LMPD Database

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LMP006804

UniProt Annotations

Entry Information
Gene Namelysophosphatidylcholine acyltransferase 3
Protein EntryQ6P1A2_HUMAN
UniProt IDQ6P1A2
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q6P1A2-1; Sequence=Displayed; Name=2; IsoId=Q6P1A2-2; Sequence=VSP_053680; Note=No experimental confirmation available.;
Biophysicochemical PropertiesKinetic parameters: KM=41.29 uM for palmitoyl-CoA ; KM=36.65 uM for stearoyl-CoA ; KM=72.68 uM for oleoyl-CoA ; KM=201.4 uM for linoleoyl-CoA ; KM=71.56 uM for arachidonoyl-CoA ; KM=72.19 uM for 1-palmitoyl-lysophosphatidylcholine ; Vmax=1782 nmol/min/mg enzyme with palmitoyl-CoA and 1-palmitoyl- lysophosphatidylcholine as substrates ; Vmax=996 nmol/min/mg enzyme with stearoyl-CoA and 1-palmitoyl- lysophosphatidylcholine as substrates ; Vmax=4698 nmol/min/mg enzyme with oleoyl-CoA and 1-palmitoyl- lysophosphatidylcholine as substrates ; Vmax=18148 nmol/min/mg enzyme with linoleoyl-CoA and 1- palmitoyl-lysophosphatidylcholine as substrates ; Vmax=6247 nmol/min/mg enzyme with arachidonoyl-CoA and 1- palmitoyl-lysophosphatidylcholine as substrates ;
Catalytic ActivityAcyl-CoA + 1-acyl-sn-glycero-3- phosphatidylserine = CoA + 1,2-diacyl-sn-glycero-3- phosphatidylserine.
Catalytic ActivityAcyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
DomainThe di-lysine motif confers endoplasmic reticulum localization.
Enzyme RegulationActivity is inhibited by thimerosal.
FunctionAcyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3- phosphocholine or PC) (LPCAT activity). Catalyzes also the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero- 3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn- glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak lysophosphatidylethanolamine acyltransferase activity (LPEAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle. {ECO
PathwayLipid metabolism; phospholipid metabolism.
Sequence CautionSequence=AAB51326.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence= ; Sequence=AAC51640.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence= ; Sequence=BAG37917.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence= ;
SimilarityBelongs to the membrane-bound acyltransferase family.
Subcellular LocationEndoplasmic reticulum membrane ; Multi-pass membrane protein .
Tissue SpecificityHighly expressed in liver, pancreas and adipose tissue. Very low expression in skeletal muscle and heart. Detected in neutrophils. {ECO