Q3TFD2 · PCAT1_MOUSE

  • Protein
    Lysophosphatidylcholine acyltransferase 1
  • Gene
    Lpcat1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Exhibits both acyltransferase and acetyltransferase activities (PubMed:16704971, PubMed:18156367, PubMed:18285344).
Activity is calcium-independent (PubMed:16704971, PubMed:18285344).
Catalyzes the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:16704971, PubMed:18156367, PubMed:18285344).
Catalyzes the conversion 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity).
Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively (PubMed:16704971, PubMed:18285344).
Involved in platelet-activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF) (PubMed:18285344).
May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology (PubMed:16704971).
Involved in the regulation of lipid droplet number and size (By similarity).

Catalytic activity

  • 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-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
    EC:2.3.1.51 (UniProtKB | ENZYME | Rhea)
  • 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + an acyl-CoA = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphocholine + CoA
    EC:2.3.1.25 (UniProtKB | ENZYME | Rhea)
  • 1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-O-hexadecyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-O-hexadecyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-O-(1Z)-alkenyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA
    This reaction proceeds in the forward direction.
  • 1-dodecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-dodecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-tetradecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-tetradecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-O-octadecyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-O-octadecyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-octadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-eicosanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-eicosanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + hexanoyl-CoA = 1-hexadecanoyl-2-hexanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + octanoyl-CoA = 1-hexadecanoyl-2-octanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + decanoyl-CoA = 1-hexadecanoyl-2-decanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + dodecanoyl-CoA = 1-hexadecanoyl-2-dodecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + tetradecanoyl-CoA = 1-hexadecanoyl-2-tetradecanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • (9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-hexadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-hexadecanoyl-sn-glycero-3-phosphocholine + eicosanoyl-CoA = 1-hexadecanoyl-2-eicosanoyl-sn-glycero-3-phosphocholine + CoA
    This reaction proceeds in the forward direction.
  • 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + 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.
  • a 1-acyl-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-acyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA
    This reaction proceeds in the forward direction.
  • 1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + hexadecanoyl-CoA = 1-acyl-2-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA
    This reaction proceeds in the forward direction.

Activity regulation

Not activated by inflammatory stimulation (PubMed:18285344).
Inhibited by Cu2+, Fe2+, Ca2+ and Mg2+ (PubMed:18156367, PubMed:18285344).
Activity is not affected by Co2+ or Mn2+ (PubMed:18285344).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
2.3 μM1-palmitoyl-LPC
3 μMpalmitoyl-CoA

pH Dependence

Optimum pH is 7.5.

Pathway

Lipid metabolism; phospholipid metabolism.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site392Ca2+ (UniProtKB | ChEBI)
Binding site394Ca2+ (UniProtKB | ChEBI)
Binding site398Ca2+ (UniProtKB | ChEBI)
Binding site403Ca2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular ComponentGolgi apparatus
Cellular ComponentGolgi membrane
Cellular Componentlipid droplet
Cellular Componentmembrane
Cellular Componentplasma membrane
Molecular Function1-acylglycerol-3-phosphate O-acyltransferase activity
Molecular Function1-acylglycerophosphocholine O-acyltransferase activity
Molecular Function1-alkylglycerophosphocholine O-acetyltransferase activity
Molecular Function1-alkylglycerophosphocholine O-acyltransferase activity
Molecular Functioncalcium ion binding
Molecular Functionlysophosphatidic acid acyltransferase activity
Molecular Functionplasmalogen synthase activity
Biological Processnegative regulation of phosphatidylcholine biosynthetic process
Biological Processphosphatidylcholine acyl-chain remodeling
Biological Processphosphatidylcholine biosynthetic process
Biological Processphospholipid biosynthetic process
Biological Processpositive regulation of protein catabolic process
Biological Processprotein catabolic process
Biological Processretina development in camera-type eye
Biological Processsurfactant homeostasis

Keywords

Enzyme and pathway databases

Chemistry

Names & Taxonomy

Protein names

  • Recommended name
    Lysophosphatidylcholine acyltransferase 1
  • EC number
  • Short names
    LPC acyltransferase 1; LPCAT-1; LysoPC acyltransferase 1; mLPCAT1
  • Alternative names
    • 1-acylglycerol-3-phosphate O-acyltransferase (EC:2.3.1.51
      ) . EC:2.3.1.51 (UniProtKB | ENZYME | Rhea)
    • 1-acylglycerophosphocholine O-acyltransferase
    • 1-alkenylglycerophosphocholine O-acyltransferase (EC:2.3.1.25
      ) . EC:2.3.1.25 (UniProtKB | ENZYME | Rhea)
    • 1-alkylglycerophosphocholine O-acetyltransferase (EC:2.3.1.67
      ) . EC:2.3.1.67 (UniProtKB | ENZYME | Rhea)
    • Acetyl-CoA:lyso-platelet-activating factor acetyltransferase (Acetyl-CoA:lyso-PAF acetyltransferase; Lyso-PAF acetyltransferase; LysoPAFAT)
    • Acyltransferase-like 2

Gene names

    • Name
      Lpcat1
    • Synonyms
      Aytl2

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • NOD
    • Czech II
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q3TFD2
  • Secondary accessions
    • Q3TAX4
    • Q6NXZ6
    • Q8BG23
    • Q8BUX7
    • Q99JU6

Proteomes

Organism-specific databases

Subcellular Location

Endoplasmic reticulum membrane
; Single-pass type II membrane protein
Golgi apparatus membrane
; Single-pass type II membrane protein
Cell membrane
; Single-pass type II membrane protein
Lipid droplet
Note: May adopt a monotopic topology when embedded in the lipid monolayer of the lipid droplet, with both termini exposed to the cytoplasm.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-57Cytoplasmic
Transmembrane58-78Helical; Signal-anchor for type II membrane protein
Topological domain79-534Lumenal

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis135Loss of activity.
Mutagenesis135-140Abolishes activity.
Mutagenesis140Loss of activity.
Mutagenesis160No effect on activity for acetyl-CoA. Reduced activity for palmitoyl-CoA.
Mutagenesis162Greatly reduced activity.
Mutagenesis163Greatly reduced activity.
Mutagenesis164Slightly increased activity.
Mutagenesis164-177Abolishes activity.
Mutagenesis166Greatly reduced activity.
Mutagenesis167Slightly reduced activity.
Mutagenesis168Reduced activity.
Mutagenesis169Slightly reduced activity.
Mutagenesis170Slightly reduced activity.
Mutagenesis171Reduced activity.
Mutagenesis173Greatly reduced activity.
Mutagenesis174Loss of lyso-PAFAT activity. LPCAT activity is partially reduced.
Mutagenesis175No activity for acetyl-CoA. Activity for palmitoyl-CoA decreased.
Mutagenesis177Loss of lyso-PAFAT activity. LPCAT activity is partially reduced.
Mutagenesis203-209Abolishes activity.
Mutagenesis208Loss of activity.
Mutagenesis209Reduced activity.
Mutagenesis227Reduced activity.
Mutagenesis227-233Abolishes activity.
Mutagenesis230Reduced activity.
Mutagenesis233Reduced activity.

Variants

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

The viewer provides 32 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_00002470651-534Lysophosphatidylcholine acyltransferase 1

Proteomic databases

PTM databases

Expression

Tissue specificity

Predominantly expressed in lung where it is enriched in alveolar type II cells. Expressed at lower levels in spleen and brain. Also detected in erythroleukemic cells and reticulocytes. Weakly or not expressed in other tissues.

Induction

Constitutively expressed. Not induced by inflammatory stimulation.

Developmental stage

Expression increases steadily throughout embryogenesis and decreases slightly in the adult.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, motif, domain.

TypeIDPosition(s)Description
Region1-25Disordered
Motif135-140HXXXXD motif
Domain379-414EF-hand 1
Domain451-486EF-hand 2
Motif531-534Di-lysine motif

Domain

The di-lysine motif may confer endoplasmic reticulum localization.
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphocholine.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q3TFD2-1

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
    534
  • Mass (Da)
    59,744
  • Last updated
    2005-10-11 v1
  • Checksum
    50C1EF4A5D494DF2
MRLRGRGPRAAPSSSSGAGDARRLAPPGRNPFVHELRLSALQKAQVAFMTLTLFPIRLLFAAFMMLLAWPFALLASLGPPDKEPEQPLALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNKLDTITWTWQGPGALKILWLTLCQFQNQVEIEFLPVYCPSEEEKRNPALYASNVRRVMAKALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPENLEKDLDKYSESARMKRGEKIRLPEFAAYLEVPVSDALEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTLATIQLAFKMYGSPEDGSIDEANLSCILKTALGVSELTVTDLFQAIDQEDKGRITFDDFCGFAEMYPDYAEDYLYPDQTHFDSCAQTPPAPTPNGFCIDFSPENSDFGRKNSCKKAD

Q3TFD2-2

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

Q3TFD2-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D6RFA8D6RFA8_MOUSELpcat146
D6RE48D6RE48_MOUSELpcat177

Sequence caution

The sequence AAH05662.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAC32594.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAC32760.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0199141-48in isoform 2
Alternative sequenceVSP_0199131-203in isoform 3
Sequence conflict25in Ref. 3; BAC38353
Sequence conflict101in Ref. 4; AAH66809
Sequence conflict232in Ref. 3; BAE42540
Sequence conflict272in Ref. 4; AAH66809
Sequence conflict338in Ref. 3; BAC32594/BAC32760
Sequence conflict442in Ref. 4; AAH66809

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB244717
EMBL· GenBank· DDBJ
BAE94687.2
EMBL· GenBank· DDBJ
mRNA
AK046079
EMBL· GenBank· DDBJ
BAC32594.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK046507
EMBL· GenBank· DDBJ
BAC32760.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK081865
EMBL· GenBank· DDBJ
BAC38353.1
EMBL· GenBank· DDBJ
mRNA
AK155286
EMBL· GenBank· DDBJ
BAE33166.1
EMBL· GenBank· DDBJ
mRNA
AK169190
EMBL· GenBank· DDBJ
BAE40966.1
EMBL· GenBank· DDBJ
mRNA
AK170723
EMBL· GenBank· DDBJ
BAE41980.1
EMBL· GenBank· DDBJ
mRNA
AK171582
EMBL· GenBank· DDBJ
BAE42540.1
EMBL· GenBank· DDBJ
mRNA
BC005662
EMBL· GenBank· DDBJ
AAH05662.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC066809
EMBL· GenBank· DDBJ
AAH66809.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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