UniProt Accession

 PCAT1_HUMAN; Q8NF37; Q1HAQ1; Q7Z4G6; Q8N3U7; Q8WUL8; Q9GZW6 

Genbank Protein ID

 AB244719; AK090444; BC020166; AK022505; AK022499; AF530061; AL831864 

Genbank Nucleotide ID

 BAE94688.1; BAC03425.1; AAH20166.3; BAB14065.1; BAB14061.1; AAQ09945.1; CAD38556.1 

Protein Name

 Lysophosphatidylcholine acyltransferase 1 

Protein Synonyms/Alias

 LPC acyltransferase 1; LPCAT-1; LysoPC acyltransferase 1; 1-acylglycerophosphocholine O-acyltransferase; 1-alkylglycerophosphocholine O-acetyltransferase; Acetyl-CoA:lyso-platelet-activating factor acetyltransferase; Acetyl-CoA:lyso-PAF acetyltransferase; Lyso-PAF acetyltransferase; LysoPAFAT; Acyltransferase-like 2; Phosphonoformate immuno-associated protein 3 

Gene Name

 LPCAT1 

Gene Synonyms/Alias

 AYTL2; PFAAP3 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
93	QPPALWRKVVDFLLK	ubiquitination	[1]
191	RKTVEEIKRRAQSNG	ubiquitination	[2]
199	RRAQSNGKWPQIMIF	ubiquitination	[2]
221	RTCLITFKPGAFIPG	ubiquitination	[3]
344	LVRGLGLKPEKLEKD	ubiquitination	[2]
347	GLGLKPEKLEKDLDR	ubiquitination	[2]
470	IDQEEKGKITFADFH	ubiquitination	[2]

Reference

 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology. 

Sequence Annotation

 DOMAIN 379 414 EF-hand 1.
 DOMAIN 451 486 EF-hand 2.
 MOTIF 135 140 HXXXXD motif.
 MOTIF 531 534 Di-lysine motif.  

Keyword

 Acyltransferase; Calcium; Complete proteome; Endoplasmic reticulum; Golgi apparatus; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome; Repeat; Signal-anchor; Transferase; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 534 AA 

Protein Sequence

Gene Ontology

 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; ISS:UniProtKB.
 GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; IEA:EC.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:2001246; P:negative regulation of phosphatidylcholine biosynthetic process; IEA:Compara.
 GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
 GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome.
 GO:0036148; P:phosphatidylglycerol acyl-chain remodeling; TAS:Reactome.
 GO:0045732; P:positive regulation of protein catabolic process; IEA:Compara.
 GO:0060041; P:retina development in camera-type eye; IEA:Compara.
 GO:0043129; P:surfactant homeostasis; IEA:Compara.
 GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome. 

Interpro

 IPR011992; EF-hand-like_dom.
 IPR002048; EF_hand_dom.
 IPR002123; Plipid/glycerol_acylTrfase. 

Pfam

 PF01553; Acyltransferase
 PF13405; EF_hand_4 

SMART

 SM00054; EFh
 SM00563; PlsC 

PROSITE

 PS00018; EF_HAND_1
 PS50222; EF_HAND_2 

PRINTS