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Protein

Lysophosphatidylcholine acyltransferase 1

Gene

Lpcat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Possesses both acyltransferase and acetyltransferase activities (PubMed:16704971). Activity is calcium-independent (PubMed:18285344). Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC) (PubMed:16704971, PubMed:18156367). 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). 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).By similarity3 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

Enzyme regulationi

Not activated by inflammatory stimulation. Inhibited by Cu2+ and Fe2+. Activity is not affected by Co2+, Mg2+ or Mn2+.1 Publication

Kineticsi

  1. KM=2.3 µM for 1-palmitoyl-LPC2 Publications
  2. KM=3 µM for palmitoyl-CoA2 Publications

    pH dependencei

    Optimum pH is 7.5.2 Publications

    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 bindingi392 – 4031PROSITE-ProRule annotationAdd BLAST12

    GO - Molecular functioni

    GO - Biological processi

    • negative regulation of phosphatidylcholine biosynthetic process Source: MGI
    • phosphatidylcholine acyl-chain remodeling Source: MGI
    • phospholipid biosynthetic process Source: UniProtKB
    • positive regulation of protein catabolic process Source: MGI
    • retina development in camera-type eye Source: MGI
    • surfactant homeostasis Source: MGI
    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

    BRENDAi2.3.1.23. 3474.
    2.3.1.67. 3474.
    ReactomeiR-MMU-1482788. Acyl chain remodelling of PC.
    R-MMU-1482925. Acyl chain remodelling of PG.
    R-MMU-1483166. Synthesis of PA.
    R-MMU-1483191. Synthesis of PC.
    R-MMU-6798695. Neutrophil degranulation.
    R-MMU-75109. Triglyceride Biosynthesis.
    UniPathwayiUPA00085.

    Chemistry databases

    SwissLipidsiSLP:000000297.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysophosphatidylcholine acyltransferase 1 (EC:2.3.1.23)
    Short name:
    LPC acyltransferase 1
    Short name:
    LPCAT-1
    Short name:
    LysoPC acyltransferase 1
    Short name:
    mLPCAT1
    Alternative name(s):
    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 2
    Gene namesi
    Name:Lpcat1
    Synonyms:Aytl2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 13

    Organism-specific databases

    MGIiMGI:2384812. Lpcat1.

    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 – 534LumenalSequence analysisAdd BLAST456

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Lipid droplet, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi135 – 140Missing : Abolishes activity. 1 Publication6
    Mutagenesisi135H → A: Loss of activity. 1 Publication1
    Mutagenesisi140D → A: Loss of activity. 1 Publication1
    Mutagenesisi160I → A: No effect on activity for acetyl-CoA. Reduced activity for palmitoyl-CoA. 1 Publication1
    Mutagenesisi162I → A: Greatly reduced activity. 1 Publication1
    Mutagenesisi163W → A: Greatly reduced activity. 1 Publication1
    Mutagenesisi164 – 177Missing : Abolishes activity. 1 PublicationAdd BLAST14
    Mutagenesisi164G → A: Slightly increased activity. 1 Publication1
    Mutagenesisi166L → A: Greatly reduced activity. 1 Publication1
    Mutagenesisi167I → A: Slightly reduced activity. 1 Publication1
    Mutagenesisi168R → A: Reduced activity. 1 Publication1
    Mutagenesisi169Y → A: Slightly reduced activity. 1 Publication1
    Mutagenesisi170I → A: Slightly reduced activity. 1 Publication1
    Mutagenesisi171R → A: Reduced activity. 1 Publication1
    Mutagenesisi173V → A: Greatly reduced activity. 1 Publication1
    Mutagenesisi174F → A: Loss of lyso-PAFAT activity. LPCAT activity is partially reduced. 1 Publication1
    Mutagenesisi175V → A: No activity for acetyl-CoA. Activity for palmitoyl-CoA decreased. 1 Publication1
    Mutagenesisi177R → A: Loss of lyso-PAFAT activity. LPCAT activity is partially reduced. 1 Publication1
    Mutagenesisi203 – 209Missing : Abolishes activity. 1 Publication7
    Mutagenesisi208E → A: Loss of activity. 1 Publication1
    Mutagenesisi209G → A: Reduced activity. 1 Publication1
    Mutagenesisi227 – 233Missing : Abolishes activity. 1 Publication7
    Mutagenesisi227P → A: Reduced activity. 1 Publication1
    Mutagenesisi230P → A: Reduced activity. 1 Publication1
    Mutagenesisi233P → A: Reduced activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002470651 – 534Lysophosphatidylcholine acyltransferase 1Add BLAST534

    Proteomic databases

    EPDiQ3TFD2.
    MaxQBiQ3TFD2.
    PaxDbiQ3TFD2.
    PeptideAtlasiQ3TFD2.
    PRIDEiQ3TFD2.

    PTM databases

    iPTMnetiQ3TFD2.
    PhosphoSitePlusiQ3TFD2.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Developmental stagei

    Expression increases steadily throughout embryogenesis and decreases slightly in the adult.1 Publication

    Inductioni

    Constitutively expressed. Not induced by inflammatory stimulation.1 Publication

    Gene expression databases

    BgeeiENSMUSG00000021608.
    CleanExiMM_LPCAT1.
    ExpressionAtlasiQ3TFD2. baseline and differential.
    GenevisibleiQ3TFD2. MM.

    Interactioni

    Protein-protein interaction databases

    IntActiQ3TFD2. 1 interactor.
    MINTiMINT-4112667.
    STRINGi10090.ENSMUSP00000022099.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3TFD2.
    SMRiQ3TFD2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini379 – 414EF-hand 1PROSITE-ProRule annotationAdd BLAST36
    Domaini451 – 486EF-hand 2PROSITE-ProRule annotationAdd BLAST36

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi135 – 140HXXXXD motif6
    Motifi531 – 534Di-lysine motif4

    Domaini

    The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphocholine.By similarity
    The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.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.
    InParanoidiQ3TFD2.
    KOiK13510.
    OMAiDYLYPDQ.
    OrthoDBiEOG091G09LH.
    PhylomeDBiQ3TFD2.
    TreeFamiTF323244.

    Family and domain databases

    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.
    PF13833. EF-hand_8. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 3 hits.
    SM00563. PlsC. 1 hit.
    [Graphical view]
    SUPFAMiSSF47473. SSF47473. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q3TFD2-1) [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
    MRLRGRGPRA APSSSSGAGD ARRLAPPGRN PFVHELRLSA LQKAQVAFMT
    60 70 80 90 100
    LTLFPIRLLF AAFMMLLAWP FALLASLGPP DKEPEQPLAL WRKVVDFLLK
    110 120 130 140 150
    AIMRTMWFAG GFHRVAVKGR QALPTEAAIL TLAPHSSYFD AIPVTMTMSS
    160 170 180 190 200
    IVMKAESRDI PIWGTLIRYI RPVFVSRSDQ DSRRKTVEEI KRRAQSNGKW
    210 220 230 240 250
    PQIMIFPEGT CTNRTCLITF KPGAFIPGVP VQPVVLRYPN KLDTITWTWQ
    260 270 280 290 300
    GPGALKILWL TLCQFQNQVE IEFLPVYCPS EEEKRNPALY ASNVRRVMAK
    310 320 330 340 350
    ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPENLEK
    360 370 380 390 400
    DLDKYSESAR MKRGEKIRLP EFAAYLEVPV SDALEDMFSL FDESGGGEID
    410 420 430 440 450
    LREYVVALSV VCRPSQTLAT IQLAFKMYGS PEDGSIDEAN LSCILKTALG
    460 470 480 490 500
    VSELTVTDLF QAIDQEDKGR ITFDDFCGFA EMYPDYAEDY LYPDQTHFDS
    510 520 530
    CAQTPPAPTP NGFCIDFSPE NSDFGRKNSC KKAD
    Length:534
    Mass (Da):59,744
    Last modified:October 11, 2005 - v1
    Checksum:i50C1EF4A5D494DF2
    GO
    Isoform 2 (identifier: Q3TFD2-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-48: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:486
    Mass (Da):54,650
    Checksum:i058873866F2736C6
    GO
    Isoform 3 (identifier: Q3TFD2-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-203: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:331
    Mass (Da):36,982
    Checksum:i2B9F5AA5431F7DBA
    GO

    Sequence cautioni

    The sequence AAH05662 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC32594 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC32760 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti25A → T in BAC38353 (PubMed:16141072).Curated1
    Sequence conflicti101A → T in AAH66809 (PubMed:15489334).Curated1
    Sequence conflicti232Q → R in BAE42540 (PubMed:16141072).Curated1
    Sequence conflicti272E → G in AAH66809 (PubMed:15489334).Curated1
    Sequence conflicti338V → M in BAC32594 (PubMed:16141072).Curated1
    Sequence conflicti338V → M in BAC32760 (PubMed:16141072).Curated1
    Sequence conflicti442S → P in AAH66809 (PubMed:15489334).Curated1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0199131 – 203Missing in isoform 3. 1 PublicationAdd BLAST203
    Alternative sequenceiVSP_0199141 – 48Missing in isoform 2. 1 PublicationAdd BLAST48

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB244717 mRNA. Translation: BAE94687.2.
    AK046079 mRNA. Translation: BAC32594.1. Different initiation.
    AK046507 mRNA. Translation: BAC32760.1. Different initiation.
    AK081865 mRNA. Translation: BAC38353.1.
    AK155286 mRNA. Translation: BAE33166.1.
    AK169190 mRNA. Translation: BAE40966.1.
    AK170723 mRNA. Translation: BAE41980.1.
    AK171582 mRNA. Translation: BAE42540.1.
    BC005662 mRNA. Translation: AAH05662.1. Different initiation.
    BC066809 mRNA. Translation: AAH66809.1.
    CCDSiCCDS36726.1. [Q3TFD2-1]
    RefSeqiNP_663351.3. NM_145376.5. [Q3TFD2-1]
    UniGeneiMm.284649.

    Genome annotation databases

    EnsembliENSMUST00000022099; ENSMUSP00000022099; ENSMUSG00000021608. [Q3TFD2-1]
    GeneIDi210992.
    KEGGimmu:210992.
    UCSCiuc007rdk.1. mouse. [Q3TFD2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB244717 mRNA. Translation: BAE94687.2.
    AK046079 mRNA. Translation: BAC32594.1. Different initiation.
    AK046507 mRNA. Translation: BAC32760.1. Different initiation.
    AK081865 mRNA. Translation: BAC38353.1.
    AK155286 mRNA. Translation: BAE33166.1.
    AK169190 mRNA. Translation: BAE40966.1.
    AK170723 mRNA. Translation: BAE41980.1.
    AK171582 mRNA. Translation: BAE42540.1.
    BC005662 mRNA. Translation: AAH05662.1. Different initiation.
    BC066809 mRNA. Translation: AAH66809.1.
    CCDSiCCDS36726.1. [Q3TFD2-1]
    RefSeqiNP_663351.3. NM_145376.5. [Q3TFD2-1]
    UniGeneiMm.284649.

    3D structure databases

    ProteinModelPortaliQ3TFD2.
    SMRiQ3TFD2.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ3TFD2. 1 interactor.
    MINTiMINT-4112667.
    STRINGi10090.ENSMUSP00000022099.

    Chemistry databases

    SwissLipidsiSLP:000000297.

    PTM databases

    iPTMnetiQ3TFD2.
    PhosphoSitePlusiQ3TFD2.

    Proteomic databases

    EPDiQ3TFD2.
    MaxQBiQ3TFD2.
    PaxDbiQ3TFD2.
    PeptideAtlasiQ3TFD2.
    PRIDEiQ3TFD2.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000022099; ENSMUSP00000022099; ENSMUSG00000021608. [Q3TFD2-1]
    GeneIDi210992.
    KEGGimmu:210992.
    UCSCiuc007rdk.1. mouse. [Q3TFD2-1]

    Organism-specific databases

    CTDi79888.
    MGIiMGI:2384812. Lpcat1.

    Phylogenomic databases

    eggNOGiKOG4666. Eukaryota.
    ENOG410XSIQ. LUCA.
    GeneTreeiENSGT00390000004914.
    HOGENOMiHOG000234374.
    HOVERGENiHBG060273.
    InParanoidiQ3TFD2.
    KOiK13510.
    OMAiDYLYPDQ.
    OrthoDBiEOG091G09LH.
    PhylomeDBiQ3TFD2.
    TreeFamiTF323244.

    Enzyme and pathway databases

    UniPathwayiUPA00085.
    BRENDAi2.3.1.23. 3474.
    2.3.1.67. 3474.
    ReactomeiR-MMU-1482788. Acyl chain remodelling of PC.
    R-MMU-1482925. Acyl chain remodelling of PG.
    R-MMU-1483166. Synthesis of PA.
    R-MMU-1483191. Synthesis of PC.
    R-MMU-6798695. Neutrophil degranulation.
    R-MMU-75109. Triglyceride Biosynthesis.

    Miscellaneous databases

    PROiQ3TFD2.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSMUSG00000021608.
    CleanExiMM_LPCAT1.
    ExpressionAtlasiQ3TFD2. baseline and differential.
    GenevisibleiQ3TFD2. MM.

    Family and domain databases

    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.
    PF13833. EF-hand_8. 1 hit.
    [Graphical view]
    SMARTiSM00054. EFh. 3 hits.
    SM00563. PlsC. 1 hit.
    [Graphical view]
    SUPFAMiSSF47473. SSF47473. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 2 hits.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPCAT1_MOUSE
    AccessioniPrimary (citable) accession number: Q3TFD2
    Secondary accession number(s): Q3TAX4
    , Q6NXZ6, Q8BG23, Q8BUX7, Q99JU6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: October 11, 2005
    Last modified: November 30, 2016
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. 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.