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UniProtKB - Q9Z2A7 (DGAT1_MOUSE)

Entry version 160 (23 Feb 2022)
Sequence version 1 (01 May 1999)
Previous versions | rss
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Protein

Diacylglycerol O-acyltransferase 1

Gene

Dgat1

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

Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates (PubMed:15834126, PubMed:19028692, PubMed:20876538, PubMed:22493088, PubMed:28420705).

Highly expressed in epithelial cells of the small intestine and its activity is essential for the absorption of dietary fats (By similarity).

In liver, plays a role in esterifying exogenous fatty acids to glycerol, and is required to synthesize fat for storage (PubMed:15834126).

Also present in female mammary glands, where it produces fat in the milk (By similarity).

May be involved in VLDL (very low density lipoprotein) assembly (By similarity).

In contrast to DGAT2 it is not essential for survival (PubMed:11959864).

Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders (PubMed:19028692).

Exhibits additional acyltransferase activities, includin acyl CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax diester synthases (PubMed:15834126).

Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705).

By similarity6 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 <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: glycerolipid metabolism

This protein is involved in the pathway glycerolipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway glycerolipid 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 describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei401Acyl-CoABy similarity1
Binding sitei415Acyl-CoABy similarity1
<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 sitei4261 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei427Important for catalytic activityBy similarity1
Binding sitei488Acyl-CoABy 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

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 metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.20, 3474

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-1482883, Acyl chain remodeling of DAG and TAG
R-MMU-6798695, Neutrophil degranulation
R-MMU-75109, Triglyceride biosynthesis

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

More...UniPathwayi		UPA00230

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000000302

<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:
Diacylglycerol O-acyltransferase 1Curated (EC:2.3.1.202 Publications)
Alternative name(s):
Acyl-CoA retinol O-fatty-acyltransferase1 Publication (EC:2.3.1.762 Publications)
Short name:
ARAT1 Publication
Short name:
Retinol O-fatty-acyltransferase1 Publication
Diglyceride acyltransferase
<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:Dgat11 PublicationImported
Synonyms:Dgat2 Publications
<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 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%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 15

Organism-specific databases

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

More...MGIi		MGI:1333825, Dgat1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000022555

<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%5Flocation%5Fsection">'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 – 92CytoplasmicCuratedAdd BLAST92
<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>Transmembranei93 – 127Helical; Name=1By similarityAdd BLAST35
Topological domaini128 – 139LumenalCuratedAdd BLAST12
Transmembranei140 – 165Helical; Name=2By similarityAdd BLAST26
Topological domaini166 – 170CytoplasmicCurated5
Transmembranei171 – 193Helical; Name=3By similarityAdd BLAST23
Topological domaini194 – 200LumenalCurated7
Transmembranei201 – 232Helical; Name=4By similarityAdd BLAST32
Topological domaini233 – 284CytoplasmicCuratedAdd BLAST52
Transmembranei285 – 319Helical; Name=5By similarityAdd BLAST35
Topological domaini320 – 326LumenalCurated7
Transmembranei327 – 364Helical; Name=6By similarityAdd BLAST38
Topological domaini365 – 410CytoplasmicCuratedAdd BLAST46
Transmembranei411 – 431Helical; Name=7By similarityAdd BLAST21
Topological domaini432 – 439LumenalCurated8
Transmembranei440 – 458Helical; Name=8By similarityAdd BLAST19
Topological domaini459 – 460CytoplasmicCurated2
Transmembranei461 – 492Helical; Name=9By similarityAdd BLAST32
Topological domaini493 – 498LumenalCurated6

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

Mice are viable and live well, but show substantially reduced levels of triacylglycerides in all tissues (PubMed:10802663, PubMed:11959864, PubMed:11956242). Mice are resistant to obesity when kept on a high-fat diet due to increased energy expenditure: they display reduced postabsorptive chylomicronemia and accumulate neutral-lipid droplets in the cytoplasm of enterocytes (PubMed:10802663, PubMed:11959864, PubMed:11956242). Mice also show increased sensitivity to insulin and to leptin and are protected against insulin resistance (PubMed:11956242). Mutant mice show reduced levels of monoalkyl-monoacylglycerol (MADAG) in the adrenal gland (PubMed:28420705).4 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>Mutagenesisi426H → A: Impairs the ability to synthesize triacylglycerols, as well as retinyl and wax esters, in an in vitro acyltransferase assay. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1075284

<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_00002076551 – 498Diacylglycerol O-acyltransferase 1Add BLAST498

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 residuei20PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9Z2A7

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9Z2A7

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9Z2A7

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

More...PaxDbi		Q9Z2A7

PRoteomics IDEntifications database

More...PRIDEi		Q9Z2A7

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		277318

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9Z2A7

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

More...PhosphoSitePlusi		Q9Z2A7

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000022555, Expressed in intestinal villus and 307 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9Z2A7, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9Z2A7, 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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer or homotetramer; both forms have similar enzymatic activities.

1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		199213, 1 interactor

Protein interaction database and analysis system

More...IntActi		Q9Z2A7, 2 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000023214

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9Z2A7

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9Z2A7, 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		Q9Z2A7

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

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 – 100Involved in homomerization1 PublicationAdd BLAST100
Regioni1 – 66DisorderedBy similarityAdd BLAST66
Regioni128 – 139Extracellular loop 1 (EL1)By similarityAdd BLAST12
Regioni140 – 498MBOAT foldBy similarityAdd BLAST359
Regioni235 – 287Intracellular loop 1 (IL1)By similarityAdd BLAST53
Regioni365 – 410Intracellular loop 2 (IL2)By similarityAdd BLAST46
Regioni385 – 393Acyl-CoA bindingBy similarity9
Regioni391 – 405Amphipathic helix (AH)By similarityAdd BLAST15

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>Motifi371 – 377FYXDWWN motifBy similarity7

<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 disordered N-terminal region is required for the diacylglycerol O-acyltransferase activity and may regulate enzymatic function via its interaction with the MBOAT fold.By similarity
The MBOAT fold forms a reaction chamber in the endoplasmic reticulum membrane that encloses the active sites. The reaction chamber has a tunnel to the cytosolic side and its entrance recognizes the hydrophilic CoA motif of an acyl-CoA molecule. The chamber has separate entrances for each of the two substrates, acyl-CoA and 1,2-diacyl-sn-glycerol.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. Sterol o-acyltransferase subfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0380, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000183081

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_018190_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9Z2A7

Identification of Orthologs from Complete Genome Data

More...OMAi		HAIIVWL

Database of Orthologous Groups

More...OrthoDBi		1275897at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9Z2A7

TreeFam database of animal gene trees

More...TreeFami		TF314921

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027251, Diacylglycerol_acylTrfase1
IPR004299, MBOAT_fam
IPR014371, Oat_ACAT_DAG_ARE

The PANTHER Classification System

More...PANTHERi		PTHR10408, PTHR10408, 1 hit

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000439, Oat_ACAT_DAG_ARE, 1 hit
PIRSF500231, Oat_dag, 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>Sequencei

<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.

Q9Z2A7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGDRGGAGSS RRRRTGSRVS VQGGSGPKVE EDEVRDAAVS PDLGAGGDAP 
        60         70         80         90        100
APAPAPAHTR DKDGRTSVGD GYWDLRCHRL QDSLFSSDSG FSNYRGILNW 
       110        120        130        140        150
CVVMLILSNA RLFLENLIKY GILVDPIQVV SLFLKDPYSW PAPCVIIASN 
       160        170        180        190        200
IFVVAAFQIE KRLAVGALTE QMGLLLHVVN LATIICFPAA VALLVESITP 
       210        220        230        240        250
VGSVFALASY SIMFLKLYSY RDVNLWCRQR RVKAKAVSTG KKVSGAAAQQ 
       260        270        280        290        300
AVSYPDNLTY RDLYYFIFAP TLCYELNFPR SPRIRKRFLL RRVLEMLFFT 
       310        320        330        340        350
QLQVGLIQQW MVPTIQNSMK PFKDMDYSRI IERLLKLAVP NHLIWLIFFY 
       360        370        380        390        400
WFFHSCLNAV AELLQFGDRE FYRDWWNAES VTYFWQNWNI PVHKWCIRHF 
       410        420        430        440        450
YKPMLRHGSS KWVARTGVFL TSAFFHEYLV SVPLRMFRLW AFTAMMAQVP 
       460        470        480        490 
LAWIVGRFFQ GNYGNAAVWV TLIIGQPVAV LMYVHDYYVL NYDAPVGV
Length:498
Mass (Da):56,790
Last modified:May 1, 1999 - 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:iE7B0DD6DDCF1EC2B
GO

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
AF078752 mRNA Translation: AAC72917.1
AK008995 mRNA No translation available.
BC003717 mRNA Translation: AAH03717.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS27573.1

NCBI Reference Sequences

More...RefSeqi		NP_034176.1, NM_010046.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000023214; ENSMUSP00000023214; ENSMUSG00000022555

Database of genes from NCBI RefSeq genomes

More...GeneIDi		13350

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:13350

UCSC genome browser

More...UCSCi		uc007wkn.1, 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
AF078752 mRNA Translation: AAC72917.1
AK008995 mRNA No translation available.
BC003717 mRNA Translation: AAH03717.1
CCDSiCCDS27573.1
RefSeqiNP_034176.1, NM_010046.3

3D structure databases

SMRiQ9Z2A7
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi199213, 1 interactor
IntActiQ9Z2A7, 2 interactors
STRINGi10090.ENSMUSP00000023214

Chemistry databases

BindingDBiQ9Z2A7
ChEMBLiCHEMBL1075284
SwissLipidsiSLP:000000302

PTM databases

iPTMnetiQ9Z2A7
PhosphoSitePlusiQ9Z2A7

Proteomic databases

EPDiQ9Z2A7
jPOSTiQ9Z2A7
MaxQBiQ9Z2A7
PaxDbiQ9Z2A7
PRIDEiQ9Z2A7
ProteomicsDBi277318

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		28443, 321 antibodies from 31 providers

The DNASU plasmid repository

More...DNASUi		13350

Genome annotation databases

EnsembliENSMUST00000023214; ENSMUSP00000023214; ENSMUSG00000022555
GeneIDi13350
KEGGimmu:13350
UCSCiuc007wkn.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8694
MGIiMGI:1333825, Dgat1
VEuPathDBiHostDB:ENSMUSG00000022555

Phylogenomic databases

eggNOGiKOG0380, Eukaryota
GeneTreeiENSGT00950000183081
HOGENOMiCLU_018190_0_0_1
InParanoidiQ9Z2A7
OMAiHAIIVWL
OrthoDBi1275897at2759
PhylomeDBiQ9Z2A7
TreeFamiTF314921

Enzyme and pathway databases

UniPathwayiUPA00230
BRENDAi2.3.1.20, 3474
ReactomeiR-MMU-1482883, Acyl chain remodeling of DAG and TAG
R-MMU-6798695, Neutrophil degranulation
R-MMU-75109, Triglyceride biosynthesis

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		13350, 2 hits in 67 CRISPR screens

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

More...ChiTaRSi		Dgat1, mouse

Protein Ontology

More...PROi		PR:Q9Z2A7
RNActiQ9Z2A7, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000022555, Expressed in intestinal villus and 307 other tissues
ExpressionAtlasiQ9Z2A7, baseline and differential
GenevisibleiQ9Z2A7, MM

Family and domain databases

InterProiView protein in InterPro
IPR027251, Diacylglycerol_acylTrfase1
IPR004299, MBOAT_fam
IPR014371, Oat_ACAT_DAG_ARE
PANTHERiPTHR10408, PTHR10408, 1 hit
PfamiView protein in Pfam
PF03062, MBOAT, 1 hit
PIRSFiPIRSF000439, Oat_ACAT_DAG_ARE, 1 hit
PIRSF500231, Oat_dag, 1 hit

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 nameiDGAT1_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: Q9Z2A7
Secondary accession number(s): Q9D7Q5
<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: October 18, 2001
Last sequence update: May 1, 1999
Last modified: February 23, 2022
This is version 160 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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