Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - O35949 (ELOV3_MOUSE)

Entry version 156 (02 Jun 2021)
Sequence version 1 (01 Jan 1998)
Previous versions | rss
Add a publicationFeedback
Protein

Elongation of very long chain fatty acids protein 3

Gene

Elovl3

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 first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated and unsaturated acyl-CoA substrates with higher activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Participates in the formation of certain VLCFA and triglycerides in certain cells of the hair follicles and the sebaceous glands, required for skin barrier function. Critical enzyme for lipid accumulation and metabolic activity in brown adipocytes during the early phase of the tissue recruitment. Plays a role in lipid storage and in resistance to diet-induced obesity.

UniRule annotation4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: polyunsaturated fatty acid biosynthesis

This protein is involved in the pathway polyunsaturated fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway polyunsaturated fatty acid biosynthesis and in Lipid metabolism.

<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 functionTransferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-2046105, Linoleic acid (LA) metabolism
R-MMU-2046106, alpha-linolenic acid (ALA) metabolism
R-MMU-75876, Synthesis of very long-chain fatty acyl-CoAs

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

More...UniPathwayi		UPA00658

<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:
Elongation of very long chain fatty acids protein 3UniRule annotationCurated (EC:2.3.1.199UniRule annotationBy similarity)
Alternative name(s):
3-keto acyl-CoA synthase Elovl3UniRule annotation
CIN-2
Cold-inducible glycoprotein of 30 kDa
ELOVL fatty acid elongase 3UniRule annotation
Short name:
ELOVL FA elongase 3UniRule annotation
Very long chain 3-ketoacyl-CoA synthase 3UniRule annotation
Very long chain 3-oxoacyl-CoA synthase 3UniRule annotation
<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:Elovl3UniRule annotation
Synonyms:Cig30
<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 19

Organism-specific databases

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

More...MGIi		MGI:1195976, Elovl3

<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 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>Transmembranei30 – 50HelicalUniRule annotationAdd BLAST21
Transmembranei67 – 87HelicalUniRule annotationAdd BLAST21
Transmembranei116 – 136HelicalUniRule annotationAdd BLAST21
Transmembranei141 – 161HelicalUniRule annotationAdd BLAST21
Transmembranei165 – 187HelicalUniRule annotationAdd BLAST23
Transmembranei199 – 219HelicalUniRule annotationAdd BLAST21
Transmembranei236 – 256HelicalUniRule annotationAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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

Mutant mice grow normally and are fertile. They display a sparse hair coat, a hyperplastic pilosebaceous system and their hair lipid content is disturbed with exceptionally high levels of eicosenoic acid (20:1). In the triglyceride fraction, fatty acids longer than 20 carbon atoms are almost undetectable. As a result, mice exhibited a severe defect in water repulsion and increased trans-epidermal water loss. When exposed to cold stress, mutants exhibit a significantly reduced VLCFA elongation activity in brown adipose tissue, but only during the initial phase. Cold-acclimated mutants are equally efficient as normal mice at elongating fatty acids. Mutant mice are lean and resistant to diet-induced weight gain, they show normal food intake but increased metabolic rate, and show reduced hepatic lipogenesis and triglycerides synthesis.3 Publications

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5775

<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_00002075411 – 271Elongation of very long chain fatty acids protein 3Add BLAST271

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi6N-linked (GlcNAc...) asparagineUniRule annotation2 Publications1

<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

N-Glycosylated.UniRule annotation1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O35949

MaxQB - The MaxQuant DataBase

More...MaxQBi		O35949

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

More...PaxDbi		O35949

PRoteomics IDEntifications database

More...PRIDEi		O35949

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		277787

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		O35949, 1 site

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O35949

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

More...PhosphoSitePlusi		O35949

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in brown adipose tissue and liver. In the skin, strong expressed in the cells of the inner layer of the outer root sheath of the hair follicles and in the sebocytes of the sebaceous glands. Hardly detectable in the epidermis and not at all in fibroblasts.2 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Strongly up-regulated in brown adipose tissue in conditions of brown fat recruitment, such as cold stress, perinatal development and after diet-induced thermogenesis. A synergistic action of both catecholamines and glucocorticoids is required for the induction.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000038754, Expressed in lip and 88 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O35949, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O35949, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000036357

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O35949

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O35949, 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

<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

<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 ELO family. ELOVL3 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3072, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT01030000234600

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_048483_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O35949

Identification of Orthologs from Complete Genome Data

More...OMAi		QPYNFEL

Database of Orthologous Groups

More...OrthoDBi		1094172at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O35949

TreeFam database of animal gene trees

More...TreeFami		TF106467

Family and domain databases

HAMAP database of protein families

More...HAMAPi		MF_03203, VLCF_elongase_3, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR030457, ELO_CS
IPR002076, ELO_fam
IPR033679, ELOVL3

The PANTHER Classification System

More...PANTHERi		PTHR11157, PTHR11157, 1 hit
PTHR11157:SF68, PTHR11157:SF68, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01151, ELO, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01188, ELO, 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

O35949-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDTSMNFSRG LKMDLMQPYD FETFQDLRPF LEEYWVSSFL IVVVYLLLIV 
        60         70         80         90        100
VGQTYMRTRK SFSLQRPLIL WSFFLAIFSI LGTLRMWKFM ATVMFTVGLK 
       110        120        130        140        150
QTVCFAIYTD DAVVRFWSFL FLLSKVVELG DTAFIILRKR PLIFVHWYHH 
       160        170        180        190        200
STVLLFTSFG YKNKVPSGGW FMTMNFGVHS VMYTYYTMKA AKLKHPNLLP 
       210        220        230        240        250
MVITSLQILQ MVLGTIFGIL NYIWRQEKGC HTTTEHFFWS FMLYGTYFIL 
       260        270 
FAHFFHRAYL RPKGKVASKS Q
Length:271
Mass (Da):32,060
Last modified:January 1, 1998 - 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:iF7CA96199BE89401
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
A0A498WFQ4A0A498WFQ4_MOUSE
Elongation of very long chain fatty...
Elovl3
248Annotation score:

Annotation score:3 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
U97107 mRNA Translation: AAC06127.1
AF054504 Genomic DNA Translation: AAD51088.1
BC016468 mRNA Translation: AAH16468.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS29871.1

NCBI Reference Sequences

More...RefSeqi		NP_031729.1, NM_007703.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000237098; ENSMUSP00000157465; ENSMUSG00000038754

Database of genes from NCBI RefSeq genomes

More...GeneIDi		12686

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:12686

UCSC genome browser

More...UCSCi		uc008hsk.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
U97107 mRNA Translation: AAC06127.1
AF054504 Genomic DNA Translation: AAD51088.1
BC016468 mRNA Translation: AAH16468.1
CCDSiCCDS29871.1
RefSeqiNP_031729.1, NM_007703.2

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000036357

Chemistry databases

BindingDBiO35949
ChEMBLiCHEMBL5775

PTM databases

GlyGeniO35949, 1 site
iPTMnetiO35949
PhosphoSitePlusiO35949

Proteomic databases

jPOSTiO35949
MaxQBiO35949
PaxDbiO35949
PRIDEiO35949
ProteomicsDBi277787

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		31401, 192 antibodies

The DNASU plasmid repository

More...DNASUi		12686

Genome annotation databases

EnsembliENSMUST00000237098; ENSMUSP00000157465; ENSMUSG00000038754
GeneIDi12686
KEGGimmu:12686
UCSCiuc008hsk.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		83401
MGIiMGI:1195976, Elovl3

Phylogenomic databases

eggNOGiKOG3072, Eukaryota
GeneTreeiENSGT01030000234600
HOGENOMiCLU_048483_1_1_1
InParanoidiO35949
OMAiQPYNFEL
OrthoDBi1094172at2759
PhylomeDBiO35949
TreeFamiTF106467

Enzyme and pathway databases

UniPathwayiUPA00658
ReactomeiR-MMU-2046105, Linoleic acid (LA) metabolism
R-MMU-2046106, alpha-linolenic acid (ALA) metabolism
R-MMU-75876, Synthesis of very long-chain fatty acyl-CoAs

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		12686, 0 hits in 52 CRISPR screens

Protein Ontology

More...PROi		PR:O35949
RNActiO35949, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000038754, Expressed in lip and 88 other tissues
ExpressionAtlasiO35949, baseline and differential
GenevisibleiO35949, MM

Family and domain databases

HAMAPiMF_03203, VLCF_elongase_3, 1 hit
InterProiView protein in InterPro
IPR030457, ELO_CS
IPR002076, ELO_fam
IPR033679, ELOVL3
PANTHERiPTHR11157, PTHR11157, 1 hit
PTHR11157:SF68, PTHR11157:SF68, 1 hit
PfamiView protein in Pfam
PF01151, ELO, 1 hit
PROSITEiView protein in PROSITE
PS01188, ELO, 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 nameiELOV3_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: O35949
<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: January 23, 2002
Last sequence update: January 1, 1998
Last modified: June 2, 2021
This is version 156 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again