Q8CJC5 · NEUL3_MOUSE

  • Protein
    E3 ubiquitin-protein ligase NEURL3
  • Gene
    Neurl3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

E3 ubiquitin-protein ligase that plays a role in various biological processes such as lung development or innate immunity (PubMed:15936721, PubMed:35792897).
Seems to utilize UBE2E1. Promotes innate antiviral response by catalyzing 'Lys-63'-linked ubiquitination of IRF7 (PubMed:35792897).

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Molecular Functionmetal ion binding
Molecular Functionubiquitin protein ligase activity
Biological Processinnate immune response
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase NEURL3
  • EC number
  • Alternative names
    • Lung-inducible neuralized-related C3CH4 RING domain protein
    • Neuralized-like protein 3
    • RING-type E3 ubiquitin transferase NEURL3

Gene names

    • Name
      Neurl3
    • Synonyms
      Lincr

Organism names

  • Taxonomic identifier
  • Strains
    • Swiss Webster
    • C57BL/6J
    • NOD
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8CJC5
  • Secondary accessions
    • Q8BS05

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Mutant mice produce less type I IFNs and exhibit increased susceptibility to viral infection.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 12 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003257721-254E3 ubiquitin-protein ligase NEURL3

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in alveolar epithelial type II cells.

Induction

Induced in lung during endotoxemia. By LPS and inflammatory cytokines in alveolar epithelial type II cells.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, zinc finger.

TypeIDPosition(s)Description
Domain17-174NHR
Zinc finger197-236RING-type

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8CJC5-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    254
  • Mass (Da)
    28,040
  • Last updated
    2003-03-01 v1
  • Checksum
    A24DE91AC3C0E77E
MGSLLSPEANAEVPREALSFHGNATGAQVHLDDQRSTARRRSTFHDGIVFSQRPVWPGERVALRVLRHEEGWCGGLRVGFTRLDPAQVAASCLPPFVCPDLEEQSPTWAALLPEGFVRAGNVVCFWVNRRGWLFAKVNAGRPLLLRKDVLVQGAPLWAVMDVYGTTKAIELLDPKANAWIRSGEPVPESEVISGEECVICFHNTANTRLMPCGHSHFCGSCAWHIFKDTARCPICRWQIEEVAVVSSLKAEEGS

Q8CJC5-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 173-195: DPKANAWIRSGEPVPESEVISGE → GETPWGPDTECGMETKVQMTSC
    • 196-254: Missing

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A087WP78A0A087WP78_MOUSENeurl3195

Sequence caution

The sequence BAC30757.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict148in Ref. 2; BAC30757
Alternative sequenceVSP_032400173-195in isoform 2
Alternative sequenceVSP_032401196-254in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF321278
EMBL· GenBank· DDBJ
AAN16205.1
EMBL· GenBank· DDBJ
mRNA
AK040949
EMBL· GenBank· DDBJ
BAC30757.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK156207
EMBL· GenBank· DDBJ
BAE33626.1
EMBL· GenBank· DDBJ
mRNA
BC056622
EMBL· GenBank· DDBJ
AAH56622.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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