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Protein

Lysophosphatidylcholine acyltransferase 2

Gene

LPCAT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. 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). Also converts lyso-PAF to 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases. Also catalyzes the conversion of 1-acyl-sn-glycero-3-phosphocholine to 1,2-diacyl-sn-glycero-3-phosphocholine.2 Publications

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.1 Publication
Acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine.1 Publication
Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.1 Publication

Enzyme regulationi

Acetyltransferase activity is increased following acute inflammatory stimulation by lipopolysaccharide (LPS). Acyltransferase activity is unchanged (By similarity).By similarity

Pathwayi: phospholipid metabolism

This protein is involved in the pathway phospholipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phospholipid metabolism and in Lipid metabolism.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi404 – 4151PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi441 – 4522PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS01567-MONOMER.
BRENDAi2.3.1.23. 2681.
2.3.1.51. 2681.
2.3.1.67. 2681.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
UniPathwayiUPA00085.

Chemistry databases

SwissLipidsiSLP:000000279.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophosphatidylcholine acyltransferase 2 (EC:2.3.1.23)
Short name:
LPC acyltransferase 2
Short name:
LPCAT-2
Short name:
LysoPC acyltransferase 2
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 11 (EC:2.3.1.51)
Short name:
1-AGP acyltransferase 11
Short name:
1-AGPAT 11
1-acylglycerophosphocholine O-acyltransferase
1-alkylglycerophosphocholine O-acetyltransferase (EC:2.3.1.67)
Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
Short name:
Acetyl-CoA:lyso-PAF acetyltransferase
Short name:
Lyso-PAF acetyltransferase
Short name:
LysoPAFAT
Acyltransferase-like 1
Lysophosphatidic acid acyltransferase alpha
Short name:
LPAAT-alpha
Gene namesi
Name:LPCAT2
Synonyms:AGPAT11, AYTL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:26032. LPCAT2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 57CytoplasmicSequence analysisAdd BLAST57
Transmembranei58 – 78Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini79 – 544LumenalSequence analysisAdd BLAST466

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
  • Golgi membrane Source: UniProtKB-SubCell
  • Golgi stack Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • lipid particle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Lipid droplet, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi54947.
OpenTargetsiENSG00000087253.
PharmGKBiPA162394265.

Polymorphism and mutation databases

BioMutaiLPCAT2.
DMDMi74738601.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002470581 – 544Lysophosphatidylcholine acyltransferase 2Add BLAST544

Proteomic databases

EPDiQ7L5N7.
MaxQBiQ7L5N7.
PaxDbiQ7L5N7.
PeptideAtlasiQ7L5N7.
PRIDEiQ7L5N7.

PTM databases

iPTMnetiQ7L5N7.
PhosphoSitePlusiQ7L5N7.
SwissPalmiQ7L5N7.

Expressioni

Gene expression databases

BgeeiENSG00000087253.
CleanExiHS_LPCAT2.
ExpressionAtlasiQ7L5N7. baseline and differential.
GenevisibleiQ7L5N7. HS.

Organism-specific databases

HPAiHPA007891.

Interactioni

Protein-protein interaction databases

BioGridi120286. 5 interactors.
IntActiQ7L5N7. 2 interactors.
STRINGi9606.ENSP00000262134.

Structurei

3D structure databases

ProteinModelPortaliQ7L5N7.
SMRiQ7L5N7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini391 – 426EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini428 – 463EF-hand 2PROSITE-ProRule annotationAdd BLAST36

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi146 – 151HXXXXD motif6
Motifi220 – 223EGTC motif4

Domaini

The HXXXXD motif is essential for acyltransferase activity.By similarity

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4666. Eukaryota.
ENOG410XSIQ. LUCA.
GeneTreeiENSGT00390000004914.
HOGENOMiHOG000234374.
HOVERGENiHBG060273.
InParanoidiQ7L5N7.
KOiK13510.
OMAiTACCPEK.
OrthoDBiEOG091G09LH.
PhylomeDBiQ7L5N7.
TreeFamiTF323244.

Family and domain databases

CDDicd00051. EFh. 2 hits.
Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
SM00563. PlsC. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7L5N7-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSRCAQAAEV AATVPGAGVG NVGLRPPMVP RQASFFPPPV PNPFVQQTQI
60 70 80 90 100
GSARRVQIVL LGIILLPIRV LLVALILLLA WPFAAISTVC CPEKLTHPIT
110 120 130 140 150
GWRRKITQTA LKFLGRAMFF SMGFIVAVKG KIASPLEAPV FVAAPHSTFF
160 170 180 190 200
DGIACVVAGL PSMVSRNENA QVPLIGRLLR AVQPVLVSRV DPDSRKNTIN
210 220 230 240 250
EIIKRTTSGG EWPQILVFPE GTCTNRSCLI TFKPGAFIPG VPVQPVLLRY
260 270 280 290 300
PNKLDTVTWT WQGYTFIQLC MLTFCQLFTK VEVEFMPVQV PNDEEKNDPV
310 320 330 340 350
LFANKVRNLM AEALGIPVTD HTYEDCRLMI SAGQLTLPME AGLVEFTKIS
360 370 380 390 400
RKLKLDWDGV RKHLDEYASI ASSSKGGRIG IEEFAKYLKL PVSDVLRQLF
410 420 430 440 450
ALFDRNHDGS IDFREYVIGL AVLCNPSNTE EIIQVAFKLF DVDEDGYITE
460 470 480 490 500
EEFSTILQAS LGVPDLDVSG LFKEIAQGDS ISYEEFKSFA LKHPEYAKIF
510 520 530 540
TTYLDLQTCH VFSLPKEVQT TPSTASNKVS PEKHEESTSD KKDD
Length:544
Mass (Da):60,208
Last modified:July 5, 2004 - v1
Checksum:iB823D86272A739C0
GO
Isoform 2 (identifier: Q7L5N7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-270: Missing.

Note: No experimental confirmation available.
Show »
Length:274
Mass (Da):30,895
Checksum:i1B7DE26E0D7791EA
GO

Sequence cautioni

The sequence BAA91199 differs from that shown. Reason: Frameshift at position 44.Curated
The sequence CAE46034 differs from that shown. Reason: Frameshift at position 295.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_027058163M → I.Corresponds to variant rs837550dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0199121 – 270Missing in isoform 2. 1 PublicationAdd BLAST270

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB244718 mRNA. Translation: BAF47696.1.
AK000488 mRNA. Translation: BAA91199.1. Frameshift.
BX641069 mRNA. Translation: CAE46034.1. Frameshift.
BC002472 mRNA. Translation: AAH02472.2.
CCDSiCCDS10753.1. [Q7L5N7-1]
RefSeqiNP_060309.2. NM_017839.4. [Q7L5N7-1]
XP_011521471.1. XM_011523169.2. [Q7L5N7-2]
UniGeneiHs.460857.

Genome annotation databases

EnsembliENST00000262134; ENSP00000262134; ENSG00000087253. [Q7L5N7-1]
GeneIDi54947.
KEGGihsa:54947.
UCSCiuc002eie.5. human. [Q7L5N7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB244718 mRNA. Translation: BAF47696.1.
AK000488 mRNA. Translation: BAA91199.1. Frameshift.
BX641069 mRNA. Translation: CAE46034.1. Frameshift.
BC002472 mRNA. Translation: AAH02472.2.
CCDSiCCDS10753.1. [Q7L5N7-1]
RefSeqiNP_060309.2. NM_017839.4. [Q7L5N7-1]
XP_011521471.1. XM_011523169.2. [Q7L5N7-2]
UniGeneiHs.460857.

3D structure databases

ProteinModelPortaliQ7L5N7.
SMRiQ7L5N7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120286. 5 interactors.
IntActiQ7L5N7. 2 interactors.
STRINGi9606.ENSP00000262134.

Chemistry databases

SwissLipidsiSLP:000000279.

PTM databases

iPTMnetiQ7L5N7.
PhosphoSitePlusiQ7L5N7.
SwissPalmiQ7L5N7.

Polymorphism and mutation databases

BioMutaiLPCAT2.
DMDMi74738601.

Proteomic databases

EPDiQ7L5N7.
MaxQBiQ7L5N7.
PaxDbiQ7L5N7.
PeptideAtlasiQ7L5N7.
PRIDEiQ7L5N7.

Protocols and materials databases

DNASUi54947.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262134; ENSP00000262134; ENSG00000087253. [Q7L5N7-1]
GeneIDi54947.
KEGGihsa:54947.
UCSCiuc002eie.5. human. [Q7L5N7-1]

Organism-specific databases

CTDi54947.
DisGeNETi54947.
GeneCardsiLPCAT2.
HGNCiHGNC:26032. LPCAT2.
HPAiHPA007891.
MIMi612040. gene.
neXtProtiNX_Q7L5N7.
OpenTargetsiENSG00000087253.
PharmGKBiPA162394265.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4666. Eukaryota.
ENOG410XSIQ. LUCA.
GeneTreeiENSGT00390000004914.
HOGENOMiHOG000234374.
HOVERGENiHBG060273.
InParanoidiQ7L5N7.
KOiK13510.
OMAiTACCPEK.
OrthoDBiEOG091G09LH.
PhylomeDBiQ7L5N7.
TreeFamiTF323244.

Enzyme and pathway databases

UniPathwayiUPA00085.
BioCyciZFISH:HS01567-MONOMER.
BRENDAi2.3.1.23. 2681.
2.3.1.51. 2681.
2.3.1.67. 2681.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.

Miscellaneous databases

ChiTaRSiLPCAT2. human.
GenomeRNAii54947.
PROiQ7L5N7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087253.
CleanExiHS_LPCAT2.
ExpressionAtlasiQ7L5N7. baseline and differential.
GenevisibleiQ7L5N7. HS.

Family and domain databases

CDDicd00051. EFh. 2 hits.
Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
PF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
SM00563. PlsC. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPCAT2_HUMAN
AccessioniPrimary (citable) accession number: Q7L5N7
Secondary accession number(s): A3KBM1, Q6MZJ6, Q9NX23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.