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Entry version 134 (16 Oct 2019)
Sequence version 1 (11 Oct 2005)
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Protein

Lysophosphatidylcholine acyltransferase 1

Gene

Lpcat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi392 – 4031PROSITE-ProRule annotationAdd BLAST12

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAcyltransferase, Transferase
    Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism
    LigandCalcium, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.3.1.23 3474
    2.3.1.67 3474

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-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

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00085

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000000297

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:Lpcat1
    Synonyms:Aytl2
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

    Organism-specific databases

    Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

    More...
    MGIi
    MGI:2384812 Lpcat1

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 57CytoplasmicSequence analysisAdd BLAST57
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei58 – 78Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini79 – 534LumenalSequence analysisAdd BLAST456

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Lipid droplet, Membrane

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002470651 – 534Lysophosphatidylcholine acyltransferase 1Add BLAST534

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q3TFD2

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q3TFD2

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q3TFD2

    PeptideAtlas

    More...
    PeptideAtlasi
    Q3TFD2

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q3TFD2

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q3TFD2

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    Q3TFD2

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    Q3TFD2

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

    <p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Constitutively expressed. Not induced by inflammatory stimulation.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSMUSG00000021608 Expressed in 283 organ(s), highest expression level in primary oocyte

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q3TFD2 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q3TFD2 MM

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    229195, 1 interactor

    Protein interaction database and analysis system

    More...
    IntActi
    Q3TFD2, 1 interactor

    Molecular INTeraction database

    More...
    MINTi
    Q3TFD2

    STRING: functional protein association networks

    More...
    STRINGi
    10090.ENSMUSP00000022099

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q3TFD2

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini379 – 414EF-hand 1PROSITE-ProRule annotationAdd BLAST36
    Domaini451 – 486EF-hand 2PROSITE-ProRule annotationAdd BLAST36

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi135 – 140HXXXXD motif6
    Motifi531 – 534Di-lysine motif4

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG4666 Eukaryota
    ENOG410XSIQ LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00950000182744

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000234374

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q3TFD2

    KEGG Orthology (KO)

    More...
    KOi
    K13510

    Database of Orthologous Groups

    More...
    OrthoDBi
    1266853at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q3TFD2

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF323244

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011992 EF-hand-dom_pair
    IPR018247 EF_Hand_1_Ca_BS
    IPR002048 EF_hand_dom
    IPR002123 Plipid/glycerol_acylTrfase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01553 Acyltransferase, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00054 EFh, 3 hits
    SM00563 PlsC, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF47473 SSF47473, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00018 EF_HAND_1, 1 hit
    PS50222 EF_HAND_2, 2 hits

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q3TFD2-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    D6RFA8D6RFA8_MOUSE
    Acyltransferase like 2, isoform CRA...
    Lpcat1 Aytl2, mCG_10024
    46Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    D6RE48D6RE48_MOUSE
    Lysophosphatidylcholine acyltransfe...
    Lpcat1
    77Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAH05662 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
    The sequence BAC32594 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
    The sequence BAC32760 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS36726.1 [Q3TFD2-1]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_663351.3, NM_145376.5 [Q3TFD2-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSMUST00000022099; ENSMUSP00000022099; ENSMUSG00000021608 [Q3TFD2-1]
    ENSMUST00000223060; ENSMUSP00000152190; ENSMUSG00000021608 [Q3TFD2-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    210992

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mmu:210992

    UCSC genome browser

    More...
    UCSCi
    uc007rdk.1 mouse [Q3TFD2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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]

    3D structure databases

    SMRiQ3TFD2
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi229195, 1 interactor
    IntActiQ3TFD2, 1 interactor
    MINTiQ3TFD2
    STRINGi10090.ENSMUSP00000022099

    Chemistry databases

    SwissLipidsiSLP:000000297

    PTM databases

    iPTMnetiQ3TFD2
    PhosphoSitePlusiQ3TFD2
    SwissPalmiQ3TFD2

    Proteomic databases

    EPDiQ3TFD2
    MaxQBiQ3TFD2
    PaxDbiQ3TFD2
    PeptideAtlasiQ3TFD2
    PRIDEiQ3TFD2

    Genome annotation databases

    EnsembliENSMUST00000022099; ENSMUSP00000022099; ENSMUSG00000021608 [Q3TFD2-1]
    ENSMUST00000223060; ENSMUSP00000152190; ENSMUSG00000021608 [Q3TFD2-2]
    GeneIDi210992
    KEGGimmu:210992
    UCSCiuc007rdk.1 mouse [Q3TFD2-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    79888
    MGIiMGI:2384812 Lpcat1

    Phylogenomic databases

    eggNOGiKOG4666 Eukaryota
    ENOG410XSIQ LUCA
    GeneTreeiENSGT00950000182744
    HOGENOMiHOG000234374
    InParanoidiQ3TFD2
    KOiK13510
    OrthoDBi1266853at2759
    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

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    Lpcat1 mouse

    Protein Ontology

    More...
    PROi
    PR:Q3TFD2

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSMUSG00000021608 Expressed in 283 organ(s), highest expression level in primary oocyte
    ExpressionAtlasiQ3TFD2 baseline and differential
    GenevisibleiQ3TFD2 MM

    Family and domain databases

    InterProiView protein in InterPro
    IPR011992 EF-hand-dom_pair
    IPR018247 EF_Hand_1_Ca_BS
    IPR002048 EF_hand_dom
    IPR002123 Plipid/glycerol_acylTrfase
    PfamiView protein in Pfam
    PF01553 Acyltransferase, 1 hit
    SMARTiView protein in SMART
    SM00054 EFh, 3 hits
    SM00563 PlsC, 1 hit
    SUPFAMiSSF47473 SSF47473, 1 hit
    PROSITEiView protein in PROSITE
    PS00018 EF_HAND_1, 1 hit
    PS50222 EF_HAND_2, 2 hits

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPCAT1_MOUSE
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q3TFD2
    Secondary accession number(s): Q3TAX4
    , Q6NXZ6, Q8BG23, Q8BUX7, Q99JU6
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: October 11, 2005
    Last modified: October 16, 2019
    This is version 134 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    UniProt is an ELIXIR core data resource
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