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 175 (29 Sep 2021)
Sequence version 2 (25 Jul 2003)
Previous versions | rss
Add a publicationFeedback
Protein

Diacylglycerol O-acyltransferase 1

Gene

DGAT1

Organism
Homo sapiens (Human)
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:16214399, PubMed:18768481, PubMed:28420705, PubMed:9756920, PubMed:32433611, PubMed:32433610).

Highly expressed in epithelial cells of the small intestine and its activity is essential for the absorption of dietary fats (PubMed:18768481).

In liver, plays a role in esterifying exogenous fatty acids to glycerol, and is required to synthesize fat for storage (PubMed:16214399).

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 (PubMed:18768481).

In contrast to DGAT2 it is not essential for survival (By similarity).

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:16214399).

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

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_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

XP620 is a selective DGAT1 inhibitor.1 Publication

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

  1. KM=25.9 µM for retinol1 Publication
  2. KM=13.9 µM for palmitoyl coenzyme A1 Publication
  3. KM=14.6 µM for (9Z)-octadecenoyl-CoA1 Publication
  4. KM=8.6 µM for octadecanoyl-CoA1 Publication
  5. KM=6.4 µM for hexadecanoyl-coA1 Publication
  6. KM=6.2 µM for (9Z)-hexadecenoyl-CoA1 Publication
  7. KM=597.1 µM for 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homodimer)1 Publication
  8. KM=497.5 µM for 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homotetramer)1 Publication
  1. Vmax=956.6 pmol/min/µg enzyme with (9Z)-octadecenoyl-CoA as substrate1 Publication
  2. Vmax=839.4 pmol/min/µg enzyme with octadecanoyl-CoA as substrate1 Publication
  3. Vmax=767.8 pmol/min/µg enzyme with hexadecanoyl-coA as substrate1 Publication
  4. Vmax=838.6 pmol/min/µg enzyme with (9Z)-hexadecenoyl-CoA as substrate1 Publication
  5. Vmax=3310 pmol/min/µg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homodimer) as substrate1 Publication
  6. Vmax=3628 pmol/min/µg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homotetramer) as substrate1 Publication

<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: 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_section">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 sitei390Acyl-CoACombined sources2 Publications1
Binding sitei404Acyl-CoACombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei4151 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>Sitei416Important for catalytic activity1 Publication1
Binding sitei477Acyl-CoACombined sources1 Publication1

<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 metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.1.20, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
O75907

Reactome - a knowledgebase of biological pathways and processes

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O75907

SIGNOR Signaling Network Open Resource

More...
SIGNORi
O75907

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

More...
UniPathwayi
UPA00230

Protein family/group databases

Transport Classification Database

More...
TCDBi
2.A.50.4.1, the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000308

<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:
Diacylglycerol O-acyltransferase 1Curated (EC:2.3.1.203 Publications)
Alternative name(s):
ACAT-related gene product 1
Acyl-CoA retinol O-fatty-acyltransferase1 Publication (EC:2.3.1.761 Publication)
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_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:DGAT11 PublicationImported
Synonyms:AGRP11 Publication, DGAT
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 8

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2843, DGAT1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
604900, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O75907

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000185000

<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 – 83Cytoplasmic2 PublicationsAdd BLAST83
<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>Transmembranei84 – 118Helical; Name=1Combined sources2 PublicationsAdd BLAST35
Topological domaini119 – 130Lumenal2 PublicationsAdd BLAST12
Transmembranei131 – 156Helical; Name=2Combined sources2 PublicationsAdd BLAST26
Topological domaini157 – 161Cytoplasmic2 Publications5
Transmembranei162 – 184Helical; Name=3Combined sources2 PublicationsAdd BLAST23
Topological domaini185 – 191Lumenal2 Publications7
Transmembranei192 – 223Helical; Name=4Combined sources2 PublicationsAdd BLAST32
Topological domaini224 – 273Cytoplasmic2 PublicationsAdd BLAST50
Transmembranei274 – 308Helical; Name=5Combined sources2 PublicationsAdd BLAST35
Topological domaini309 – 315Lumenal2 Publications7
Transmembranei316 – 353Helical; Name=6Combined sources2 PublicationsAdd BLAST38
Topological domaini354 – 399Cytoplasmic2 PublicationsAdd BLAST46
Transmembranei400 – 420Helical; Name=7Combined sources2 PublicationsAdd BLAST21
Topological domaini421 – 428Lumenal2 Publications8
Transmembranei429 – 447Helical; Name=8Combined sources2 PublicationsAdd BLAST19
Topological domaini448 – 449Cytoplasmic2 Publications2
Transmembranei450 – 481Helical; Name=9Combined sources2 PublicationsAdd BLAST32
Topological domaini482 – 488Lumenal2 Publications7

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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Diarrhea 7, protein-losing enteropathy type (DIAR7)2 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA life-threatening disease characterized by severe, intractable, watery diarrhea.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_082141458 – 488Missing in DIAR7; unknown pathological significance. 1 PublicationAdd BLAST31

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>Mutagenesisi346L → W: Strongly reduced diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi371T → A: Decreased diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi375Q → A: Slightly decreased diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi377W → F: Abolished diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi378N → A or L: Abolished diacylglycerol O-acyltransferase activity. 2 Publications1
Mutagenesisi381V → A: Does not affect diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi381V → W: Decreased diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi382H → A: Decreased diacylglycerol O-acyltransferase activity. 2 Publications1
Mutagenesisi385C → W: Decreased diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi386I → A: Slightly decreased diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi390Y → A: Decreased diacylglycerol O-acyltransferase activity. 2 Publications1
Mutagenesisi391K → A: Slightly decreased diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi400K → L: Decreased diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi404R → A: Does not affect diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi404R → L: Decreased diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi407V → F: Decreased diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi411S → A or W: Abolished diacylglycerol O-acyltransferase activity. 2 Publications1
Mutagenesisi411S → I: Decreased diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi415H → A: Abolished diacylglycerol O-acyltransferase activity. 2 Publications1
Mutagenesisi416E → A: Abolished diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi434M → A or I: Reduced diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi437Q → A: Reduced diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi465Q → A: Reduced diacylglycerol O-acyltransferase activity. 1 Publication1
Mutagenesisi469V → A: Slightly decreased diacylglycerol O-acyltransferase activity. 1 Publication1

Keywords - Diseasei

Disease variant

Organism-specific databases

DisGeNET

More...
DisGeNETi
8694

MalaCards human disease database

More...
MalaCardsi
DGAT1
MIMi615863, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000185000

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
329242, Congenital chronic diarrhea with protein-losing enteropathy

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27303

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
O75907, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL6009

DrugCentral

More...
DrugCentrali
O75907

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2821

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
DGAT1

<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_00002076541 – 488Diacylglycerol O-acyltransferase 1Add BLAST488

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 residuei17PhosphoserineCombined sources1
Modified residuei18PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O75907

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O75907

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
O75907

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O75907

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

More...
PaxDbi
O75907

PeptideAtlas

More...
PeptideAtlasi
O75907

PRoteomics IDEntifications database

More...
PRIDEi
O75907

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
50257

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O75907

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

More...
PhosphoSitePlusi
O75907

<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
ENSG00000185000, Expressed in small intestine and 115 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O75907, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O75907, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000185000, Tissue enriched (intestine)

<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_section">'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_section">'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.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
114241, 19 interactors

Protein interaction database and analysis system

More...
IntActi
O75907, 13 interactors

Molecular INTeraction database

More...
MINTi
O75907

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000482264

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O75907

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
O75907, 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

Secondary structure

1488
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
O75907

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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 – 91Involved in homomerizationBy similarityAdd BLAST91
Regioni1 – 57Disordered1 PublicationAdd BLAST57
Regioni119 – 130Extracellular loop 1 (EL1)1 PublicationAdd BLAST12
Regioni131 – 488MBOAT fold1 PublicationAdd BLAST358
Regioni224 – 276Intracellular loop 1 (IL1)1 PublicationAdd BLAST53
Regioni354 – 399Intracellular loop 2 (IL2)1 PublicationAdd BLAST46
Regioni374 – 382Acyl-CoA bindingCombined sources2 Publications9
Regioni380 – 394Amphipathic helix (AH)1 PublicationAdd 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>Motifi360 – 366FYXDWWN motif1 Publication7

<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.2 Publications
The MBOAT fold forms a reaction chamber in the endoplasmic reticulum membrane that encloses the active sites (PubMed:32433611, PubMed:32433610). The reaction chamber has a tunnel to the cytosolic side and its entrance recognizes the hydrophilic CoA motif of an acyl-CoA molecule (PubMed:32433610). The chamber has separate entrances for each of the two substrates, acyl-CoA and 1,2-diacyl-sn-glycerol (PubMed:32433610).2 Publications

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

Keywords - Domaini

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
O75907

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
O75907

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_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>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O75907-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGDRGSSRRR RTGSRPSSHG GGGPAAAEEE VRDAAAGPDV GAAGDAPAPA
60 70 80 90 100
PNKDGDAGVG SGHWELRCHR LQDSLFSSDS GFSNYRGILN WCVVMLILSN
110 120 130 140 150
ARLFLENLIK YGILVDPIQV VSLFLKDPYS WPAPCLVIAA NVFAVAAFQV
160 170 180 190 200
EKRLAVGALT EQAGLLLHVA NLATILCFPA AVVLLVESIT PVGSLLALMA
210 220 230 240 250
HTILFLKLFS YRDVNSWCRR ARAKAASAGK KASSAAAPHT VSYPDNLTYR
260 270 280 290 300
DLYYFLFAPT LCYELNFPRS PRIRKRFLLR RILEMLFFTQ LQVGLIQQWM
310 320 330 340 350
VPTIQNSMKP FKDMDYSRII ERLLKLAVPN HLIWLIFFYW LFHSCLNAVA
360 370 380 390 400
ELMQFGDREF YRDWWNSESV TYFWQNWNIP VHKWCIRHFY KPMLRRGSSK
410 420 430 440 450
WMARTGVFLA SAFFHEYLVS VPLRMFRLWA FTGMMAQIPL AWFVGRFFQG
460 470 480
NYGNAAVWLS LIIGQPIAVL MYVHDYYVLN YEAPAAEA
Length:488
Mass (Da):55,278
Last modified:July 25, 2003 - v2
<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:i6574D5DBF15D6171
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
A0A0A0MR74A0A0A0MR74_HUMAN
Diacylglycerol O-acyltransferase 1
DGAT1
315Annotation score:

Annotation score:2 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 conflicti129Y → H in AAC63997 (PubMed:9756920).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_082141458 – 488Missing in DIAR7; unknown pathological significance. 1 PublicationAdd BLAST31

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
AF059202 mRNA Translation: AAC63997.1
AB057815 mRNA Translation: BAC66170.1
CH471162 Genomic DNA Translation: EAW82127.1
CH471162 Genomic DNA Translation: EAW82129.1
BC015762 mRNA Translation: AAH15762.1
BC023565 mRNA Translation: AAH23565.1
BC150649 mRNA Translation: AAI50650.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS6420.1

NCBI Reference Sequences

More...
RefSeqi
NP_036211.2, NM_012079.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000528718; ENSP00000482264; ENSG00000185000
ENST00000644790; ENSP00000495489; ENSG00000285482

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8694

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:8694

UCSC genome browser

More...
UCSCi
uc003zbv.5, human

<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
AF059202 mRNA Translation: AAC63997.1
AB057815 mRNA Translation: BAC66170.1
CH471162 Genomic DNA Translation: EAW82127.1
CH471162 Genomic DNA Translation: EAW82129.1
BC015762 mRNA Translation: AAH15762.1
BC023565 mRNA Translation: AAH23565.1
BC150649 mRNA Translation: AAI50650.1
CCDSiCCDS6420.1
RefSeqiNP_036211.2, NM_012079.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6VP0electron microscopy3.10C/E1-488[»]
6VYIelectron microscopy3.00A/B1-488[»]
6VZ1electron microscopy3.20A/B1-488[»]
SMRiO75907
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114241, 19 interactors
IntActiO75907, 13 interactors
MINTiO75907
STRINGi9606.ENSP00000482264

Chemistry databases

BindingDBiO75907
ChEMBLiCHEMBL6009
DrugCentraliO75907
GuidetoPHARMACOLOGYi2821
SwissLipidsiSLP:000000308

Protein family/group databases

TCDBi2.A.50.4.1, the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family

PTM databases

iPTMnetiO75907
PhosphoSitePlusiO75907

Genetic variation databases

BioMutaiDGAT1

Proteomic databases

EPDiO75907
jPOSTiO75907
MassIVEiO75907
MaxQBiO75907
PaxDbiO75907
PeptideAtlasiO75907
PRIDEiO75907
ProteomicsDBi50257

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
28443, 320 antibodies

The DNASU plasmid repository

More...
DNASUi
8694

Genome annotation databases

EnsembliENST00000528718; ENSP00000482264; ENSG00000185000
ENST00000644790; ENSP00000495489; ENSG00000285482
GeneIDi8694
KEGGihsa:8694
UCSCiuc003zbv.5, human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8694
DisGeNETi8694

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DGAT1
HGNCiHGNC:2843, DGAT1
HPAiENSG00000185000, Tissue enriched (intestine)
MalaCardsiDGAT1
MIMi604900, gene
615863, phenotype
neXtProtiNX_O75907
OpenTargetsiENSG00000185000
Orphaneti329242, Congenital chronic diarrhea with protein-losing enteropathy
PharmGKBiPA27303
VEuPathDBiHostDB:ENSG00000185000

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0380, Eukaryota
GeneTreeiENSGT00950000183081
HOGENOMiCLU_018190_0_0_1
InParanoidiO75907
OMAiHAIIVWL
OrthoDBi1275897at2759
PhylomeDBiO75907
TreeFamiTF314921

Enzyme and pathway databases

UniPathwayiUPA00230
BRENDAi2.3.1.20, 2681
PathwayCommonsiO75907
ReactomeiR-HSA-1482883, Acyl chain remodeling of DAG and TAG
R-HSA-6798695, Neutrophil degranulation
R-HSA-75109, Triglyceride biosynthesis
SABIO-RKiO75907
SIGNORiO75907

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
8694, 12 hits in 1013 CRISPR screens

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

More...
ChiTaRSi
DGAT1, human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
8694
PharosiO75907, Tclin

Protein Ontology

More...
PROi
PR:O75907
RNActiO75907, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000185000, Expressed in small intestine and 115 other tissues
ExpressionAtlasiO75907, baseline and differential
GenevisibleiO75907, HS

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_HUMAN
<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: O75907
Secondary accession number(s): B2RWQ2, D3DWL6, Q96BB8
<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: October 18, 2001
Last sequence update: July 25, 2003
Last modified: September 29, 2021
This is version 175 of the entry and version 2 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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