M1EM31 · M1EM31_MUSPF

Function

function

Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided it contains an arachidonoyl group. Also involved in the production of alkyl-lysophosphatidic acid, another bioactive lipid, through the phosphorylation of 1-alkyl-2-acetyl glycerol.

Catalytic activity

  • 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • 1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • 1,2-dihexadecanoyl-sn-glycerol + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • 1-O-alkyl-2-acyl-sn-glycerol + ATP = 1-O-alkyl-2-acyl-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • a 1-O-alkyl-sn-glycerol + ATP = a 1-O-alkyl-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
    EC:2.7.1.93 (UniProtKB | ENZYME | Rhea)
  • 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • 1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • 1-O-hexadecyl-2-acetyl-sn-glycerol + ATP = 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • 1-O-hexadecyl-sn-glycerol + ATP = 1-O-hexadecyl-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • 2-(9Z-octadecenoyl)-glycerol + ATP = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
  • a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H+
    This reaction proceeds in the forward direction.
    EC:2.7.1.107 (UniProtKB | ENZYME | Rhea)

Pathway

Lipid metabolism; glycerolipid metabolism.

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular FunctionATP-dependent diacylglycerol kinase activity
Molecular Functioncalcium ion binding
Biological Processdiacylglycerol metabolic process
Biological Processintracellular signal transduction
Biological Processlipid phosphorylation
Biological Processphospholipase C-activating G protein-coupled receptor signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Diacylglycerol kinase alpha
  • EC number
  • Alternative names
    • Diglyceride kinase alpha

Organism names

Accessions

  • Primary accession
    M1EM31

Subcellular Location

PTM/Processing

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain108-143EF-hand
Domain153-188EF-hand
Domain203-251Phorbol-ester/DAG-type
Domain267-317Phorbol-ester/DAG-type
Domain370-504DAGKc

Sequence similarities

Belongs to the eukaryotic diacylglycerol kinase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    547
  • Mass (Da)
    61,898
  • Last updated
    2013-05-01 v1
  • Checksum
    30D54B041BAAE281
MAKEKGLISPNDFAQLQKYMEYSTNKVSDVLKLFEDGDMAEYLQGDAIGYEGFQQFLKIYLEADNVPNHLSLALFQSFKMGHLEDTVKNDVVYLSDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDRIIIQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSLAEWLRAGATTVPLLVLLGLEMTLKDNGQHLWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYVVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLVGLHCVWCHLEIHDDCLQAMGHECDCGLLRDHILPPSSIYPSVLASGQERKTSKTSQKTMDDLHLSTFEALRIDPVSNTHPLLVFVNPKSGGKQGERVLWKFQYLLNPRQVFNLLKDGPEPGLRFFRDVPGCRILVCGGDGTVGWILETIDKANMPVVPPVAVLPLGTGNDLARCLRWGGGYEGQNLGKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIMREKYPEKFN

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue547

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JP008574
EMBL· GenBank· DDBJ
AER97171.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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