Q3TFD2 · PCAT1_MOUSE
- ProteinLysophosphatidylcholine acyltransferase 1
- GeneLpcat1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids534 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- 1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoAThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-O-hexadecyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-O-hexadecyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoAThis 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 + CoAThis 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) + CoAThis reaction proceeds in the forward direction.
- 1-dodecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-dodecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-tetradecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-tetradecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-O-octadecyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-O-octadecyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-octadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-eicosanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-eicosanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + hexanoyl-CoA = 1-hexadecanoyl-2-hexanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + octanoyl-CoA = 1-hexadecanoyl-2-octanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + decanoyl-CoA = 1-hexadecanoyl-2-decanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + dodecanoyl-CoA = 1-hexadecanoyl-2-dodecanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + tetradecanoyl-CoA = 1-hexadecanoyl-2-tetradecanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + CoAThis 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 + CoAThis 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 + CoAThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-hexadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphocholine + eicosanoyl-CoA = 1-hexadecanoyl-2-eicosanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- 1-O-hexadecyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- a 1-acyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-acyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoAThis reaction proceeds in the forward direction.
- a 1-acyl-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-acyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoAThis 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) + CoAThis 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).
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 μM | 1-palmitoyl-LPC | |||||
3 μM | palmitoyl-CoA |
pH Dependence
Optimum pH is 7.5.
Pathway
Lipid metabolism; phospholipid metabolism.
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameLysophosphatidylcholine acyltransferase 1
- EC number
- Short namesLPC acyltransferase 1; LPCAT-1; LysoPC acyltransferase 1; mLPCAT1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ3TFD2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-57 | Cytoplasmic | ||||
Sequence: MRLRGRGPRAAPSSSSGAGDARRLAPPGRNPFVHELRLSALQKAQVAFMTLTLFPIR | ||||||
Transmembrane | 58-78 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LLFAAFMMLLAWPFALLASLG | ||||||
Topological domain | 79-534 | Lumenal | ||||
Sequence: PPDKEPEQPLALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNKLDTITWTWQGPGALKILWLTLCQFQNQVEIEFLPVYCPSEEEKRNPALYASNVRRVMAKALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPENLEKDLDKYSESARMKRGEKIRLPEFAAYLEVPVSDALEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTLATIQLAFKMYGSPEDGSIDEANLSCILKTALGVSELTVTDLFQAIDQEDKGRITFDDFCGFAEMYPDYAEDYLYPDQTHFDSCAQTPPAPTPNGFCIDFSPENSDFGRKNSCKKAD |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 135 | Loss of activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 135-140 | Abolishes activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 140 | Loss of activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 160 | No effect on activity for acetyl-CoA. Reduced activity for palmitoyl-CoA. | ||||
Sequence: I → A | ||||||
Mutagenesis | 162 | Greatly reduced activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 163 | Greatly reduced activity. | ||||
Sequence: W → A | ||||||
Mutagenesis | 164 | Slightly increased activity. | ||||
Sequence: G → A | ||||||
Mutagenesis | 164-177 | Abolishes activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 166 | Greatly reduced activity. | ||||
Sequence: L → A | ||||||
Mutagenesis | 167 | Slightly reduced activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 168 | Reduced activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 169 | Slightly reduced activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 170 | Slightly reduced activity. | ||||
Sequence: I → A | ||||||
Mutagenesis | 171 | Reduced activity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 173 | Greatly reduced activity. | ||||
Sequence: V → A | ||||||
Mutagenesis | 174 | Loss of lyso-PAFAT activity. LPCAT activity is partially reduced. | ||||
Sequence: F → A | ||||||
Mutagenesis | 175 | No activity for acetyl-CoA. Activity for palmitoyl-CoA decreased. | ||||
Sequence: V → A | ||||||
Mutagenesis | 177 | Loss of lyso-PAFAT activity. LPCAT activity is partially reduced. | ||||
Sequence: R → A | ||||||
Mutagenesis | 203-209 | Abolishes activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 208 | Loss of activity. | ||||
Sequence: E → A | ||||||
Mutagenesis | 209 | Reduced activity. | ||||
Sequence: G → A | ||||||
Mutagenesis | 227 | Reduced activity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 227-233 | Abolishes activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 230 | Reduced activity. | ||||
Sequence: P → A | ||||||
Mutagenesis | 233 | Reduced activity. | ||||
Sequence: P → A |
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.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000247065 | 1-534 | Lysophosphatidylcholine acyltransferase 1 | |||
Sequence: MRLRGRGPRAAPSSSSGAGDARRLAPPGRNPFVHELRLSALQKAQVAFMTLTLFPIRLLFAAFMMLLAWPFALLASLGPPDKEPEQPLALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNKLDTITWTWQGPGALKILWLTLCQFQNQVEIEFLPVYCPSEEEKRNPALYASNVRRVMAKALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPENLEKDLDKYSESARMKRGEKIRLPEFAAYLEVPVSDALEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTLATIQLAFKMYGSPEDGSIDEANLSCILKTALGVSELTVTDLFQAIDQEDKGRITFDDFCGFAEMYPDYAEDYLYPDQTHFDSCAQTPPAPTPNGFCIDFSPENSDFGRKNSCKKAD |
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
Structure
Family & Domains
Features
Showing features for region, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-25 | Disordered | ||||
Sequence: MRLRGRGPRAAPSSSSGAGDARRLA | ||||||
Motif | 135-140 | HXXXXD motif | ||||
Sequence: HSSYFD | ||||||
Domain | 379-414 | EF-hand 1 | ||||
Sequence: PVSDALEDMFSLFDESGGGEIDLREYVVALSVVCRP | ||||||
Domain | 451-486 | EF-hand 2 | ||||
Sequence: VSELTVTDLFQAIDQEDKGRITFDDFCGFAEMYPDY | ||||||
Motif | 531-534 | Di-lysine motif | ||||
Sequence: KKAD |
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
Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length534
- Mass (Da)59,744
- Last updated2005-10-11 v1
- Checksum50C1EF4A5D494DF2
Q3TFD2-2
- Name2
- Differences from canonical
- 1-48: Missing
Q3TFD2-3
- Name3
- Differences from canonical
- 1-203: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_019914 | 1-48 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_019913 | 1-203 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 25 | in Ref. 3; BAC38353 | ||||
Sequence: A → T | ||||||
Sequence conflict | 101 | in Ref. 4; AAH66809 | ||||
Sequence: A → T | ||||||
Sequence conflict | 232 | in Ref. 3; BAE42540 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 272 | in Ref. 4; AAH66809 | ||||
Sequence: E → G | ||||||
Sequence conflict | 338 | in Ref. 3; BAC32594/BAC32760 | ||||
Sequence: V → M | ||||||
Sequence conflict | 442 | in Ref. 4; AAH66809 | ||||
Sequence: S → P |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |