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Protein

1-acylglycerol-3-phosphate O-acyltransferase ABHD5

Gene

ABHD5

Organism
Homo sapiens (Human)
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:18606822). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (PubMed:16679289). Involved in keratinocyte differentiation (PubMed:18832586). Regulates lipid droplet fusion (By similarity).By similarity3 Publications

Catalytic activityi

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

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

BioCyciZFISH:HS00306-MONOMER.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Protein family/group databases

ESTHERihuman-ABHD5. CGI-58_ABHD5_ABHD4.
MEROPSiS33.975.

Chemistry databases

SwissLipidsiSLP:000000098.

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
Gene namesi
Name:ABHD5
Synonyms:NCIE2
ORF Names:CGI-58
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:21396. ABHD5.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Lipid droplet By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Lipid droplet

Pathology & Biotechi

Involvement in diseasei

Chanarin-Dorfman syndrome (CDS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive inborn error of lipid metabolism with multisystemic accumulation of triglycerides although plasma concentrations are normal. Clinical characteristics are congenital generalized ichthyosis, vacuolated leukocytes, hepatomegaly, myopathy, cataracts, neurosensory hearing loss and developmental delay. The disorder presents at birth with generalized, fine, white scaling of the skin and a variable degree of erythema resembling non-bullous congenital ichthyosiform erythroderma.
See also OMIM:275630
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0233877E → K in CDS. 1 PublicationCorresponds to variant rs104893676dbSNPEnsembl.1
Natural variantiVAR_05795382H → R Found in a patient with CDS but without evidence it may cause the disease. 1 Publication1
Natural variantiVAR_057954115S → G in CDS. 1 Publication1
Natural variantiVAR_023388130Q → P in CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity. 3 PublicationsCorresponds to variant rs28939077dbSNPEnsembl.1
Natural variantiVAR_023389260E → K in CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity. 3 PublicationsCorresponds to variant rs28939078dbSNPEnsembl.1

Keywords - Diseasei

Cataract, Deafness, Disease mutation, Ichthyosis

Organism-specific databases

DisGeNETi51099.
MalaCardsiABHD5.
MIMi275630. phenotype.
OpenTargetsiENSG00000011198.
Orphaneti98907. Dorfman-Chanarin disease.
PharmGKBiPA134891622.

Polymorphism and mutation databases

BioMutaiABHD5.
DMDMi73921640.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000808662 – 3491-acylglycerol-3-phosphate O-acyltransferase ABHD5Add BLAST348

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei122PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8WTS1.
MaxQBiQ8WTS1.
PaxDbiQ8WTS1.
PeptideAtlasiQ8WTS1.
PRIDEiQ8WTS1.

PTM databases

iPTMnetiQ8WTS1.
PhosphoSitePlusiQ8WTS1.

Expressioni

Tissue specificityi

Widely expressed in various tissues, including lymphocytes, liver, skeletal muscle and brain. Expressed by upper epidermal layers and dermal fibroblasts in skin, hepatocytes and neurons (at protein level).2 Publications

Developmental stagei

Detected in fetal epidermis from 49 to 135 days estimated gestational age (at protein level).1 Publication

Inductioni

Up-regulated upon keratinocyte differentiation (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000011198.
CleanExiHS_ABHD5.
ExpressionAtlasiQ8WTS1. baseline and differential.
GenevisibleiQ8WTS1. HS.

Organism-specific databases

HPAiCAB020685.
HPA035851.
HPA035852.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi119288. 12 interactors.
IntActiQ8WTS1. 3 interactors.
MINTiMINT-4650384.
STRINGi9606.ENSP00000390849.

Structurei

3D structure databases

ProteinModelPortaliQ8WTS1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini77 – 184AB hydrolase-1Sequence analysisAdd BLAST108

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi327 – 332HXXXXD 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.
HOGENOMiHOG000007445.
HOVERGENiHBG054445.
InParanoidiQ8WTS1.
KOiK13699.
OMAiWTLKFSH.
OrthoDBiEOG091G0AEW.
PhylomeDBiQ8WTS1.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8WTS1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAEEEEVDS ADTGERSGWL TGWLPTWCPT SISHLKEAEE KMLKCVPCTY
60 70 80 90 100
KKEPVRISNG NKIWTLKFSH NISNKTPLVL LHGFGGGLGL WALNFGDLCT
110 120 130 140 150
NRPVYAFDLL GFGRSSRPRF DSDAEEVENQ FVESIEEWRC ALGLDKMILL
160 170 180 190 200
GHNLGGFLAA AYSLKYPSRV NHLILVEPWG FPERPDLADQ DRPIPVWIRA
210 220 230 240 250
LGAALTPFNP LAGLRIAGPF GLSLVQRLRP DFKRKYSSMF EDDTVTEYIY
260 270 280 290 300
HCNVQTPSGE TAFKNMTIPY GWAKRPMLQR IGKMHPDIPV SVIFGARSCI
310 320 330 340
DGNSGTSIQS LRPHSYVKTI AILGAGHYVY ADQPEEFNQK VKEICDTVD
Length:349
Mass (Da):39,096
Last modified:March 1, 2002 - v1
Checksum:i85958A2DEC169C82
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti263F → S in AAD34053 (PubMed:10810093).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0233877E → K in CDS. 1 PublicationCorresponds to variant rs104893676dbSNPEnsembl.1
Natural variantiVAR_03757472I → T.Corresponds to variant rs2302349dbSNPEnsembl.1
Natural variantiVAR_05795382H → R Found in a patient with CDS but without evidence it may cause the disease. 1 Publication1
Natural variantiVAR_057954115S → G in CDS. 1 Publication1
Natural variantiVAR_023388130Q → P in CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity. 3 PublicationsCorresponds to variant rs28939077dbSNPEnsembl.1
Natural variantiVAR_023389260E → K in CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity. 3 PublicationsCorresponds to variant rs28939078dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL606838 Genomic DNA. Translation: CAD12731.1.
AF151816 mRNA. Translation: AAD34053.1.
AK313811 mRNA. Translation: BAG36547.1.
AC105903 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64699.1.
BC021958 mRNA. Translation: AAH21958.1.
CCDSiCCDS2711.1.
RefSeqiNP_057090.2. NM_016006.4.
UniGeneiHs.19385.

Genome annotation databases

EnsembliENST00000458276; ENSP00000390849; ENSG00000011198.
GeneIDi51099.
KEGGihsa:51099.
UCSCiuc003cmx.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL606838 Genomic DNA. Translation: CAD12731.1.
AF151816 mRNA. Translation: AAD34053.1.
AK313811 mRNA. Translation: BAG36547.1.
AC105903 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64699.1.
BC021958 mRNA. Translation: AAH21958.1.
CCDSiCCDS2711.1.
RefSeqiNP_057090.2. NM_016006.4.
UniGeneiHs.19385.

3D structure databases

ProteinModelPortaliQ8WTS1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119288. 12 interactors.
IntActiQ8WTS1. 3 interactors.
MINTiMINT-4650384.
STRINGi9606.ENSP00000390849.

Chemistry databases

SwissLipidsiSLP:000000098.

Protein family/group databases

ESTHERihuman-ABHD5. CGI-58_ABHD5_ABHD4.
MEROPSiS33.975.

PTM databases

iPTMnetiQ8WTS1.
PhosphoSitePlusiQ8WTS1.

Polymorphism and mutation databases

BioMutaiABHD5.
DMDMi73921640.

Proteomic databases

EPDiQ8WTS1.
MaxQBiQ8WTS1.
PaxDbiQ8WTS1.
PeptideAtlasiQ8WTS1.
PRIDEiQ8WTS1.

Protocols and materials databases

DNASUi51099.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000458276; ENSP00000390849; ENSG00000011198.
GeneIDi51099.
KEGGihsa:51099.
UCSCiuc003cmx.4. human.

Organism-specific databases

CTDi51099.
DisGeNETi51099.
GeneCardsiABHD5.
HGNCiHGNC:21396. ABHD5.
HPAiCAB020685.
HPA035851.
HPA035852.
MalaCardsiABHD5.
MIMi275630. phenotype.
604780. gene.
neXtProtiNX_Q8WTS1.
OpenTargetsiENSG00000011198.
Orphaneti98907. Dorfman-Chanarin disease.
PharmGKBiPA134891622.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4409. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00390000016277.
HOGENOMiHOG000007445.
HOVERGENiHBG054445.
InParanoidiQ8WTS1.
KOiK13699.
OMAiWTLKFSH.
OrthoDBiEOG091G0AEW.
PhylomeDBiQ8WTS1.
TreeFamiTF314196.

Enzyme and pathway databases

BioCyciZFISH:HS00306-MONOMER.
ReactomeiR-HSA-163560. Hormone-sensitive lipase (HSL)-mediated triacylglycerol hydrolysis.

Miscellaneous databases

GeneWikiiABHD5.
GenomeRNAii51099.
PROiQ8WTS1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000011198.
CleanExiHS_ABHD5.
ExpressionAtlasiQ8WTS1. baseline and differential.
GenevisibleiQ8WTS1. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q8WTS1
Secondary accession number(s): B2R9K0, Q9Y369
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2002
Last modified: November 2, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. 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.