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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)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi392 – 403121PROSITE-ProRule annotationAdd
    BLAST

    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-75109. Triglyceride Biosynthesis.
    UniPathwayiUPA00085.

    Chemistry

    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)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5757CytoplasmicSequence analysisAdd
    BLAST
    Transmembranei58 – 7821Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
    BLAST
    Topological domaini79 – 534456LumenalSequence analysisAdd
    BLAST

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi135 – 1406Missing : Abolishes activity. 1 Publication
    Mutagenesisi135 – 1351H → A: Loss of activity. 1 Publication
    Mutagenesisi140 – 1401D → A: Loss of activity. 1 Publication
    Mutagenesisi160 – 1601I → A: No effect on activity for acetyl-CoA. Reduced activity for palmitoyl-CoA. 1 Publication
    Mutagenesisi162 – 1621I → A: Greatly reduced activity. 1 Publication
    Mutagenesisi163 – 1631W → A: Greatly reduced activity. 1 Publication
    Mutagenesisi164 – 17714Missing : Abolishes activity. 1 PublicationAdd
    BLAST
    Mutagenesisi164 – 1641G → A: Slightly increased activity. 1 Publication
    Mutagenesisi166 – 1661L → A: Greatly reduced activity. 1 Publication
    Mutagenesisi167 – 1671I → A: Slightly reduced activity. 1 Publication
    Mutagenesisi168 – 1681R → A: Reduced activity. 1 Publication
    Mutagenesisi169 – 1691Y → A: Slightly reduced activity. 1 Publication
    Mutagenesisi170 – 1701I → A: Slightly reduced activity. 1 Publication
    Mutagenesisi171 – 1711R → A: Reduced activity. 1 Publication
    Mutagenesisi173 – 1731V → A: Greatly reduced activity. 1 Publication
    Mutagenesisi174 – 1741F → A: Loss of lyso-PAFAT activity. LPCAT activity is partially reduced. 1 Publication
    Mutagenesisi175 – 1751V → A: No activity for acetyl-CoA. Activity for palmitoyl-CoA decreased. 1 Publication
    Mutagenesisi177 – 1771R → A: Loss of lyso-PAFAT activity. LPCAT activity is partially reduced. 1 Publication
    Mutagenesisi203 – 2097Missing : Abolishes activity. 1 Publication
    Mutagenesisi208 – 2081E → A: Loss of activity. 1 Publication
    Mutagenesisi209 – 2091G → A: Reduced activity. 1 Publication
    Mutagenesisi227 – 2337Missing : Abolishes activity. 1 Publication
    Mutagenesisi227 – 2271P → A: Reduced activity. 1 Publication
    Mutagenesisi230 – 2301P → A: Reduced activity. 1 Publication
    Mutagenesisi233 – 2331P → A: Reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 534534Lysophosphatidylcholine acyltransferase 1PRO_0000247065Add
    BLAST

    Proteomic databases

    EPDiQ3TFD2.
    MaxQBiQ3TFD2.
    PaxDbiQ3TFD2.
    PRIDEiQ3TFD2.

    PTM databases

    iPTMnetiQ3TFD2.
    PhosphoSiteiQ3TFD2.

    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

    BgeeiQ3TFD2.
    CleanExiMM_LPCAT1.
    ExpressionAtlasiQ3TFD2. baseline and differential.
    GenevisibleiQ3TFD2. MM.

    Interactioni

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ3TFD2.
    SMRiQ3TFD2. Positions 337-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini379 – 41436EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini451 – 48636EF-hand 2PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi135 – 1406HXXXXD motif
    Motifi531 – 5344Di-lysine motif

    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.
    OrthoDBiEOG7NCV5G.
    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 AAH05662.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC32594.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC32760.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251A → T in BAC38353 (PubMed:16141072).Curated
    Sequence conflicti101 – 1011A → T in AAH66809 (PubMed:15489334).Curated
    Sequence conflicti232 – 2321Q → R in BAE42540 (PubMed:16141072).Curated
    Sequence conflicti272 – 2721E → G in AAH66809 (PubMed:15489334).Curated
    Sequence conflicti338 – 3381V → M in BAC32594 (PubMed:16141072).Curated
    Sequence conflicti338 – 3381V → M in BAC32760 (PubMed:16141072).Curated
    Sequence conflicti442 – 4421S → P in AAH66809 (PubMed:15489334).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 203203Missing in isoform 3. 1 PublicationVSP_019913Add
    BLAST
    Alternative sequencei1 – 4848Missing in isoform 2. 1 PublicationVSP_019914Add
    BLAST

    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]
    XP_011242803.1. XM_011244501.1. [Q3TFD2-2]
    XP_011242804.1. XM_011244502.1. [Q3TFD2-3]
    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]
    XP_011242803.1. XM_011244501.1. [Q3TFD2-2]
    XP_011242804.1. XM_011244502.1. [Q3TFD2-3]
    UniGeneiMm.284649.

    3D structure databases

    ProteinModelPortaliQ3TFD2.
    SMRiQ3TFD2. Positions 337-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Chemistry

    SwissLipidsiSLP:000000297.

    PTM databases

    iPTMnetiQ3TFD2.
    PhosphoSiteiQ3TFD2.

    Proteomic databases

    EPDiQ3TFD2.
    MaxQBiQ3TFD2.
    PaxDbiQ3TFD2.
    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.
    OrthoDBiEOG7NCV5G.
    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-75109. Triglyceride Biosynthesis.

    Miscellaneous databases

    NextBioi373109.
    PROiQ3TFD2.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ3TFD2.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1): expression in alveolar type II cells and possible involvement in surfactant production."
      Nakanishi H., Shindou H., Hishikawa D., Harayama T., Ogasawara R., Suwabe A., Taguchi R., Shimizu T.
      J. Biol. Chem. 281:20140-20147(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells."
      Chen X., Hyatt B.A., Mucenski M.L., Mason R.J., Shannon J.M.
      Proc. Natl. Acad. Sci. U.S.A. 103:11724-11729(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    3. "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] (ISOFORMS 1 AND 3).
      Strain: C57BL/6J and NOD.
      Tissue: Corpora quadrigemina, Head and Kidney.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-534.
      Strain: C57BL/6J and Czech II.
      Tissue: Egg and Mammary tumor.
    5. "Identification of a novel noninflammatory biosynthetic pathway of platelet-activating factor."
      Harayama T., Shindou H., Ogasawara R., Suwabe A., Shimizu T.
      J. Biol. Chem. 283:11097-11106(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, MUTAGENESIS OF 135-HIS--ASP-140; HIS-135; ASP-140; ILE-160; ILE-162; TRP-163; 164-GLY--ARG-177; GLY-164; LEU-166; ILE-167; ARG-168; TYR-169; ILE-170; ARG-171; VAL-173; PHE-174; VAL-175; ARG-177; 203-ILE--GLY-209; GLU-208; GLY-209; 227-PRO--PRO-233; PRO-227; PRO-230 AND PRO-233.
    6. "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: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Lung and Spleen.

    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: March 16, 2016
    This is version 110 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.