Q8GXU8 · LPAT1_ARATH

Function

function

Plastidial enzyme of the prokaryotic glycerol-3-phosphate pathway that converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at position sn-2 (PubMed:15169931).
Utilizes palmitoyl-ACP (16:0-ACP) to produce phosphatidic acid containing a saturated group at position sn-2, which is characteristic of lipids synthesized by the prokaryotic pathway (PubMed:15169931).
In vitro, can use 16:0-CoA as acyl donor (PubMed:14976237).
Essential for embryo development during the transition from the globular to the heart stage when chloroplasts begin to form (PubMed:14976237, PubMed:15169931).

Catalytic activity

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.

GO annotations

AspectTerm
Cellular Componentchloroplast
Cellular Componentchloroplast envelope
Cellular Componentchloroplast membrane
Cellular Componentplasma membrane
Cellular Componentplastid
Molecular Function1-acylglycerol-3-phosphate O-acyltransferase activity
Biological ProcessCDP-diacylglycerol biosynthetic process
Biological Processembryo development ending in seed dormancy
Biological Processphosphatidylglycerol biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
  • EC number
  • Alternative names
    • Lysophosphatidyl acyltransferase 1
    • Protein EMBRYO DEFECTIVE 1995

Gene names

    • Name
      LPAT1
    • Synonyms
      ATS2
      , EMB1995
      , LPAAT1
    • ORF names
      F17I23.80
    • Ordered locus names
      At4g30580

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q8GXU8
  • Secondary accessions
    • Q9M0A2

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane127-147Helical
Transmembrane224-244Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Embryonic lethality due to embryo development arrest at globular stage.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis230In lpat1-4; suppression of the sensitivity of fab1 mutant plants to low temperature.
Mutagenesis290In lpat1-3; suppression of the sensitivity of fab1 mutant plants to low temperature.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-56Chloroplast
ChainPRO_000002470157-3561-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic

Proteomic databases

Expression

Tissue specificity

Widely expressed. Expressed at higher level in leaves. Expressed at lower level in silique walls compared to leaves.

Developmental stage

Expression transiently increases in siliques 4 hours after flowering.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif202-207HXXXXD motif

Domain

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q8GXU8-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    356
  • Mass (Da)
    39,395
  • Last updated
    2003-03-01 v1
  • Checksum
    27A9EB5EBE028940
MDVASARSISSHPSYYGKPICSSQSSLIRISRDKVCCFGRISNGMTSFTTSLHAVPSEKFMGETRRTGIQWSNRSLRHDPYRFLDKKSPRSSQLARDITVRADLSGAATPDSSFPEPEIKLSSRLRGIFFCVVAGISATFLIVLMIIGHPFVLLFDPYRRKFHHFIAKLWASISIYPFYKINIEGLENLPSSDTPAVYVSNHQSFLDIYTLLSLGKSFKFISKTGIFVIPIIGWAMSMMGVVPLKRMDPRSQVDCLKRCMELLKKGASVFFFPEGTRSKDGRLGSFKKGAFTVAAKTGVAVVPITLMGTGKIMPTGSEGILNHGNVRVIIHKPIHGSKADVLCNEARSKIAESMDL

Q8GXU8-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0135941-144in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL161577
EMBL· GenBank· DDBJ
CAB79776.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE85783.1
EMBL· GenBank· DDBJ
Genomic DNA
AY136460
EMBL· GenBank· DDBJ
AAM97125.1
EMBL· GenBank· DDBJ
mRNA
BT006253
EMBL· GenBank· DDBJ
AAP13361.1
EMBL· GenBank· DDBJ
mRNA
AK118028
EMBL· GenBank· DDBJ
BAC42660.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp