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UniProtKB - Q3TFD2 (PCAT1_MOUSE)

Entry version 144 (29 Sep 2021)
Sequence version 1 (11 Oct 2005)
Previous versions | rss
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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

Exhibits both acyltransferase and acetyltransferase activities (PubMed:16704971, PubMed:18285344, PubMed:18156367).

Activity is calcium-independent (PubMed:16704971, PubMed:18285344).

Catalyzes the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:16704971, PubMed:18285344, PubMed:18156367).

Catalyzes the conversion 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity).

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).

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: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 (PubMed:18285344). Inhibited by Cu2+, Fe2+, Ca2+ and Mg2+ (PubMed:18285344, PubMed:18156367). Activity is not affected by Co2+ or Mn2+ (PubMed:18285344).2 Publications

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
2.3.1.51, 3474
2.3.1.62, 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:2.3.1.233 Publications)
Short name:
LPC acyltransferase 1
Short name:
LPCAT-1
Short name:
LysoPC acyltransferase 1
Short name:
mLPCAT1
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase (EC:2.3.1.51By similarity)
1-acylglycerophosphocholine O-acyltransferase
1-alkenylglycerophosphocholine O-acyltransferase (EC:2.3.1.252 Publications)
1-alkylglycerophosphocholine O-acetyltransferase (EC:2.3.1.671 Publication)
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000021608

<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

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

Cell membrane, 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 or proteolytic cleavage.<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

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		294337 [Q3TFD2-1]
294338 [Q3TFD2-2]
294339 [Q3TFD2-3]

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 primary oocyte and 306 other tissues

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, 6 interactors

Molecular INTeraction database

More...MINTi		Q3TFD2

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000022099

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q3TFD2, protein

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 25DisorderedSequence analysisAdd BLAST25

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 motif1 Publication6
Motifi531 – 534Di-lysine motif1 Publication4

<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 di-lysine motif may confer endoplasmic reticulum localization.1 Publication
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphocholine.1 Publication

<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

Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4666, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT01030000234574

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_025017_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q3TFD2

Identification of Orthologs from Complete Genome Data

More...OMAi		WMTVKGR

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
PF13833, EF-hand_8, 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.

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.

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
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>
D6RFA8D6RFA8_MOUSE
Lysophosphatidylcholine acyltransfe...
Lpcat1
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>

<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, 6 interactors
MINTiQ3TFD2
STRINGi10090.ENSMUSP00000022099

Chemistry databases

SwissLipidsiSLP:000000297

PTM databases

iPTMnetiQ3TFD2
PhosphoSitePlusiQ3TFD2
SwissPalmiQ3TFD2

Proteomic databases

EPDiQ3TFD2
MaxQBiQ3TFD2
PaxDbiQ3TFD2
PeptideAtlasiQ3TFD2
PRIDEiQ3TFD2
ProteomicsDBi294337 [Q3TFD2-1]
294338 [Q3TFD2-2]
294339 [Q3TFD2-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1587, 222 antibodies

The DNASU plasmid repository

More...DNASUi		210992

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
VEuPathDBiHostDB:ENSMUSG00000021608

Phylogenomic databases

eggNOGiKOG4666, Eukaryota
GeneTreeiENSGT01030000234574
HOGENOMiCLU_025017_0_1_1
InParanoidiQ3TFD2
OMAiWMTVKGR
OrthoDBi1266853at2759
PhylomeDBiQ3TFD2
TreeFamiTF323244

Enzyme and pathway databases

UniPathwayiUPA00085
BRENDAi2.3.1.23, 3474
2.3.1.51, 3474
2.3.1.62, 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

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		210992, 3 hits in 65 CRISPR screens

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
RNActiQ3TFD2, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000021608, Expressed in primary oocyte and 306 other tissues
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
PF13833, EF-hand_8, 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

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: September 29, 2021
This is version 144 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

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
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