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Q42870 (PLSC_LIMDO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase

Short name=1-AGP acyltransferase
Short name=1-AGPAT
EC=2.3.1.51
Alternative name(s):
Lysophosphatidic acid acyltransferase
Short name=LPAAT
Gene names
Name:PLSC
OrganismLimnanthes douglasii (Douglas's meadowfoam)
Taxonomic identifier28973 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesLimnanthaceaeLimnanthes

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position. This enzyme uses erucoyl-CoA as an acyl donor.

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.

Sequence similarities

Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function1-acylglycerol-3-phosphate O-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2812811-acyl-sn-glycerol-3-phosphate acyltransferase
PRO_0000208187

Regions

Transmembrane40 – 6021Helical; Potential
Transmembrane71 – 9121Helical; Potential
Transmembrane110 – 13021Helical; Potential
Motif109 – 1146HXXXXD motif

Experimental info

Sequence conflict461I → V in CAA86877. Ref.2
Sequence conflict1881R → G in CAA86877. Ref.2
Sequence conflict2621V → I in CAA86877. Ref.2
Sequence conflict2811N → K in CAA86877. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q42870 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9C880BD9E492EE2A

FASTA28131,717
        10         20         30         40         50         60 
MAKTRTSSLR NRRQLKPAVA ATADDDKDGV FMVLLSCFKI FVCFAIVLIT AVAWGLIMVL 

        70         80         90        100        110        120 
LLPWPYMRIR LGNLYGHIIG GLVIWIYGIP IKIQGSEHTK KRAIYISNHA SPIDAFFVMW 

       130        140        150        160        170        180 
LAPIGTVGVA KKEVIWYPLL GQLYTLAHHI RIDRSNPAAA IQSMKEAVRV ITEKNLSLIM 

       190        200        210        220        230        240 
FPEGTRSRDG RLLPFKKGFV HLALQSHLPI VPMILTGTHL AWRKGTFRVR PVPITVKYLP 

       250        260        270        280 
PINTDDWTVD KIDDYVKMIH DVYVRNLPAS QKPLGSTNRS N 

« Hide

References

[1]"A plant acyltransferase involved in triacylglycerol biosynthesis complements an Escherichia coli sn-1-acylglycerol-3-phosphate acyltransferase mutant."
Hanke C., Wolter F.P., Coleman J., Peterek G., Frentzen M.
Eur. J. Biochem. 232:806-810(1995) [PubMed: 7588719] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification of a cDNA that encodes a 1-acyl-sn-glycerol-3-phosphate acyltransferase from Limnanthes douglasii."
Brown A.P., Brough C.L., Kroon J., Slabas A.R.
Plant Mol. Biol. 29:267-278(1995) [PubMed: 7579178] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83266 mRNA. Translation: CAA58239.1.
Z46836 mRNA. Translation: CAA86877.1.
PIRS60477.

3D structure databases

ProteinModelPortalQ42870.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.51. 3028.

Family and domain databases

InterProIPR002123. Acyltransferase.
IPR004552. AGP_acyltrans.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsTIGR00530. AGP_acyltrn. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLSC_LIMDO
AccessionPrimary (citable) accession number: Q42870
Secondary accession number(s): Q40120
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: May 31, 2011
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families