Glycerol-3-phosphate acyltransferase 4 precursor

Contribute

Send feedback

Read comments (?) or add your own

Q86UL3 (GPAT4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Inferred from direct assay Ref.2. Source: UniProtKB lactation Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylcholine biosynthetic process Inferred from direct assay Ref.2. Source: UniProtKB triglyceride biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Non-traceable author statement Ref.2. Source: UniProtKB membrane fraction Inferred from direct assay Ref.2. Source: UniProtKB
Molecular function	glycerol-3-phosphate O-acyltransferase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 37

Potential

Chain

38 – 456

419

Glycerol-3-phosphate acyltransferase 4

PRO_0000024703

Regions

Transmembrane

156 – 176

Helical; Potential

Transmembrane

180 – 200

Helical; Potential

Motif

248 – 253

HXXXXD motif

Amino acid modifications

Modified residue

218

Phosphotyrosine Ref.5

Glycosylation

247

N-linked (GlcNAc...) Potential

Glycosylation

327

N-linked (GlcNAc...) Potential

Glycosylation

328

N-linked (GlcNAc...) Potential

Glycosylation

362

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q86UL3 [UniParc].

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

FASTA

456

52,071

        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' referencesShow '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: 12938015] [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: 18238778] [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. Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[5]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-218, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	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.
IPI	IPI00016070.
RefSeq	NP_848934.1. NM_178819.3.
UniGene	Hs.355753.
3D structure databases
ProteinModelPortal	Q86UL3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86UL3. 1 interaction.
MINT	MINT-2878746.
STRING	Q86UL3.
Polymorphism databases
DMDM	68052729.
Proteomic databases
PRIDE	Q86UL3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000396987; ENSP00000380184; ENSG00000158669.
GeneID	137964.
KEGG	hsa:137964.
UCSC	uc003xnz.1. human.
Organism-specific databases
CTD	137964.
GeneCards	GC08P041435.
H-InvDB	HIX0007472.
HGNC	HGNC:20880. AGPAT6.
HPA	HPA016471.
MIM	608143. gene.
neXtProt	NX_Q86UL3.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG408354.
InParanoid	Q86UL3.
OMA	YRICVRA.
OrthoDB	EOG4RXZ04.
PhylomeDB	Q86UL3.
Enzyme and pathway databases
Reactome	REACT_22258. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	Q86UL3.
Bgee	Q86UL3.
CleanEx	HS_AGPAT6.
Genevestigator	Q86UL3.
GermOnline	ENSG00000158669. Homo sapiens.
Family and domain databases
InterPro	IPR002123. Acyltransferase. [Graphical view]
KO	K13506.
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	83709.
SOURCE	Search...

Entry information

Entry name

GPAT4_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 8

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

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents