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Protein

Lysophosphatidylcholine acyltransferase 2

Gene

Lpcat2

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:17182612, PubMed:18156367). Activity is calcium-dependent (PubMed:17182612). 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:17182612). 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 (PubMed:17182612, PubMed:18156367). Under resting conditions, acyltransferase activity is preferred (PubMed:17182612). Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases (PubMed:17182612). Also catalyzes the conversion of 1-acyl-sn-glycero-3-phosphocholine to 1,2-diacyl-sn-glycero-3-phosphocholine. Involved in the regulation of lipid droplet number and size (By similarity).By similarity2 Publications

Catalytic activityi

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

Enzyme regulationi

Acetyltransferase activity is increased following acute inflammatory stimulation by lipopolysaccharide (LPS). Acyltransferase activity is unchanged.1 Publication

Kineticsi

  1. KM=50.4 µM for acetyl-CoA1 Publication
  2. KM=21.1 µM for arachidonoyl-CoA1 Publication

    Temperature dependencei

    Optimum temperature is 7.4 degrees Celsius.1 Publication

    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)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi404 – 415121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi441 – 452122PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    GO - Biological processi

    • membrane organization Source: UniProtKB
    • phosphatidylcholine acyl-chain remodeling Source: MGI
    • platelet activating factor biosynthetic process Source: UniProtKB
    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.
    UniPathwayiUPA00085.

    Chemistry

    SwissLipidsiSLP:000000293.

    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
    Gene namesi
    Name:Lpcat2
    Synonyms:Aytl1, Aytl1a, Lpcat2a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 8

    Organism-specific databases

    MGIiMGI:3606214. Lpcat2.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5858CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei59 – 7921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
    BLAST
    Topological domaini80 – 544465LumenalSequence analysisAdd
    BLAST

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Lipid droplet, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 544544Lysophosphatidylcholine acyltransferase 2PRO_0000247059Add
    BLAST

    Proteomic databases

    MaxQBiQ8BYI6.
    PaxDbiQ8BYI6.
    PRIDEiQ8BYI6.

    PTM databases

    iPTMnetiQ8BYI6.
    PhosphoSiteiQ8BYI6.

    Expressioni

    Tissue specificityi

    Highest expression is found in resident macrophages and casein-induced neutrophils followed by skin, colon, spleen and thioglycollate-induced macrophages. Detected in erythroleukemic cells but not in reticulocytes.2 Publications

    Inductioni

    By inflammatory stimulation by LPS and by ODN1826, a TLR9 ligand, but not by poly(I:C), a TLR3 ligand.1 Publication

    Gene expression databases

    BgeeiQ8BYI6.
    CleanExiMM_LPCAT2.
    GenevisibleiQ8BYI6. MM.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000049252.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BYI6.
    SMRiQ8BYI6. Positions 312-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini391 – 42636EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini428 – 46336EF-hand 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi146 – 1516HXXXXD motif
    Motifi220 – 2234EGTC motif

    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.
    InParanoidiQ8BYI6.
    KOiK13510.
    OMAiTACCPEK.
    OrthoDBiEOG7NCV5G.
    PhylomeDBiQ8BYI6.
    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.
    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 (3)i

    Sequence statusi: Complete.

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

    Isoform 1 (identifier: Q8BYI6-1) [UniParc]FASTAAdd to basket

    Also known as: a, Aytl1_v1

    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
    MNRCAEAAAV AATVPGSGVG DAGLRPPMVP RQASFFPPPV PNPFVQQTTI
    60 70 80 90 100
    SASRRLQMFL LGIILLPVRA LLVGIILLLA WPFAVISTAC CPEKLTHPIS
    110 120 130 140 150
    NWRRKITRPA LTFLARAMFF SMGFTVTVKG KVASPLEAPI FVVAPHSTFF
    160 170 180 190 200
    DGIACVVAGL PSLVSRNENA QTPLVGRLLR ALQPVLVSRV DPDSRKNTIN
    210 220 230 240 250
    EIKKRATSGG EWPQILVFPE GTCTNRSCLI TFKPGAFIPG VPVQPVLLRY
    260 270 280 290 300
    PNKLDTVTWT WQGYTFLQLC VLTFCQLFTK VEIEFMPVQA PSEEEKNDPV
    310 320 330 340 350
    LFASRIRNLM AEALEIPVTD HTYEDCRLMI SAGQLTLPME AGLVEFSKIS
    360 370 380 390 400
    RKLKLDWDGI RKHLDEYASI ASSSKGGRIG IEEFAEYLKL PVSDVLRQLF
    410 420 430 440 450
    ALFDRNNDGS IDFREYVIGL AVLCNPANTE EIIQVAFKLF DVDEDGYITE
    460 470 480 490 500
    EEFCTILQAS LGVPDLNVSG LFREIAQRDS VSYEEFKSFA LKHPEYAKIF
    510 520 530 540
    TTYLDLQTCH VFSLPEEVQT APSVASNKVS PESQEEGTSD KKVD
    Length:544
    Mass (Da):60,254
    Last modified:March 1, 2003 - v1
    Checksum:i8A790A4C71BB8898
    GO
    Isoform 2 (identifier: Q8BYI6-2) [UniParc]FASTAAdd to basket

    Also known as: b, Aytl1_v2

    The sequence of this isoform differs from the canonical sequence as follows:
         215-254: Missing.

    Show »
    Length:504
    Mass (Da):55,871
    Checksum:iA8F8F2F31006CAD9
    GO
    Isoform 3 (identifier: Q8BYI6-3) [UniParc]FASTAAdd to basket

    Also known as: c, Aytl1_v3

    The sequence of this isoform differs from the canonical sequence as follows:
         215-236: ILVFPEGTCTNRSCLITFKPGA → EPSSQEFQCSPSSSDTQTSWIL
         237-544: Missing.

    Show »
    Length:236
    Mass (Da):25,486
    Checksum:i51FA6EC5F42CC049
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei215 – 25440Missing in isoform 2. 1 PublicationVSP_037079Add
    BLAST
    Alternative sequencei215 – 23622ILVFP…FKPGA → EPSSQEFQCSPSSSDTQTSW IL in isoform 3. 1 PublicationVSP_037080Add
    BLAST
    Alternative sequencei237 – 544308Missing in isoform 3. 1 PublicationVSP_037081Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB244716 mRNA. Translation: BAF47695.1.
    AK039431 mRNA. Translation: BAC30345.1.
    EF442783 mRNA. Translation: ABR20912.1.
    EF442784 mRNA. Translation: ABR20913.1.
    CCDSiCCDS22524.1. [Q8BYI6-1]
    RefSeqiNP_766602.1. NM_173014.1. [Q8BYI6-1]
    XP_011246693.1. XM_011248391.1. [Q8BYI6-2]
    UniGeneiMm.21463.

    Genome annotation databases

    EnsembliENSMUST00000046290; ENSMUSP00000049252; ENSMUSG00000033192. [Q8BYI6-1]
    GeneIDi270084.
    KEGGimmu:270084.
    UCSCiuc009muf.1. mouse. [Q8BYI6-3]
    uc009mug.1. mouse. [Q8BYI6-1]
    uc012gij.1. mouse. [Q8BYI6-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB244716 mRNA. Translation: BAF47695.1.
    AK039431 mRNA. Translation: BAC30345.1.
    EF442783 mRNA. Translation: ABR20912.1.
    EF442784 mRNA. Translation: ABR20913.1.
    CCDSiCCDS22524.1. [Q8BYI6-1]
    RefSeqiNP_766602.1. NM_173014.1. [Q8BYI6-1]
    XP_011246693.1. XM_011248391.1. [Q8BYI6-2]
    UniGeneiMm.21463.

    3D structure databases

    ProteinModelPortaliQ8BYI6.
    SMRiQ8BYI6. Positions 312-486.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000049252.

    Chemistry

    SwissLipidsiSLP:000000293.

    PTM databases

    iPTMnetiQ8BYI6.
    PhosphoSiteiQ8BYI6.

    Proteomic databases

    MaxQBiQ8BYI6.
    PaxDbiQ8BYI6.
    PRIDEiQ8BYI6.

    Protocols and materials databases

    DNASUi270084.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000046290; ENSMUSP00000049252; ENSMUSG00000033192. [Q8BYI6-1]
    GeneIDi270084.
    KEGGimmu:270084.
    UCSCiuc009muf.1. mouse. [Q8BYI6-3]
    uc009mug.1. mouse. [Q8BYI6-1]
    uc012gij.1. mouse. [Q8BYI6-2]

    Organism-specific databases

    CTDi54947.
    MGIiMGI:3606214. Lpcat2.

    Phylogenomic databases

    eggNOGiKOG4666. Eukaryota.
    ENOG410XSIQ. LUCA.
    GeneTreeiENSGT00390000004914.
    HOGENOMiHOG000234374.
    InParanoidiQ8BYI6.
    KOiK13510.
    OMAiTACCPEK.
    OrthoDBiEOG7NCV5G.
    PhylomeDBiQ8BYI6.
    TreeFamiTF323244.

    Enzyme and pathway databases

    UniPathwayiUPA00085.
    BRENDAi2.3.1.23. 3474.
    2.3.1.67. 3474.
    ReactomeiR-MMU-1482788. Acyl chain remodelling of PC.

    Miscellaneous databases

    ChiTaRSiLpcat2. mouse.
    NextBioi393188.
    PROiQ8BYI6.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8BYI6.
    CleanExiMM_LPCAT2.
    GenevisibleiQ8BYI6. 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.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:lyso-PAF acetyltransferase."
      Shindou H., Hishikawa D., Nakanishi H., Harayama T., Ishii S., Taguchi R., Shimizu T.
      J. Biol. Chem. 282:6532-6539(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Spinal cord.
    3. "Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes."
      Soupene E., Fyrst H., Kuypers F.A.
      Proc. Natl. Acad. Sci. U.S.A. 105:88-93(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 175-299 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 175-544 (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPCAT2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BYI6
    Secondary accession number(s): A3KBM0, A9Q1G2, A9Q1G3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: March 1, 2003
    Last modified: February 17, 2016
    This is version 112 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.