Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 130 (07 Oct 2020)
Sequence version 1 (01 Dec 2001)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Lysophospholipid acyltransferase 5

Gene

Lpcat3

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

Lysophospholipid O-acyltransferase (LPLAT) that catalyzes the reacylation step of the phospholipid remodeling process also known as the Lands cycle (PubMed:18287005, PubMed:25898003). Catalyzes transfer of the fatty acyl chain from fatty acyl-CoA to 1-acyl lysophospholipid to form various classes of phospholipids. Converts 1-acyl lysophosphatidylcholine (LPC) into phosphatidylcholine (PC) (LPCAT activity), 1-acyl lysophosphatidylserine (LPS) into phosphatidylserine (PS) (LPSAT activity) and 1-acyl lysophosphatidylethanolamine (LPE) into phosphatidylethanolamine (PE) (LPEAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs (PubMed:18287005, PubMed:25898003). Has higher activity for LPC acyl acceptors compared to LPEs and LPSs (PubMed:18287005). Can also transfer the fatty acyl chain from fatty acyl-CoA to 1-O-alkyl lysophospholipid or 1-O-alkenyl lysophospholipid with lower efficiency (PubMed:18287005). Acts as a major LPC O-acyltransferase in liver and intestine (PubMed:25898003, PubMed:26833026). As a component of the liver X receptor/NR1H3 or NR1H2 signaling pathway, mainly catalyzes the incorporation of arachidonate into PCs of endoplasmic reticulum (ER) membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles (PubMed:25806685). Promotes processing of sterol regulatory protein SREBF1 in hepatocytes, likely by facilitating the translocation of SREBF1-SCAP complex from ER to the Golgi apparatus (PubMed:28846071). Participates in mechanisms by which the liver X receptor/NR1H3 or NR1H2 signaling pathway counteracts lipid-induced ER stress response and inflammation (PubMed:24206663). Downregulates hepatic inflammation by limiting arachidonic acid availability for synthesis of inflammatory eicosanoids, such as prostaglandins (PubMed:24206663). In enterocytes, acts as a component of a gut-brain feedback loop that coordinates dietary lipid absorption and food intake. Regulates the abundance of PCs containing linoleate and arachidonate in enterocyte membranes, enabling passive diffusion of fatty acids and cholesterol across the membrane for efficient chylomicron assembly (PubMed:26833026). In the intestinal crypt, acts as a component of dietary-responsive phospholipid-cholesterol axis, regulating the biosynthesis of cholesterol and its mitogenic effects on intestinal stem cells (PubMed:29395055).7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 '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=7.8 µM for arachidonoyl-CoA (in the presence of LPC C16:0 as cosubstrate)1 Publication
  2. KM=44.1 µM for arachidonoyl-CoA (in the presence of LPE C18:1 as cosubstrate)1 Publication
  3. KM=28 µM for arachidonoyl-CoA (in the presence of LPS C18:1 as cosubstrate)1 Publication
  4. KM=34.5 µM for LPC C16:0 (in the presence of arachidonoyl-CoA as cosubstrate)1 Publication
  5. KM=29.7 µM for LPE C18:1 (in the presence of arachidonoyl-CoA as cosubstrate)1 Publication
  6. KM=22.3 µM for LPS C18:1 (in the presence of arachidonoyl-CoA as cosubstrate)1 Publication
  1. Vmax=1085.5 nmol/min/mg enzyme with arachidonoyl-CoA and LPC C16:0 as substrates1 Publication
  2. Vmax=389.25 nmol/min/mg enzyme with arachidonoyl-CoA and LPE C18:1 as substrates1 Publication
  3. Vmax=335.75 nmol/min/mg enzyme with arachidonoyl-CoA and LPS C18:1 as substrates1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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.2 Publications
View all proteins of this organism that are known to be involved in the pathway phospholipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei338By similarity1
Active sitei374By similarity1

<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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.1.23, 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1482788, Acyl chain remodelling of PC
R-MMU-1482801, Acyl chain remodelling of PS
R-MMU-1482839, Acyl chain remodelling of PE

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:000000286

<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%5Fand%5Ftaxonomy%5Fsection">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:
Lysophospholipid acyltransferase 5 (EC:2.3.1.-2 Publications)
Short name:
LPLAT 5
Alternative name(s):
1-acylglycerophosphocholine O-acyltransferase (EC:2.3.1.232 Publications)
1-acylglycerophosphoethanolamine O-acyltransferase (EC:2.3.1.n71 Publication)
1-acylglycerophosphoserine O-acyltransferase (EC:2.3.1.n61 Publication)
Lysophosphatidylcholine acyltransferase
Short name:
LPCAT
Short name:
Lyso-PC acyltransferase
Lysophosphatidylcholine acyltransferase 3
Short name:
Lyso-PC acyltransferase 3
Short name:
mLPCAT3
Lysophosphatidylethanolamine acyltransferase
Short name:
LPEAT
Short name:
Lyso-PE acyltransferase
Lysophosphatidylserine acyltransferase
Short name:
LPSAT
Short name:
Lyso-PS acyltransferase
Membrane-bound O-acyltransferase domain-containing protein 5
Short name:
O-acyltransferase domain-containing protein 5
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Lpcat3
Synonyms:Grcc3fImported, Mboat5, Oact5
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 6

Organism-specific databases

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

More...
MGIi
MGI:1315211, Lpcat3

<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%5Flocation%5Fsection">'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>Transmembranei44 – 64HelicalSequence analysisAdd BLAST21
Transmembranei84 – 104HelicalSequence analysisAdd BLAST21
Transmembranei111 – 131HelicalSequence analysisAdd BLAST21
Transmembranei180 – 200HelicalSequence analysisAdd BLAST21
Transmembranei236 – 256HelicalSequence analysisAdd BLAST21
Transmembranei285 – 305HelicalSequence analysisAdd BLAST21
Transmembranei364 – 384HelicalSequence analysisAdd BLAST21
Transmembranei422 – 442HelicalSequence analysisAdd BLAST21
Transmembranei453 – 473HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, 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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant mice are born at the expected Mendelian frequency, but none survives beyond day 2 due to an extensive triacylglycerol accumulation in enterocytes associated with very low blood glucose levels at birth (P1.5) (PubMed:25806685, PubMed:25898003). Conditional knockdown in intestine results in hyperproliferation of the intestinal crypt and increased susceptibility to intestinal tumorigenesis (PubMed:29395055).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi374H → A: Loss of O-acyltransferase activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1255159

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00002333832 – 487Lysophospholipid acyltransferase 5Add BLAST486

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi225N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi308N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi331N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q91V01

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q91V01

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q91V01

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

More...
PaxDbi
Q91V01

PeptideAtlas

More...
PeptideAtlasi
Q91V01

PRoteomics IDEntifications database

More...
PRIDEi
Q91V01

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q91V01, 3 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q91V01

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

More...
PhosphoSitePlusi
Q91V01

<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

Detected ubiquitously, with high expression levels in small intestine, brown adipose tissue, liver, kidney and testis (PubMed:18287005, PubMed:28846071, PubMed:25898003, PubMed:25806685, PubMed:24206663). Expressed in liver and both proximal and distal small intestine (at protein level) (PubMed:25898003). Expressed in peritoneal macrophages (PubMed:24206663).5 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

Expressed at late embryonic stages between 18.5 and 19.5 dpc in intestine and liver.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

Up-regulated in response to liver X receptor/NR1H3 or NR1H2 agonist GW3965 (PubMed:28846071, PubMed:25898003, PubMed:25806685, PubMed:24206663). Up-regulated in peritoneal macrophages upon exposure to 22(R)-hydroxycholesterol (PubMed:24206663).4 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000004270, Expressed in jejunum and 306 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q91V01, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q91V01, 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
200053, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000004381

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q91V01, protein

<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

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>Motifi484 – 487Di-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 di-lysine motif confers endoplasmic reticulum localization.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

Belongs to the membrane-bound acyltransferase family.Sequence analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2705, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT01000000214520

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_011340_6_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q91V01

KEGG Orthology (KO)

More...
KOi
K13515

Identification of Orthologs from Complete Genome Data

More...
OMAi
TMPHCIL

Database of Orthologous Groups

More...
OrthoDBi
881262at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q91V01

TreeFam database of animal gene trees

More...
TreeFami
TF106143

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004299, MBOAT_fam

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03062, MBOAT, 1 hit

<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%5Flength">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q91V01-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASTADGDMG ETLEQMRGLW PGVEDLSLNK LATSLGASEQ ALRLIFSIFL
60 70 80 90 100
GYPLALFYRH YLFYKDSYLI HLFHTFTGLS IAYFNFGHQF YHSLLCVVLQ
110 120 130 140 150
FLILRLMGRT VTAVITTLCF QMAYLLAGYY YTATGDYDIK WTMPHCVLTL
160 170 180 190 200
KLIGLCIDYY DGGKDGNSLT SEQQKYAIRG VPSLLEVAGF SYFYGAFLVG
210 220 230 240 250
PQFSMNHYMK LVRGQLTDIP GKMPNSTIPA LKRLSLGLVY LVGYTLLSPH
260 270 280 290 300
ITDDYLLTED YDNRPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILSGL
310 320 330 340 350
GFNGFDENGT VRWDACANMK VWLFETTPRF NGTIASFNIN TNAWVARYIF
360 370 380 390 400
KRLKFLGNKE LSQGLSLLFL ALWHGLHSGY LICFQMEFLI VIVEKQVSSL
410 420 430 440 450
IRDSPALSSL ASITALQPFY YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV
460 470 480
YRSIYFLGHV FFLSLLFILP YIHKAMVPRK EKLKKRE
Length:487
Mass (Da):56,147
Last modified:December 1, 2001 - 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:iEBC51DB3734B17C7
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0N4SUM3A0A0N4SUM3_MOUSE
Lysophospholipid acyltransferase 5
Lpcat3
99Annotation 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>

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 conflicti48 – 49IF → SH in AAC36007 (PubMed:9445485).Curated2

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
AY028317 mRNA Translation: AAK20915.1
AB294194 mRNA Translation: BAG12120.1
CH466523 Genomic DNA Translation: EDK99746.1
BC006753 mRNA Translation: AAH06753.2
AC002397 Genomic DNA Translation: AAC36007.1
AK083687 mRNA Translation: BAC38993.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS20523.1

NCBI Reference Sequences

More...
RefSeqi
NP_660112.1, NM_145130.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000004381; ENSMUSP00000004381; ENSMUSG00000004270

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
14792

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:14792

UCSC genome browser

More...
UCSCi
uc009drf.2, mouse

<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
AY028317 mRNA Translation: AAK20915.1
AB294194 mRNA Translation: BAG12120.1
CH466523 Genomic DNA Translation: EDK99746.1
BC006753 mRNA Translation: AAH06753.2
AC002397 Genomic DNA Translation: AAC36007.1
AK083687 mRNA Translation: BAC38993.1
CCDSiCCDS20523.1
RefSeqiNP_660112.1, NM_145130.2

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi200053, 2 interactors
STRINGi10090.ENSMUSP00000004381

Chemistry databases

ChEMBLiCHEMBL1255159
SwissLipidsiSLP:000000286

PTM databases

GlyGeniQ91V01, 3 sites
iPTMnetiQ91V01
PhosphoSitePlusiQ91V01

Proteomic databases

EPDiQ91V01
jPOSTiQ91V01
MaxQBiQ91V01
PaxDbiQ91V01
PeptideAtlasiQ91V01
PRIDEiQ91V01

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
67641, 61 antibodies

Genome annotation databases

EnsembliENSMUST00000004381; ENSMUSP00000004381; ENSMUSG00000004270
GeneIDi14792
KEGGimmu:14792
UCSCiuc009drf.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10162
MGIiMGI:1315211, Lpcat3

Phylogenomic databases

eggNOGiKOG2705, Eukaryota
GeneTreeiENSGT01000000214520
HOGENOMiCLU_011340_6_1_1
InParanoidiQ91V01
KOiK13515
OMAiTMPHCIL
OrthoDBi881262at2759
PhylomeDBiQ91V01
TreeFamiTF106143

Enzyme and pathway databases

UniPathwayiUPA00085
BRENDAi2.3.1.23, 3474
ReactomeiR-MMU-1482788, Acyl chain remodelling of PC
R-MMU-1482801, Acyl chain remodelling of PS
R-MMU-1482839, Acyl chain remodelling of PE

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
14792, 3 hits in 18 CRISPR screens

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

More...
ChiTaRSi
Lpcat3, mouse

Protein Ontology

More...
PROi
PR:Q91V01
RNActiQ91V01, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000004270, Expressed in jejunum and 306 other tissues
ExpressionAtlasiQ91V01, baseline and differential
GenevisibleiQ91V01, MM

Family and domain databases

InterProiView protein in InterPro
IPR004299, MBOAT_fam
PfamiView protein in Pfam
PF03062, MBOAT, 1 hit

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 nameiMBOA5_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: Q91V01
Secondary accession number(s): B1B362, O35131, Q8BNH6
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: December 1, 2001
Last modified: October 7, 2020
This is version 130 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again