NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/c;
TISSUE=Liver;
DOI=10.1038/ng880; PubMed=11967537 [NCBI, ExPASy, EBI, Israel, Japan]
Agarwal A.K., Arioglu E., de Almeida S., Akkoc N., Taylor S.I., Bowcock A.M., Barnes R.I., Garg A.;
"AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34.";
Nat. Genet. 31:21-23(2002).

[2]

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-255 AND SER-260, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr0604155; PubMed=17203969 [NCBI, ExPASy, EBI, Israel, Japan]
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry.";
J. Proteome Res. 6:250-262(2007).

Comments

FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3 .
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (Potential).
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).
SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY072769; AAL62337.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_080488.1; -.

UniGene

Mm.24244

3D structure databases

ModBase

Q8K3K7.

PTM databases

PhosphoSite

Q8K3K7; -.

Organism-specific databases

MGI

MGI:1914762; Agpat2.

Gene expression databases

GermOnline

ENSMUSG00000026922; Mus musculus.

Ontologies

GO:0005783;	Cellular component: endoplasmic reticulum (inferred from direct assay from UniProtKB).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0003841;	Molecular function: 1-acylglycerol-3-phosphate O-acyltransferase activity (inferred from direct assay from UniProtKB).
GO:0008654;	Biological process: phospholipid biosynthetic process (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR002123; Acyltransferase.
IPR004552; AGP_acyltrans.
Graphical view of domain structure.

Pfam

PF01553; Acyltransferase; 1.
Pfam graphical view of domain structure.

SMART

SM00563; PlsC; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00530; AGP_acyltrn; 1.

ProtoNet

Q8K3K7.

Genome annotation databases

Ensembl

ENSMUSG00000026922; Mus musculus. [Contig view]

GeneID

67512; -.

KEGG

mmu:67512; -.

Phylogenomic databases

HOGENOM

Q8K3K7; -.

HOVERGEN

Q8K3K7; -.

Other

NextBio

324790; -.

SOURCE

Agpat2; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Membrane; Phospholipid biosynthesis; Phosphoprotein; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 278`	`278`	`1-acyl-sn-glycerol-3-phosphate acyltransferase beta.`	`PRO_0000208193`
`TRANSMEM`	`1 21`	`21`	`Potential.`
`TRANSMEM`	`30 50`	`21`	`Potential.`
`TRANSMEM`	`122 142`	`21`	`Potential.`
`MOTIF`	`98 103`	`6`	`HXXXXD motif.`
`MOD_RES`	`255 255`		`Phosphothreonine.`
`MOD_RES`	`260 260`		`Phosphoserine.`

Sequence information

Length: 278 AA [This is the length of the unprocessed precursor]

Molecular weight: 31011 Da [This is the MW of the unprocessed precursor]

CRC64: 57A54BFB1A0EFF56 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDPWPWLTAA LLLLLLLVQL SRTARFYAKV GLYCVLCLSF SAAASIVCLL RHGGRTVDNM 

        70         80         90        100        110        120 
SIISWFVRSF KYVYGLRFEV SGQKKLEVDG PCVIISNHQS ILDMMGLMEI LPKRCVQIAK 

       130        140        150        160        170        180 
RELMFTGPVG LIMYLGGVYF INRQQARTAM SVMADLGDLM VKENLKVWIY PEGTRNDNGD 

       190        200        210        220        230        240 
LLPFKKGAFY LAIQAQVPII PVVYSSFSSF YNVKTKLFTS GTIKVQVLDA VPTNGLTDAD 

       250        260        270 
VTKLVDTCYQ SMRATFLQIS QIPQENSAIK EPGVLPAQ

Q8K3K7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools