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UniProtKB - Q9ERM3 (DGAT1_RAT)

Entry version 121 (23 Feb 2022)
Sequence version 1 (01 Mar 2001)
Previous versions | rss
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Protein

Diacylglycerol O-acyltransferase 1

Gene

Dgat1

Organism
Rattus norvegicus (Rat)
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 transcript 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. Highly expressed in epithelial cells of the small intestine and its activity is essential for the absorption of dietary fats. In liver, plays a role in esterifying exogenous fatty acids to glycerol, and is required to synthesize fat for storage (By similarity).

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 (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 (By similarity).

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) (By similarity).

By similarity

<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 sitei426By similarity1
<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, 5301

Reactome - a knowledgebase of biological pathways and processes

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

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

More...UniPathwayi		UPA00230

<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:2.3.1.20By similarity)
Alternative name(s):
Acyl-CoA retinol O-fatty-acyltransferase (EC:2.3.1.76)
Short name:
ARAT
Short name:
Retinol O-fatty-acyltransferase
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:Dgat1Imported
Synonyms:Dgat
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 › Rattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...RGDi		628673, Dgat1

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL6129

<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_00002076561 – 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

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

More...PaxDbi		Q9ERM3

PeptideAtlas

More...PeptideAtlasi		Q9ERM3

<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.

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000035110

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9ERM3

<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		Q9ERM3

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 – 96Involved in homomerizationBy similarityAdd BLAST96
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

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9ERM3

Database of Orthologous Groups

More...OrthoDBi		1275897at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9ERM3

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>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.

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

Q9ERM3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGDRGGAGSS RRRRTGSRVS VQGGSGPKVE EDEVREAAVS PDLGAGGDAP 
        60         70         80         90        100
APAPAPAHTR DKDRQTSVGD GHWELRCHRL QDSLFSSDSG FSNYRGILNW 
       110        120        130        140        150
CVVMLILSNA RLSLENLIKY GILVDPIQVV SLFLKDPYSW PAPCLIIASN 
       160        170        180        190        200
IFIVATFQIE KRLSVGALTE QMGLLLHVVN LATIICFPAA VALLVESITP 
       210        220        230        240        250
VGSLFALASY SIIFLKLSSY RDVNLWCRQR RVKAKAVSAG KKVSGAAAQN 
       260        270        280        290        300
TVSYPDNLTY RDLYYFIFAP TLCYELNFPR SPRIRKRFLL RRVLEMLFFT 
       310        320        330        340        350
QLQVGLIQQW MVPTIQNSMK PFKDMDYSRI IERLLKLAVP NHLIWLIFFY 
       360        370        380        390        400
WLFHSCLNAV AELLQFGDRE FYRDWWNAES VTYFWQNWNI PVHKWCIRHF 
       410        420        430        440        450
YKPMLRLGSN KWMARTGVFW ASAFFHEYLV SIPLRMFRLW AFTAMMAQVP 
       460        470        480        490 
LAWIVNRFFQ GNYGNAAVWV TLIIGQPVAV LMYVHDYYVL NYDAPVGA
Length:498
Mass (Da):56,870
Last modified:March 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:i5B24DD4AEB87CB4D
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
Q8BHI5Q8BHI5_RAT
O-acyltransferase
Dgat1 DGAT, rCG_59622
500Annotation 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>

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
AF296131 mRNA Translation: AAG10084.1

NCBI Reference Sequences

More...RefSeqi		NP_445889.1, NM_053437.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		84497

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:84497

UCSC genome browser

More...UCSCi		RGD:628673, rat

<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
AF296131 mRNA Translation: AAG10084.1
RefSeqiNP_445889.1, NM_053437.1

3D structure databases

SMRiQ9ERM3
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000035110

Chemistry databases

BindingDBiQ9ERM3
ChEMBLiCHEMBL6129

Proteomic databases

PaxDbiQ9ERM3
PeptideAtlasiQ9ERM3

Genome annotation databases

GeneIDi84497
KEGGirno:84497
UCSCiRGD:628673, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8694
RGDi628673, Dgat1

Phylogenomic databases

eggNOGiKOG0380, Eukaryota
InParanoidiQ9ERM3
OrthoDBi1275897at2759
PhylomeDBiQ9ERM3

Enzyme and pathway databases

UniPathwayiUPA00230
BRENDAi2.3.1.20, 5301
ReactomeiR-RNO-1482883, Acyl chain remodeling of DAG and TAG
R-RNO-6798695, Neutrophil degranulation
R-RNO-75109, Triglyceride biosynthesis

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q9ERM3

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_RAT
<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: Q9ERM3
<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: March 1, 2001
Last modified: February 23, 2022
This is version 121 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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