Q643R3 · LPCT4_HUMAN

  • Protein
    Lysophospholipid acyltransferase LPCAT4
  • Gene
    LPCAT4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-lysophatidylethanolamine to 1-alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl-phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors.

Catalytic activity

  • a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA
    EC:2.3.1.n7 (UniProtKB | ENZYME | Rhea)
  • 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + an acyl-CoA = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + CoA
    EC:2.3.1.121 (UniProtKB | ENZYME | Rhea)
  • a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA
    EC:2.3.1.23 (UniProtKB | ENZYME | Rhea)
  • 1-O-alkyl-sn-glycero-3-phosphocholine + acetyl-CoA = a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + CoA
    EC:2.3.1.67 (UniProtKB | ENZYME | Rhea)
  • a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CoA
    EC:2.3.1.n6 (UniProtKB | ENZYME | Rhea)
  • a 1-acyl-sn-glycero-3-phosphoethanolamine + octanoyl-CoA = 1-acyl-2-octanoyl-sn-glycero-3-phosphoethanolamine + CoA
    This reaction proceeds in the forward direction.
  • a 1-acyl-sn-glycero-3-phosphoethanolamine + hexadecanoyl-CoA = 1-acyl-2-hexadecanoyl-sn-glycero-3-phosphoethanolamine + CoA
    This reaction proceeds in the forward direction.
  • a 1-acyl-sn-glycero-3-phosphoethanolamine + octadecanoyl-CoA = 1-acyl-2-octadecanoyl-sn-glycero-3-phosphoethanolamine + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-phosphoethanolamine = 1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphoethanolamine + CoA
    This reaction proceeds in the forward direction.
  • (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-phosphoethanolamine = 1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + CoA
    This reaction proceeds in the forward direction.
  • 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + octanoyl-CoA = 1-O-(1Z)-alkenyl-2-octanoyl-sn-glycero-3-phosphoethanolamine + CoA
    This reaction proceeds in the forward direction.
  • 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + hexadecanoyl-CoA = 1-O-(1Z)-alkenyl-2-hexadecanoyl-sn-glycero-3-phosphoethanolamine + CoA
    This reaction proceeds in the forward direction.
  • 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + octadecanoyl-CoA = 1-O-(1Z)-alkenyl-2-octadecanoyl-sn-glycero-3-phosphoethanolamine + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphoethanolamine + CoA
    This reaction proceeds in the forward direction.
  • (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + CoA
    This reaction proceeds in the forward direction.
  • a 1-acyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-acyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-phosphocholine = 1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-octadecenoyl-CoA + 1-O-hexadecyl-sn-glycero-3-phosphocholine = 1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-hexadecyl-sn-glycero-3-phosphocholine = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phospho-L-serine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA
    This reaction proceeds in the forward direction.
  • (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA
    This reaction proceeds in the forward direction.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
80 μMlysophosphatidylethanolamine
20 μMoleoyl-CoA
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
270 pmol/min/mgwith lysophosphatidylethanolamine and oleoyl-CoA as substrates

Pathway

Lipid metabolism; phospholipid metabolism.

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular Componentmembrane
Molecular Function1-acylglycerol-3-phosphate O-acyltransferase activity
Molecular Function1-acylglycerophosphocholine O-acyltransferase activity
Molecular Function1-acylglycerophosphoethanolamine O-acyltransferase activity
Molecular Function1-acylglycerophosphoserine O-acyltransferase activity
Molecular Function1-alkenylglycerophosphoethanolamine O-acyltransferase activity
Molecular Function1-alkylglycerophosphocholine O-acetyltransferase activity
Molecular Function2-acylglycerol-3-phosphate O-acyltransferase activity
Molecular Functionlysophosphatidic acid acyltransferase activity
Molecular Functionlysophospholipid acyltransferase activity
Biological Processphosphatidic acid biosynthetic process
Biological Processphosphatidylcholine acyl-chain remodeling
Biological Processphosphatidylethanolamine acyl-chain remodeling
Biological Processphosphatidylglycerol acyl-chain remodeling
Biological Processphosphatidylserine acyl-chain remodeling
Biological Processphospholipid metabolic process

Keywords

Enzyme and pathway databases

Chemistry

Names & Taxonomy

Protein names

  • Recommended name
    Lysophospholipid acyltransferase LPCAT4
  • Alternative names
    • 1-acylglycerol-3-phosphate O-acyltransferase 7 (1-AGP acyltransferase 7; 1-AGPAT 7)
    • 1-acylglycerophosphocholine O-acyltransferase (EC:2.3.1.23
      ) . EC:2.3.1.23 (UniProtKB | ENZYME | Rhea)
    • 1-acylglycerophosphoserine O-acyltransferase (EC:2.3.1.n6
      ) . EC:2.3.1.n6 (UniProtKB | ENZYME | Rhea)
    • 1-alkenylglycerophosphoethanolamine O-acyltransferase (EC:2.3.1.121
      ) . EC:2.3.1.121 (UniProtKB | ENZYME | Rhea)
    • 1-alkylglycerophosphocholine O-acetyltransferase (EC:2.3.1.67
      ) . EC:2.3.1.67 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      LPCAT4
    • Synonyms
      AGPAT7, AYTL3, LPEAT2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q643R3
  • Secondary accessions
    • A8K2K8
    • O43412
    • Q7Z4P4
    • Q8IUL7
    • Q8TB38

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane40-62Helical
Transmembrane87-107Helical

Keywords

Disease & Variants

Variants

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

The viewer provides 522 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), glycosylation.

TypeIDPosition(s)SourceDescription
ChainPRO_00002470541-524UniProtLysophospholipid acyltransferase LPCAT4
Modified residue (large scale data)2PRIDEPhosphoserine
Modified residue (large scale data)5PRIDEPhosphoserine
Glycosylation152UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)503PRIDEPhosphoserine
Modified residue (large scale data)504PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed with predominant level in brain.

Gene expression databases

Organism-specific databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif, compositional bias, region.

TypeIDPosition(s)Description
Motif129-134HXXXXD motif
Compositional bias489-516Polar residues
Region489-524Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    524
  • Mass (Da)
    57,219
  • Last updated
    2004-10-25 v1
  • Checksum
    3A2A12656E1241BC
MSQGSPGDWAPLDPTPGPPASPNPFVHELHLSRLQRVKFCLLGALLAPIRVLLAFIVLFLLWPFAWLQVAGLSEEQLQEPITGWRKTVCHNGVLGLSRLLFFLLGFLRIRVRGQRASRLQAPVLVAAPHSTFFDPIVLLPCDLPKVVSRAENLSVPVIGALLRFNQAILVSRHDPASRRRVVEEVRRRATSGGKWPQVLFFPEGTCSNKKALLKFKPGAFIAGVPVQPVLIRYPNSLDTTSWAWRGPGVLKVLWLTASQPCSIVDVEFLPVYHPSPEESRDPTLYANNVQRVMAQALGIPATECEFVGSLPVIVVGRLKVALEPQLWELGKVLRKAGLSAGYVDAGAEPGRSRMISQEEFARQLQLSDPQTVAGAFGYFQQDTKGLVDFRDVALALAALDGGRSLEELTRLAFELFAEEQAEGPNRLLYKDGFSTILHLLLGSPHPAATALHAELCQAGSSQGLSLCQFQNFSLHDPLYGKLFSTYLRPPHTSRGTSQTPNASSPGNPTALANGTVQAPKQKGD

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
H3BMK4H3BMK4_HUMANLPCAT484

Sequence caution

The sequence AAC19156.1 differs from that shown. Reason: Frameshift
The sequence AAC19156.1 differs from that shown. Reason: Miscellaneous discrepancy Probable cloning artifact.
The sequence AAN33178.1 differs from that shown. Reason: Frameshift
The sequence AAP97722.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias489-516Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY734233
EMBL· GenBank· DDBJ
AAU34184.1
EMBL· GenBank· DDBJ
mRNA
AF529233
EMBL· GenBank· DDBJ
AAP97722.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AF542964
EMBL· GenBank· DDBJ
AAN33178.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AK290273
EMBL· GenBank· DDBJ
BAF82962.1
EMBL· GenBank· DDBJ
mRNA
CH471125
EMBL· GenBank· DDBJ
EAW92306.1
EMBL· GenBank· DDBJ
Genomic DNA
BC024892
EMBL· GenBank· DDBJ
AAH24892.2
EMBL· GenBank· DDBJ
mRNA
BC092463
EMBL· GenBank· DDBJ
AAH92463.1
EMBL· GenBank· DDBJ
mRNA
AF007155
EMBL· GenBank· DDBJ
AAC19156.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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