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Q5RBI4 (ABHD5_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
1-acylglycerol-3-phosphate O-acyltransferase ABHD5

EC=2.3.1.51
Alternative name(s):
Abhydrolase domain-containing protein 5
Gene names
Name:ABHD5
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Subunit structure

Interacts with ADRP, PLIN and PNPLA2 By similarity.

Subcellular location

Cytoplasm By similarity. 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.

Domain

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

Sequence similarities

Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3493491-acylglycerol-3-phosphate O-acyltransferase ABHD5
PRO_0000080869

Regions

Motif327 – 3326HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q5RBI4 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 49A6A8EC49A6023B

FASTA34939,065
        10         20         30         40         50         60 
MAAEEEEVDS ADTGERSGWL TGWLPTWCPT STSHLKEAEE KMLKCVPCTY KKEPVHISNG 

        70         80         90        100        110        120 
NKIWTLKFSH NISNKTPLVL LHGFGGGLGL WALNFGDLCT NRPVYAFDLL GFGRSSRPRF 

       130        140        150        160        170        180 
DSDAEEVENQ FVESIEEWRC ALGLDKMILL GHNLGGFLAA AYSLKYPSRV NHLILVEPWG 

       190        200        210        220        230        240 
FPERPDLADQ DRPIPVWIRA LGAALTPFNP LAGLRIAGPF GLSLVQRLRP DFKRKYSSMF 

       250        260        270        280        290        300 
EDDTVTEYIY HCNVQTPSGE TAFKNMTIPY GWAKRPMLQR IGKMHPDIPV SVIFGARSCI 

       310        320        330        340 
DGNSGTSIQS LRPHSYVKTI AILGAGHYVY ADQPEEFNQK VKEICDTVD 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR858663 mRNA. Translation: CAH90876.1.
RefSeqNP_001127344.1. NM_001133872.1.
UniGenePab.19184.

3D structure databases

ProteinModelPortalQ5RBI4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPPYT00000016242; ENSPPYP00000015621; ENSPPYG00000013964.
GeneID100174407.
KEGGpon:100174407.

Organism-specific databases

CTD51099.

Phylogenomic databases

HOVERGENHBG054445.
InParanoidQ5RBI4.
OMALNFGDLC.
OrthoDBEOG4DR9CK.

Family and domain databases

InterProIPR000073. AB_hydrolase_1.
[Graphical view]
KOK13699.
PRINTSPR00111. ABHYDROLASE.
ProtoNetSearch...

Entry information

Entry nameABHD5_PONAB
AccessionPrimary (citable) accession number: Q5RBI4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 21, 2004
Last modified: November 16, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families