Q9SHJ5 · GPAT1_ARATH

Function

function

Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Involved in pollen development, by being required for tapetum differentiation and male fertility. In addition to the sporophytic effect, it also exerts a gametophytic effect on pollen performance.

Catalytic activity

Kinetics

Vmax pH TEMPERATURE[C] NOTES EVIDENCE
217.42 pmol/min/mg

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.

GO annotations

AspectTerm
Cellular Componentmembrane
Cellular Componentmitochondrion
Molecular Functionglycerol-3-phosphate 2-O-acyltransferase activity
Molecular Functionglycerol-3-phosphate O-acyltransferase activity
Molecular Functionsn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity
Biological ProcessCDP-diacylglycerol biosynthetic process
Biological Processpollen sperm cell differentiation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glycerol-3-phosphate acyltransferase 1
  • EC number
  • Short names
    AtGPAT1

Gene names

    • Name
      GPAT1
    • ORF names
      F12K11.15
    • Ordered locus names
      At1g06520

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
    Q9SHJ5
  • Secondary accessions
    • Q8L8V5

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Membrane
; Multi-pass membrane protein
Mitochondrion
Note: According to PubMed:12897259 it is mitochondrial. However, no clear transit peptide is predicted by sequence analysis tools.

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane126-146Helical
Transmembrane334-354Helical
Transmembrane356-376Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Plants display a massive pollen development arrest due to a perturbed degeneration of the tapetum, which is associated with altered endoplasmic reticulum profiles and reduced secretion. Defects correlate with several fatty acid composition changes in flower tissues and seeds. However, no significant change in seed oil content is observed.

Variants

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

The viewer provides 28 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001952491-585Glycerol-3-phosphate acyltransferase 1

Proteomic databases

Expression

Tissue specificity

Highly expressed in developing siliques and flower buds. Weakly or not expressed in roots, seedlings and leaves.

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif403-408HXXXXD 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

Belongs to the GPAT/DAPAT family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    585
  • Mass (Da)
    66,514
  • Last updated
    2000-05-01 v1
  • Checksum
    3F7FDCE161C28EAF
MVLPELLVILAEWVLYRLLAKSCYRAARKLRGYGFQLKNLLSLSKTQSLHNNSQHHLHNHHQQNHPNQTLQDSLDPLFPSLTKYQELLLDKNRACSVSSDHYRDTFFCDIDGVLLRQHSSKHFHTFFPYFMLVAFEGGSIIRAILLLLSCSFLWTLQQETKLRVLSFITFSGLRVKDMDNVSRSVLPKFFLENLNIQVYDIWARTEYSKVVFTSLPQVLVERFLREHLNADDVIGTKLQEIKVMGRKFYTGLASGSGFVLKHKSAEDYFFDSKKKPALGIGSSSSPQDHIFISICKEAYFWNEEESMSKNNALPRERYPKPLIFHDGRLAFLPTPLATLAMFIWLPIGFLLAVFRISVGVFLPYHVANFLASMSGVRITFKTHNLNNGRPEKGNSGVLYVCNHRTLLDPVFLTTSLGKPLTAVTYSLSKFSEFIAPLKTVSLKRDRKKDGEAMQRLLSKGDLVVCPEGTTCREPYLLRFSPLFAELTEDIVPVAVDARVSMFYGTTASGLKCLDPIFFLMNPRPVYCLEILKKLPKEMTCAGGKSSFEVANFIQGELARVLGFECTNLTRRDKYLVLAGNEGIVR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict21in Ref. 3; AAM67097
Sequence conflict270in Ref. 3; AAM67097

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC007592
EMBL· GenBank· DDBJ
AAF24816.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE28001.1
EMBL· GenBank· DDBJ
Genomic DNA
AY088785
EMBL· GenBank· DDBJ
AAM67097.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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