Lpcat1
entrez
210992
canonical
uniprot
Q3TFD2
canonical
ensembl
ENSMUSG00000021608
resolver
ensp
ENSMUSP00000022099
resolver
genesymbol
Lpcat1
resolver
genesymbol_syn
Aytl2
resolver
uniprot
Q3TAX4
resolver
uniprot
Q6NXZ6
resolver
uniprot
Q8BG23
resolver
uniprot
Q8BUX7
resolver
uniprot
Q99JU6
resolver
uniprot_entry
PCAT1_MOUSE
resolver
uniprot_sec
Q3TAX4
resolver
uniprot_sec
Q6NXZ6
resolver
uniprot_sec
Q8BG23
resolver
uniprot_sec
Q8BUX7
resolver
uniprot_sec
Q99JU6
resolver
activity_regulation
ACTIVITY REGULATION: Not activated by inflammatory stimulation (PubMed:18285344). Inhibited by Cu(2+), Fe(2+), Ca(2+) and Mg(2+) (PubMed:18156367, PubMed:18285344). Activity is not affected by Co(2+) or Mn(2+) (PubMed:18285344). {ECO:0000269|PubMed:18156367, ECO:0000269|PubMed:18285344}.
uniprot
proteins
amino_acid_sequence
MRLRGRGPRAAPSSSSGAGDARRLAPPGRNPFVHELRLSALQKAQVAFMTLTLFPIRLLFAAFMMLLAWPFALLASLGPPDKEPEQPLALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNKLDTITWTWQGPGALKILWLTLCQFQNQVEIEFLPVYCPSEEEKRNPALYASNVRRVMAKALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPENLEKDLDKYSESARMKRGEKIRLPEFAAYLEVPVSDALEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTLATIQLAFKMYGSPEDGSIDEANLSCILKTALGVSELTVTDLFQAIDQEDKGRITFDDFCGFAEMYPDYAEDYLYPDQTHFDSCAQTPPAPTPNGFCIDFSPENSDFGRKNSCKKAD
uniprot
proteins
ec_number
2.3.1.23
uniprot
proteins
ec_number
2.3.1.25
uniprot
proteins
ec_number
2.3.1.51
uniprot
proteins
ec_number
2.3.1.67
uniprot
proteins
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). {ECO:0000250|UniProtKB:Q1HAQ0, ECO:0000250|UniProtKB:Q8NF37, ECO:0000269|PubMed:16704971, ECO:0000269|PubMed:18156367, ECO:0000269|PubMed:18285344}.
uniprot
proteins
mass_dalton
59744
uniprot
proteins
mutagenesis
MUTAGEN 135..140; /note="Missing: Abolishes activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 135; /note="H->A: Loss of activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 140; /note="D->A: Loss of activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 160; /note="I->A: No effect on activity for acetyl-CoA. Reduced activity for palmitoyl-CoA."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 162; /note="I->A: Greatly reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 163; /note="W->A: Greatly reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 164..177; /note="Missing: Abolishes activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 164; /note="G->A: Slightly increased activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 166; /note="L->A: Greatly reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 167; /note="I->A: Slightly reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 168; /note="R->A: Reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 169; /note="Y->A: Slightly reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 170; /note="I->A: Slightly reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 171; /note="R->A: Reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 173; /note="V->A: Greatly reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 174; /note="F->A: Loss of lyso-PAFAT activity. LPCAT activity is partially reduced."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 175; /note="V->A: No activity for acetyl-CoA. Activity for palmitoyl-CoA decreased."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 177; /note="R->A: Loss of lyso-PAFAT activity. LPCAT activity is partially reduced."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 203..209; /note="Missing: Abolishes activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 208; /note="E->A: Loss of activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 209; /note="G->A: Reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 227..233; /note="Missing: Abolishes activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 227; /note="P->A: Reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 230; /note="P->A: Reduced activity."; /evidence="ECO:0000269|PubMed:18285344"; MUTAGEN 233; /note="P->A: Reduced activity."; /evidence="ECO:0000269|PubMed:18285344
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; phospholipid metabolism.
uniprot
proteins
protein_family
1-acyl-sn-glycerol-3-phosphate acyltransferase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16704971
uniprot
proteins
pubmed
16864775
uniprot
proteins
pubmed
18156367
uniprot
proteins
pubmed
18285344
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
534
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16704971}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8NF37}. Golgi apparatus membrane {ECO:0000269|PubMed:16704971}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8NF37}. Cell membrane {ECO:0000305|PubMed:18156367}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8NF37}. Lipid droplet {ECO:0000250|UniProtKB:Q8NF37}. Note=May adopt a monotopic topology when embedded in the lipid monolayer of the lipid droplet, with both termini exposed to the cytoplasm. {ECO:0000250|UniProtKB:Q8NF37}.
uniprot
proteins
transmembrane_region
TRANSMEM 58..78; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins