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Q86UL3 (GPAT4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate acyltransferase 4

Short name=GPAT4
EC=2.3.1.15
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 6
Short name=1-AGP acyltransferase 6
Short name=1-AGPAT 6
Acyl-CoA:glycerol-3-phosphate acyltransferase 4
Lysophosphatidic acid acyltransferase zeta
Short name=LPAAT-zeta
Gene names
Name:AGPAT6
Synonyms:GPAT4
ORF Names:UNQ551/PRO1108
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Active against both saturated and unsaturated long-chain fatty acyl-CoAs. Ref.2

Catalytic activity

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

Enzyme regulation

Inhibited by N-ethylmaleimide (NEM). Ref.2

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.2.

Tissue specificity

Ubiquitous. Relatively high level of expression in skeletal muscle, heart and testis. Relatively low level of expression in lung. Ref.1 Ref.2

Domain

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 similarities

Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Phospholipid biosynthesis
Phospholipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCDP-diacylglycerol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

acyl-CoA metabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

cellular lipid metabolic process

Traceable author statement. Source: Reactome

diacylglycerol metabolic process

Inferred from electronic annotation. Source: Ensembl

fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

glandular epithelial cell maturation

Inferred from electronic annotation. Source: Ensembl

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

lactation

Inferred from sequence or structural similarity. Source: UniProtKB

lipid biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidic acid biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylcholine biosynthetic process

Inferred from direct assay Ref.2. Source: UniProtKB

phospholipid metabolic process

Traceable author statement. Source: Reactome

regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.2. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Non-traceable author statement Ref.2. Source: UniProtKB

membrane

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionglycerol-3-phosphate O-acyltransferase activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Potential
Chain38 – 456419Glycerol-3-phosphate acyltransferase 4
PRO_0000024703

Regions

Transmembrane156 – 17621Helical; Potential
Transmembrane180 – 20021Helical; Potential
Motif248 – 2536HXXXXD motif

Amino acid modifications

Glycosylation2471N-linked (GlcNAc...) Potential
Glycosylation3271N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q86UL3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 5B9DEB2912E989E5

FASTA45652,071
        10         20         30         40         50         60 
MFLLLPFDSL IVNLLGISLT VLFTLLLVFI IVPAIFGVSF GIRKLYMKSL LKIFAWATLR 

        70         80         90        100        110        120 
MERGAKEKNH QLYKPYTNGI IAKDPTSLEE EIKEIRRSGS SKALDNTPEF ELSDIFYFCR 

       130        140        150        160        170        180 
KGMETIMDDE VTKRFSAEEL ESWNLLSRTN YNFQYISLRL TVLWGLGVLI RYCFLLPLRI 

       190        200        210        220        230        240 
ALAFTGISLL VVGTTVVGYL PNGRFKEFMS KHVHLMCYRI CVRALTAIIT YHDRENRPRN 

       250        260        270        280        290        300 
GGICVANHTS PIDVIILASD GYYAMVGQVH GGLMGVIQRA MVKACPHVWF ERSEVKDRHL 

       310        320        330        340        350        360 
VAKRLTEHVQ DKSKLPILIF PEGTCINNTS VMMFKKGSFE IGATVYPVAI KYDPQFGDAF 

       370        380        390        400        410        420 
WNSSKYGMVT YLLRMMTSWA IVCSVWYLPP MTREADEDAV QFANRVKSAI ARQGGLVDLL 

       430        440        450 
WDGGLKREKV KDTFKEEQQK LYSKMIVGNH KDRSRS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and identification of the human LPAAT-zeta gene, a novel member of the lysophosphatidic acid acyltransferase family."
Li D., Yu L., Wu H., Shan Y., Guo J., Dang Y., Wei Y., Zhao S.
J. Hum. Genet. 48:438-442(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase."
Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E., Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E., Konrad R.J., Beigneux A.P., Young S.G., Cao G.
J. Biol. Chem. 283:10048-10057(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, TISSUE SPECIFICITY.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF406612 mRNA. Translation: AAP21893.1.
AY358670 mRNA. Translation: AAQ89033.1.
BC051377 mRNA. Translation: AAH51377.2.
BC061884 mRNA. Translation: AAH61884.1.
RefSeqNP_848934.1. NM_178819.3.
UniGeneHs.355753.

3D structure databases

ProteinModelPortalQ86UL3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126493. 3 interactions.
IntActQ86UL3. 2 interactions.
MINTMINT-2878746.
STRING9606.ENSP00000380184.

PTM databases

PhosphoSiteQ86UL3.

Polymorphism databases

DMDM68052729.

Proteomic databases

PaxDbQ86UL3.
PRIDEQ86UL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000396987; ENSP00000380184; ENSG00000158669.
GeneID137964.
KEGGhsa:137964.
UCSCuc003xnz.2. human.

Organism-specific databases

CTD137964.
GeneCardsGC08P041435.
HGNCHGNC:20880. AGPAT6.
HPAHPA016471.
MIM608143. gene.
neXtProtNX_Q86UL3.
PharmGKBPA142672637.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0204.
HOGENOMHOG000265725.
InParanoidQ86UL3.
KOK13506.
OMAITYHDRK.
OrthoDBEOG70GMFG.
PhylomeDBQ86UL3.
TreeFamTF315039.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00557; UER00612.

Gene expression databases

ArrayExpressQ86UL3.
BgeeQ86UL3.
CleanExHS_AGPAT6.
GenevestigatorQ86UL3.

Family and domain databases

InterProIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAGPAT6. human.
GenomeRNAi137964.
NextBio83709.
PROQ86UL3.
SOURCESearch...

Entry information

Entry nameGPAT4_HUMAN
AccessionPrimary (citable) accession number: Q86UL3
Secondary accession number(s): Q86V89
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM