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Protein

1-acylglycerol-3-phosphate O-acyltransferase ABHD5

Gene

ABHD5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • cell differentiation Source: UniProtKB-KW
  • fatty acid metabolic process Source: UniProtKB-KW
  • negative regulation of sequestering of triglyceride Source: UniProtKB
  • phosphatidic acid biosynthetic process Source: UniProtKB
  • positive regulation of triglyceride catabolic process Source: UniProtKB

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processDifferentiation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiR-HSA-163560 Triglyceride catabolism

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

EuPathDBiHostDB:ENSG00000011198.7
HGNCiHGNC:21396 ABHD5
MIMi604780 gene
neXtProtiNX_Q8WTS1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Lipid droplet

Pathology & Biotechi

Involvement in diseasei

Chanarin-Dorfman syndrome (CDS)4 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 dbSNP:rs104893676EnsemblClinVar.1
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 dbSNP:rs28939077EnsemblClinVar.1
Natural variantiVAR_023389260E → K in CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity. 3 PublicationsCorresponds to variant dbSNP:rs28939078EnsemblClinVar.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
ProteomicsDBi74594

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, 11 interactors
IntActiQ8WTS1, 19 interactors
MINTiQ8WTS1
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
OMAiVPCTYKK
OrthoDBiEOG091G0AEW
PhylomeDBiQ8WTS1
TreeFamiTF314196

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000073 AB_hydrolase_1
PfamiView protein in Pfam
PF00561 Abhydrolase_1, 1 hit
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 dbSNP:rs104893676EnsemblClinVar.1
Natural variantiVAR_03757472I → T. Corresponds to variant dbSNP:rs2302349Ensembl.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 dbSNP:rs28939077EnsemblClinVar.1
Natural variantiVAR_023389260E → K in CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity. 3 PublicationsCorresponds to variant dbSNP:rs28939078EnsemblClinVar.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

EnsembliENST00000644371; ENSP00000495778; ENSG00000011198
GeneIDi51099
KEGGihsa:51099
UCSCiuc003cmx.4 human

Similar proteinsi

Entry informationi

Entry nameiABHD5_HUMAN
AccessioniPrimary (citable) accession number: Q8WTS1
Secondary accession number(s): B2R9K0, Q9Y369
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2002
Last modified: July 18, 2018
This is version 148 of the entry and version 1 of the sequence. See 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

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