Abhd5

Organism
Mus musculus (Mouse)
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 (PubMed:16679289). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (PubMed:16679289). Involved in keratinocyte differentiation (PubMed:16679289). Regulates lipid droplet fusion (PubMed:26083785).2 Publications

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

Enzyme and pathway databases

BRENDAi2.3.1.51. 3474.
ReactomeiR-MMU-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Protein family/group databases

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

Chemistry databases

SwissLipidsiSLP:000000283.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1914719. Abhd5.

Subcellular locationi

  • Cytoplasm
  • Lipid droplet

  • 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

  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • intracellular membrane-bounded organelle Source: MGI
  • lipid particle Source: UniProtKB
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lipid droplet

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3259509.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000808671 – 3511-acylglycerol-3-phosphate O-acyltransferase ABHD5Add BLAST351

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei124PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9DBL9.
PeptideAtlasiQ9DBL9.
PRIDEiQ9DBL9.

PTM databases

iPTMnetiQ9DBL9.
PhosphoSitePlusiQ9DBL9.

Expressioni

Tissue specificityi

Highly expressed in the adipose tissue and testes. Weakly expressed in the liver, muscle, kidney, and heart. Expressed by upper epidermal layers and dermal fibroblasts in skin, hepatocytes and hypothalamus in brain (at protein level).3 Publications

Gene expression databases

BgeeiENSMUSG00000032540.
CleanExiMM_ABHD5.
ExpressionAtlasiQ9DBL9. baseline and differential.
GenevisibleiQ9DBL9. MM.

Interactioni

Subunit structurei

Interacts with ADRP (By similarity). Interacts with PLIN. Interacts with and PNPLA2. Interacts with PLIN5; promotes interaction with PNPLA2.By similarity4 Publications

Protein-protein interaction databases

BioGridi212211. 4 interactors.
DIPiDIP-61642N.
STRINGi10090.ENSMUSP00000122274.

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 23Combined sources3
Beta strandi39 – 41Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5A4HNMR-A10-43[»]
ProteinModelPortaliQ9DBL9.
SMRiQ9DBL9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini79 – 184AB hydrolase-1Sequence analysisAdd BLAST106

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi329 – 334HXXXXD motif6

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4409. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00390000016277.
HOVERGENiHBG054445.
InParanoidiQ9DBL9.
KOiK13699.
OMAiWTLKFSH.
OrthoDBiEOG091G0AEW.
PhylomeDBiQ9DBL9.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9DBL9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKAMAAEEEV DSADAGGGSG WLTGWLPTWC PTSTSHLKEA EEKMLKCVPC
60 70 80 90 100
TYKKEPVRIS NGNRIWTLMF SHNISSKTPL 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):39,155
Last modified:June 1, 2001 - v1
Checksum:i04068BFB77D33E67
GO
Isoform 2 (identifier: Q9DBL9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-171: Missing.

Note: No experimental confirmation available.
Show »
Length:198
Mass (Da):21,846
Checksum:i724796B08B1653D0
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01534519 – 171Missing in isoform 2. 1 PublicationAdd BLAST153

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004873 mRNA. Translation: BAB23632.1.
AK019488 mRNA. Translation: BAB31755.2.
AK050377 mRNA. Translation: BAC34220.1.
BC037063 mRNA. Translation: AAH37063.1.
CCDSiCCDS23646.1. [Q9DBL9-1]
RefSeqiNP_080455.1. NM_026179.2. [Q9DBL9-1]
XP_006512308.1. XM_006512245.3. [Q9DBL9-2]
UniGeneiMm.280254.

Genome annotation databases

EnsembliENSMUST00000111497; ENSMUSP00000107123; ENSMUSG00000032540. [Q9DBL9-2]
ENSMUST00000156520; ENSMUSP00000122274; ENSMUSG00000032540. [Q9DBL9-1]
GeneIDi67469.
KEGGimmu:67469.
UCSCiuc009sew.1. mouse. [Q9DBL9-1]
uc009sey.1. mouse. [Q9DBL9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004873 mRNA. Translation: BAB23632.1.
AK019488 mRNA. Translation: BAB31755.2.
AK050377 mRNA. Translation: BAC34220.1.
BC037063 mRNA. Translation: AAH37063.1.
CCDSiCCDS23646.1. [Q9DBL9-1]
RefSeqiNP_080455.1. NM_026179.2. [Q9DBL9-1]
XP_006512308.1. XM_006512245.3. [Q9DBL9-2]
UniGeneiMm.280254.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5A4HNMR-A10-43[»]
ProteinModelPortaliQ9DBL9.
SMRiQ9DBL9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212211. 4 interactors.
DIPiDIP-61642N.
STRINGi10090.ENSMUSP00000122274.

Chemistry databases

ChEMBLiCHEMBL3259509.
SwissLipidsiSLP:000000283.

Protein family/group databases

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

PTM databases

iPTMnetiQ9DBL9.
PhosphoSitePlusiQ9DBL9.

Proteomic databases

PaxDbiQ9DBL9.
PeptideAtlasiQ9DBL9.
PRIDEiQ9DBL9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000111497; ENSMUSP00000107123; ENSMUSG00000032540. [Q9DBL9-2]
ENSMUST00000156520; ENSMUSP00000122274; ENSMUSG00000032540. [Q9DBL9-1]
GeneIDi67469.
KEGGimmu:67469.
UCSCiuc009sew.1. mouse. [Q9DBL9-1]
uc009sey.1. mouse. [Q9DBL9-2]

Organism-specific databases

CTDi51099.
MGIiMGI:1914719. Abhd5.

Phylogenomic databases

eggNOGiKOG4409. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00390000016277.
HOVERGENiHBG054445.
InParanoidiQ9DBL9.
KOiK13699.
OMAiWTLKFSH.
OrthoDBiEOG091G0AEW.
PhylomeDBiQ9DBL9.
TreeFamiTF314196.

Enzyme and pathway databases

BRENDAi2.3.1.51. 3474.
ReactomeiR-MMU-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

ChiTaRSiAbhd5. mouse.
PROiQ9DBL9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032540.
CleanExiMM_ABHD5.
ExpressionAtlasiQ9DBL9. baseline and differential.
GenevisibleiQ9DBL9. MM.

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...

Entry informationi

Entry nameiABHD5_MOUSE
AccessioniPrimary (citable) accession number: Q9DBL9
Secondary accession number(s): Q9CTY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 125 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. 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.