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UniProtKB - O88908 (SOAT2_MOUSE)

Entry version 140 (02 Dec 2020)
Sequence version 2 (27 Jul 2011)
Previous versions | rss
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Protein

Sterol O-acyltransferase 2

Gene

Soat2

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 formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.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

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 sitei118CholesterolBy similarity1
Binding sitei392Acyl-CoABy similarity1
Binding sitei395Acyl-CoABy similarity1
Binding sitei398Acyl-CoABy similarity1
Binding sitei402Acyl-CoABy similarity1
Binding sitei410Acyl-CoABy similarity1
Binding sitei433Acyl-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 sitei437By 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 processCholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.26, 3474

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-8964038, LDL clearance

<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:
Sterol O-acyltransferase 2Curated (EC:2.3.1.26By similarity)
Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase 2
Short name:
ACAT-2
Cholesterol acyltransferase 2
<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:Soat2Imported
Synonyms:Acact-2, Acat2
<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:1332226, Soat2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the 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 – 119CytoplasmicCuratedAdd BLAST119
<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>Transmembranei120 – 141Helical; Name=1By similarityAdd BLAST22
Topological domaini142 – 161LumenalCuratedAdd BLAST20
Transmembranei162 – 187Helical; Name=2By similarityAdd BLAST26
Topological domaini188 – 199CytoplasmicCuratedAdd BLAST12
Transmembranei200 – 223Helical; Name=3By similarityAdd BLAST24
Topological domaini224 – 231LumenalCurated8
Transmembranei232 – 255Helical; Name=4By similarityAdd BLAST24
Topological domaini256 – 296CytoplasmicCuratedAdd BLAST41
Transmembranei297 – 329Helical; Name=5By similarityAdd BLAST33
Topological domaini330 – 346LumenalCuratedAdd BLAST17
Transmembranei347 – 372Helical; Name=6By similarityAdd BLAST26
Topological domaini373 – 420CytoplasmicCuratedAdd BLAST48
Transmembranei421 – 445Helical; Name=7By similarityAdd BLAST25
Topological domaini446 – 451LumenalCurated6
Transmembranei452 – 467Helical; Name=8By similarityAdd BLAST16
Topological domaini468 – 473CytoplasmicCurated6
Transmembranei474 – 505Helical; Name=9By similarityAdd BLAST32
Topological domaini506 – 525LumenalCuratedAdd BLAST20

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 more susceptible to high-fat diet-induced insulin resistance.1 Publication

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2653

<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_00002076461 – 525Sterol O-acyltransferase 2Add BLAST525

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 residuei280Cysteine sulfenic acid (-SOH); alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki280Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Polyubiquitinated by AMFR/gp78 at Cys-280, leading to its degradation when the lipid levels are low. Association with AMFR/gp78 is mediated via interaction with INSIG1. High concentration of cholesterol and fatty acid results in Cys-280 oxidation, preventing ubiquitination at the same site, resulting in protein stabilization.By similarity
Oxidized at Cys-280: high concentration of cholesterol and fatty acid induce reactive oxygen species, which oxidizes Cys-280, preventing ubiquitination at the same site, and resulting in protein stabilization.By similarity

Keywords - PTMi

Oxidation, Thioester bond, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O88908

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O88908

MaxQB - The MaxQuant DataBase

More...MaxQBi		O88908

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

More...PaxDbi		O88908

PRoteomics IDEntifications database

More...PRIDEi		O88908

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O88908

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

More...PhosphoSitePlusi		O88908

SwissPalm database of S-palmitoylation events

More...SwissPalmi		O88908

<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		ENSMUSG00000023045, Expressed in jejunum and 80 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O88908, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O88908, 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

May form homo- or heterodimers (By similarity).

Interacts with INSIG1; the interaction is direct and promotes association with AMFR/gp78 (By similarity).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000023806

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O88908, protein

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi380 – 386FYXDWWN 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

Each protomer consists of 9 transmembrane segments, which enclose a cytosolic tunnel and a transmembrane tunnel that converge at the predicted catalytic site: acyl-CoA enters the active site through the cytosolic tunnel, whereas cholesterol enters from the side through the transmembrane tunnel.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_031845_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O88908

Identification of Orthologs from Complete Genome Data

More...OMAi		TMNDRHT

Database of Orthologous Groups

More...OrthoDBi		1275897at2759

TreeFam database of animal gene trees

More...TreeFami		TF315226

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004299, MBOAT_fam
IPR014371, Oat_ACAT_DAG_ARE
IPR030687, Sterol_acyltranf_meta

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
PIRSF500230, Sterol_acyltranf_ACAT, 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

O88908-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQPKVPQLRR REGLGEEQEK GARGGEGNAR THGTPDLVQW TRHMEAVKTQ 
        60         70         80         90        100
FLEQAQRELA ELLDRALWEA MQAYPKQDRP LPSAAPDSTS KTQELHPGKR 
       110        120        130        140        150
KVFITRKSLI DELMEVQHFR TIYHMFIAGL CVLIISTLAI DFIDEGRLML 
       160        170        180        190        200
EFDLLLFSFG QLPLALMTWV PMFLSTLLVP YQTLWLWARP RAGGAWMLGA 
       210        220        230        240        250
SLGCVLLAAH AVVLCVLPVH VSVRHELPPA SRCVLVFEQV RLLMKSYSFL 
       260        270        280        290        300
RETVPGIFCV RGGKGISPPS FSSYLYFLFC PTLIYRETYP RTPSIRWNYV 
       310        320        330        340        350
AKNFAQVLGC LLYACFILGR LCVPVFANMS REPFSTRALL LSILHATGPG 
       360        370        380        390        400
IFMLLLIFFA FLHCWLNAFA EMLRFGDRMF YRDWWNSTSF SNYYRTWNVV 
       410        420        430        440        450
VHDWLYSYVY QDGLWLLGRR ARGVAMLGVF LVSAVVHEYI FCFVLGFFYP 
       460        470        480        490        500
VMLMLFLVFG GLLNFTMNDR HTGPAWNILM WTFLFMGQGI QVSLYCQEWY 
       510        520 
ARRHCPLPQT TFWGMVTPRS WSCHP
Length:525
Mass (Da):60,597
Last modified:July 27, 2011 - 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:iF1C2DFEB5AB6CCA8
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
F6SMH4F6SMH4_MOUSE
Sterol O-acyltransferase 2
Soat2
284Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti93Q → P in AAC64057 (PubMed:9756919).Curated1
Sequence conflicti96H → R in AAC64057 (PubMed:9756919).Curated1
Sequence conflicti104 – 105IT → VA in AAC64057 (PubMed:9756919).Curated2
Sequence conflicti131 – 132CV → WF in AAC64057 (PubMed:9756919).Curated2
Sequence conflicti175S → Y in AAC64057 (PubMed:9756919).Curated1
Sequence conflicti262G → R in AAC64057 (PubMed:9756919).Curated1
Sequence conflicti519R → Q in AAC64057 (PubMed:9756919).Curated1
Sequence conflicti525P → T in AAC64057 (PubMed:9756919).Curated1

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
AF078751 mRNA Translation: AAC64057.1
CH466550 Genomic DNA Translation: EDL04004.1
BC025931 mRNA Translation: AAH25931.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS27872.1

NCBI Reference Sequences

More...RefSeqi		NP_666176.1, NM_146064.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000023806; ENSMUSP00000023806; ENSMUSG00000023045

Database of genes from NCBI RefSeq genomes

More...GeneIDi		223920

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:223920

UCSC genome browser

More...UCSCi		uc007xut.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
AF078751 mRNA Translation: AAC64057.1
CH466550 Genomic DNA Translation: EDL04004.1
BC025931 mRNA Translation: AAH25931.1
CCDSiCCDS27872.1
RefSeqiNP_666176.1, NM_146064.1

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023806

Chemistry databases

ChEMBLiCHEMBL2653

PTM databases

iPTMnetiO88908
PhosphoSitePlusiO88908
SwissPalmiO88908

Proteomic databases

EPDiO88908
jPOSTiO88908
MaxQBiO88908
PaxDbiO88908
PRIDEiO88908

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		43294, 137 antibodies

Genome annotation databases

EnsembliENSMUST00000023806; ENSMUSP00000023806; ENSMUSG00000023045
GeneIDi223920
KEGGimmu:223920
UCSCiuc007xut.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8435
MGIiMGI:1332226, Soat2

Phylogenomic databases

eggNOGiKOG0380, Eukaryota
GeneTreeiENSGT00950000183081
HOGENOMiCLU_031845_1_0_1
InParanoidiO88908
OMAiTMNDRHT
OrthoDBi1275897at2759
TreeFamiTF315226

Enzyme and pathway databases

BRENDAi2.3.1.26, 3474
ReactomeiR-MMU-8964038, LDL clearance

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		223920, 4 hits in 17 CRISPR screens

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

More...ChiTaRSi		Soat2, mouse

Protein Ontology

More...PROi		PR:O88908
RNActiO88908, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000023045, Expressed in jejunum and 80 other tissues
ExpressionAtlasiO88908, baseline and differential
GenevisibleiO88908, MM

Family and domain databases

InterProiView protein in InterPro
IPR004299, MBOAT_fam
IPR014371, Oat_ACAT_DAG_ARE
IPR030687, Sterol_acyltranf_meta
PANTHERiPTHR10408, PTHR10408, 1 hit
PfamiView protein in Pfam
PF03062, MBOAT, 1 hit
PIRSFiPIRSF000439, Oat_ACAT_DAG_ARE, 1 hit
PIRSF500230, Sterol_acyltranf_ACAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSOAT2_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: O88908
Secondary accession number(s): Q8R0Y9
<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: July 27, 2011
Last modified: December 2, 2020
This is version 140 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

<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. SIMILARITY comments
    Index of protein domains and families
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