[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1074/jbc.272.32.20299; PubMed=9242711 [NCBI, ExPASy, EBI, Israel, Japan] Eberhardt C., Gray P.W., Tjoelker L.W.; "Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and localization to chromosome 9q34.3."; J. Biol. Chem. 272:20299-20305(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). PubMed=9291118 [NCBI, ExPASy, EBI, Israel, Japan] Stamps A.C., Elmore M.A., Hill M.E., Kelly K., Makda A.A., Finnen M.J.; "A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases."; Biochem. J. 326:455-461(1997).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). PubMed=9212163 [NCBI, ExPASy, EBI, Israel, Japan] West J., Tompkins C.K., Balantac N., Nudelman E., Meengs B., White T., Bursten S., Coleman J., Kumar A., Singer J.W., Leung D.W.; "Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells."; DNA Cell Biol. 16:691-701(1997).
[4]	SEQUENCE REVISION TO 51. Leung D.W., Tompkin C.K., West J.; Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). TISSUE=Kidney, and Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	REVIEW. DOI=10.1056/NEJMra025261; PubMed=15028826 [NCBI, ExPASy, EBI, Israel, Japan] Garg A.; "Acquired and inherited lipodystrophies."; N. Engl. J. Med. 350:1220-1234(2004).
[7]	VARIANTS CGL1 ARG-136; PHE-140 DEL; PRO-228 AND VAL-239. 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).

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).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	O15120-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	O15120-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_005071.

TISSUE SPECIFICITY: Expressed predominantly in heart and liver.
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).
DISEASE: Defects in AGPAT2 are the cause of congenital generalized lipodystrophy type 1 (CGL1) [MIM:608594]; also known as Berardinelli-Seip congenital lipodystrophy type 1 (BSCL1) or Berardinelli-Seip syndrome. CGL1 is an autosomal recessive disorder characterized by marked paucity of adipose tissue, extreme insulin resistance, hypertriglyceridemia, hepatic steatosis and early onset of diabetes.
SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=AGPAT2";.

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

AF000237; AAC51649.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF011374; AAB64299.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U56418; AAB58776.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000026; AAH00026.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004529; AAH04529.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00221372; -.
IPI00464993; -.

RefSeq

NP_001012745.1; -.
NP_006403.2; -.

UniGene

Hs.320151

3D structure databases

ModBase

O15120.

PTM databases

PhosphoSite

O15120; -.

Enzyme and pathway databases

BRENDA

2.3.1.51; 247.

Reactome

REACT_602; Lipid and lipoprotein metabolism.

Organism-specific databases

GC09M138687; -.

HIX0008552; -.

HGNC:325; AGPAT2.

603100; gene. [NCBI / EBI]
608594; phenotype. [NCBI / EBI]

Orphanet

528; Lipodystrophy, Berardinelli type.

PharmGKB

PA24622; -.

Gene expression databases

Bgee

O15120; -.

CleanEx

HS_AGPAT2; -.

GermOnline

ENSG00000169692; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005783;	Cellular component: endoplasmic reticulum (inferred from sequence or structural similarity 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 (non-traceable author statement from UniProtKB).
GO:0046027;	Molecular function: phospholipid:diacylglycerol acyltransferase activity (inferred from experiment from Reactome).
GO:0006654;	Biological process: phosphatidic acid biosynthetic process (inferred from genetic interaction from UniProtKB).
GO:0001819;	Biological process: positive regulation of cytokine production (inferred from mutant phenotype from UniProtKB).
GO:0001961;	Biological process: positive regulation of cytokine-mediated signaling pathway (inferred by curator 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.

Proteomic databases

PRIDE

O15120; -.

Genome annotation databases

Ensembl

ENSG00000169692; Homo sapiens. [Contig view]

GeneID

10555; -.

KEGG

hsa:10555; -.

Phylogenomic databases

HOVERGEN

O15120; -.

OMA

O15120; EGTRNDN.

Other

NextBio

40047; -.

SOURCE

AGPAT2; Homo sapiens.

ProtoNet

O15120.

UniRef

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

Keywords

Acyltransferase; Alternative splicing; Congenital generalized lipodystrophy; Diabetes mellitus; Disease mutation; 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_0000208192`
`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 (By similarity).`
`MOD_RES`	`260 260`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`165 196`		`Missing (in isoform 2).`	`VSP_005071`
`VARIANT`	`136 136`	`1`	`G -> R (in CGL1).`	`VAR_017328`
`VARIANT`	`140 140`	`1`	`Missing (in CGL1).`	`VAR_017326`
`VARIANT`	`228 228`	`1`	`L -> P (in CGL1).`	`VAR_017327`
`VARIANT`	`239 239`	`1`	`A -> V (in CGL1).`	`VAR_017325`
`CONFLICT`	`126 126`		`L -> V (in Ref. 2; AAB64299).`
`CONFLICT`	`200 200`		`V -> F (in Ref. 5; AAH00026).`

Sequence information

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

Molecular weight: 30914 Da [This is the MW of the unprocessed precursor]

CRC64: 1E58F537F703BE9F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MELWPCLAAA LLLLLLLVQL SRAAEFYAKV ALYCALCFTV SAVASLVCLL RHGGRTVENM 

        70         80         90        100        110        120 
SIIGWFVRSF KYFYGLRFEV RDPRRLQEAR PCVIVSNHQS ILDMMGLMEV LPERCVQIAK 

       130        140        150        160        170        180 
RELLFLGPVG LIMYLGGVFF INRQRSSTAM TVMADLGERM VRENLKVWIY PEGTRNDNGD 

       190        200        210        220        230        240 
LLPFKKGAFY LAVQAQVPIV PVVYSSFSSF YNTKKKFFTS GTVTVQVLEA IPTSGLTAAD 

       250        260        270 
VPALVDTCHR AMRTTFLHIS KTPQENGATA GSGVQPAQ

O15120 in FASTA 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