NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Endosperm;
DOI=10.1104/pp.109.3.999; PubMed=8552723 [NCBI, ExPASy, EBI, Israel, Japan]
Knutzon D.S., Lardizabal K.D., Nelsen J.S., Bleibaum J.L., Davies H.M., Metz J.G.;
"Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-phosphate acyltransferase that accepts medium-chain-length substrates.";
Plant Physiol. 109:999-1006(1995).

Comments

FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. This enzyme shows a preference for medium-chain-length fatty acyl-coenzyme a substrates.
CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
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

U29657; AAC49119.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q42670.

Enzyme and pathway databases

BRENDA

2.3.1.51; 118852.

Ontologies

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 EC).
GO:0008654;	Biological process: phospholipid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
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.

Other

ProtoNet

Q42670.

UniRef

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

Keywords

Acyltransferase; Direct protein sequencing; Membrane; Phospholipid biosynthesis; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 308`	`308`	`1-acyl-sn-glycerol-3-phosphate acyltransferase.`	`PRO_0000208185`
`TRANSMEM`	`65 85`	`21`	`Potential.`
`TRANSMEM`	`124 144`	`21`	`Potential.`
`TRANSMEM`	`148 168`	`21`	`Potential.`
`MOTIF`	`130 135`	`6`	`HXXXXD motif.`

Sequence information

Length: 308 AA [This is the length of the unprocessed precursor]

Molecular weight: 34809 Da [This is the MW of the unprocessed precursor]

CRC64: 3773CF8C03C3C0FE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDASGASSFL RGRCLESCFK ASFGMSQPKD AAGQPSRRPA DADDFVDDDR WITVILSVVR 

        70         80         90        100        110        120 
IAACFLSMMV TTIVWNMIML ILLPWPYARI RQGNLYGHVT GRMLMWILGN PITIEGSEFS 

       130        140        150        160        170        180 
NTRAIYICNH ASLVDIFLIM WLIPKGTVTI AKKEIIWYPL FGQLYVLANH QRIDRSNPSA 

       190        200        210        220        230        240 
AIESIKEVAR AVVKKNLSLI IFPEGTRSKT GRLLPFKKGF IHIALQTRLP IVPMVLTGTH 

       250        260        270        280        290        300 
LAWRKNSLRV RPAPITVKYF SPIKTDDWEE EKINHYVEMI HALYVDHLPE SQKPLVSKGR 


DASGRSNS

Q42670 in FASTA format

View entry in raw text format (no links)
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	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