Q3TBL6 · TP8L3_MOUSE

  • Protein
    Tumor necrosis factor alpha-induced protein 8-like protein 3
  • Gene
    Tnfaip8l3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Acts as a lipid transfer protein. Preferentially captures and shuttles two lipid second messengers, i.e., phosphatidylinositol 4,5- bisphosphate and phosphatidylinositol 3,4,5-trisphosphate and increases their levels in the plasma membrane. Additionally, may also function as a lipid-presenting protein to enhance the activity of the PI3K-AKT and MEK-ERK pathways. May act as a regulator of tumorigenesis through its activation of phospholipid signaling.

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
Cellular Componentcytosol
Cellular Componentnucleoplasm
Cellular Componentplasma membrane
Molecular Functionphosphatidylinositol binding
Molecular Functionphosphatidylinositol transfer activity
Biological Process1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate metabolic process
Biological Processphospholipid transport
Biological Processpositive regulation of ERK1 and ERK2 cascade
Biological Processregulation of apoptotic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tumor necrosis factor alpha-induced protein 8-like protein 3
  • Short names
    TNF alpha-induced protein 8-like protein 3; TNFAIP8-like protein 3

Gene names

    • Name
      Tnfaip8l3

Organism names

  • Taxonomic identifier
  • Strain
    • NOD
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q3TBL6

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Cell membrane
Note: On PDGF activation, translocates from cytoplasm to plasma membrane.

Keywords

Phenotypes & Variants

Disruption phenotype

Deficient mice develop normally during the first 3 months of life under pathogen-free conditions. However, following subcutaneous injection of the carcinogen 3-methylcholanthrene, deficient mice exhibit markedly delayed skin tumor onset and reduced tumor size compared with wild-type mice.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis33Reduces binding to phosphoinositide; when associated with Gln-34; Gln-38 and Gln-42.
Mutagenesis34Reduces binding to phosphoinositide; when associated with Gln-33; Gln-38 and Gln-42.
Mutagenesis38Reduces binding to phosphoinositide; when associated with Gln-33; Gln-34 and Gln-42.
Mutagenesis42Reduces binding to phosphoinositide; when associated with Gln-33; Gln-34 and Gln-38.
Mutagenesis60Reduces binding to phosphoinositide.
Mutagenesis93Reduces binding to phosphoinositide; when associated with Gln-109.
Mutagenesis109Reduces binding to phosphoinositide; when associated with Gln-93.

Variants

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

The viewer provides 10 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_00003314251-204Tumor necrosis factor alpha-induced protein 8-like protein 3

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed (at protein level).

Gene expression databases

    • ENSMUSG00000074345Expressed in dentate gyrus of hippocampal formation granule cell and 32 other cell types or tissues

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-20Disordered
Region21-204Binding to phosphoinositides

Domain

The N-terminal domain (AA 2-20) is essential for its effect on cell growth and survival.

Sequence similarities

Belongs to the TNFAIP8 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    204
  • Mass (Da)
    23,243
  • Last updated
    2005-10-11 v1
  • Checksum
    2A5830746A4D8AE5
MDSDSGEQSEGEPGTAAGPHVFSSKNLALQAQKKILSKIASKTVANMLIDDTSSEIFDELYKVTEIHTHNKKEAHKIMKDAIKVAIKIGILYRNKQFSQEEVIIVEKLRKKLNQTAMTMVSFYEVEYTFDTNVLSKLLHECKDLVHELVQRHLTPRTHGRINHVFNHFADVEFLSTLYGPHGNCRPNLKRICEGINKLLDDKIL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK170374
EMBL· GenBank· DDBJ
BAE41754.1
EMBL· GenBank· DDBJ
mRNA
AK171174
EMBL· GenBank· DDBJ
BAE42293.1
EMBL· GenBank· DDBJ
mRNA
BC118003
EMBL· GenBank· DDBJ
AAI18004.1
EMBL· GenBank· DDBJ
mRNA
BC119769
EMBL· GenBank· DDBJ
AAI19770.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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