NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1104/pp.120.3.913; PubMed=10398728 [NCBI, ExPASy, EBI, Israel, Japan]
Bourgis F., Kader J.-C., Barret P., Renard M., Robinson D., Robinson C., Delseny M., Roscoe T.J.;
"A plastidial lysophosphatidic acid acyltransferase from oilseed rape.";
Plant Physiol. 120:913-922(1999).

Comments

FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. Has preference for C-16-CoA substrates compared to C-18-CoA substrates.
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: Plastid, chloroplast membrane; Multi-pass membrane protein.
TISSUE SPECIFICITY: Ubiquitously expressed.
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

AF111161; AAF73736.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q9LLY4.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
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 electronic annotation from InterPro).
GO:0008654;	Biological process: phospholipid biosynthetic process (inferred from electronic annotation from InterPro).
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

Q9LLY4.

Other

UniRef

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

Keywords

Acyltransferase; Chloroplast; Membrane; Phospholipid biosynthesis; Plastid; Transferase; Transit peptide; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 87`	`87`	`Chloroplast (Potential).`
`CHAIN`	`88 344`	`257`	`1-acyl-sn-glycerol-3-phosphate acyltransferase 1, chloroplastic.`	`PRO_0000024702`
`TRANSMEM`	`113 133`	`21`	`Potential.`
`TRANSMEM`	`210 230`	`21`	`Potential.`
`MOTIF`	`188 193`	`6`	`HXXXXD motif.`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 37998 Da [This is the MW of the unprocessed precursor]

CRC64: B666D9C8AA09AB33 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDVASARGVS SHPPYYSKPI CSSQSSLIRI PISKGCCFAR SSNLITSLHA ASRGVTRRTS 

        70         80         90        100        110        120 
GVQWCYRSIR FDPFKVNDKN SRTVTVRSDL SGAATPESTY PEPEIKLSSR LRGICFCLVA 

       130        140        150        160        170        180 
GISAIVLIVL MIIGHPFVLL FDRYRRKFHH FIAKLWASIS IYPFYKTDIQ GLENLPSSDT 

       190        200        210        220        230        240 
PCVYVSNHQS FLDIYTLLSL GQSYKFISKT GIFVIPVIGW AMSMMGVVPL KRMDPRSQVD 

       250        260        270        280        290        300 
CLKRCMELVK KGASVFFFPE GTRSKDGRLG PFKKGAFTIA AKTGVPVVPI TLMGTGKIMP 

       310        320        330        340 
TGSEGILNHG DVRVIIHKPI YGSKADVLCE EARNKIAESM NLLS

Q9LLY4 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