Q8BME9 · CBLN4_MOUSE

  • Protein
    Cerebellin-4
  • Gene
    Cbln4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Acts as a synaptic organizer in specific subsets of neurons in the brain (PubMed:29691328).
Essential for the formation and maintenance of inhibitory GABAergic synapses (PubMed:25534236).
Promotes the development of dendrite-targeting inhibitory GABAergic synapses made by somatostatin-positive interneurons (PubMed:30679375).
May contribute to the function of ventral medial habenula region of the brain implicated in the regulation of anxiety-related behaviors (PubMed:30287486).
May play a role in CBLN3 export from the endoplasmic reticulum and secretion (PubMed:17030622).

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 Componentextracellular region
Cellular Componentextracellular space
Cellular ComponentGABA-ergic synapse
Cellular Componentglutamatergic synapse
Cellular Componentsynapse
Cellular Componentsynaptic cleft
Biological Processinhibitory synapse assembly
Biological Processprotein secretion
Biological Processtrans-synaptic signaling, modulating synaptic transmission

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Cerebellin-4
  • Alternative names
    • Cerebellin-like glycoprotein 1

Gene names

    • Name
      Cbln4
    • Synonyms
      Cblnl1

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8BME9
  • Secondary accessions
    • Q505H5
    • Q8BMF0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Mutant animals are fertile, have normal life spans and have no overt anatomical abnormalities (PubMed:22220752).
They have a normal corpus callosum, hippocampal commisure and pontine nucleus and no other gross neuroanatomical abnormalities (PubMed:22220752).
Mice exhibit increased anxiety-related behavior (PubMed:30287486).
Triple CBLN1, CBLN2 and CBLN4 knockout mice exhibit impairments in sensory processing and sensorimotor gating, in addition to severe motor deficits, seizures and reduced synapse density in the hippocampus of aging mice (PubMed:29691328).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis26No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with NRXN1, NRXN3 and DCC. Shows interaction with NEO1, GRID1 and GRID2. Total loss of N-glycosylation; when associated with Q-85.
Mutagenesis85No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with NRXN1, NRXN3 and DCC. Shows interaction with NEO1, GRID1 and GRID2. Total loss of N-glycosylation; when associated with Q-26.

Variants

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

The viewer provides 8 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
Signal1-24
ChainPRO_000000355725-198Cerebellin-4
Glycosylation26N-linked (GlcNAc...) asparagine
Disulfide bond37Interchain
Disulfide bond41Interchain
Glycosylation85N-linked (GlcNAc...) asparagine

Post-translational modification

Sialoglycoprotein.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in brain with high levels in particular thalamic nuclei. In the thalamus, predominantly expressed in neurons within the parafascicular nucleus. Found in the hippocampus, mostly in the dendrites and somata of pyramidal neurons (at protein level). Very low or no expression in most other brain regions. Highly expressed in the ventral medial habenula.

Developmental stage

In the developing brain, expressed as early as 10-13 dpc. Expression level peaks at 18 dpc and gradually decreases afterwards. Expressed in developing somatostatin-positive basket cells.

Gene expression databases

Interaction

Subunit

Homohexamer; disulfide-linked homotrimers. The trimers are assembled via the globular C1q domains. The trimers associate via N-terminal cysteine residues to form disulfide-linked hexamers (By similarity).
May form oligomers with CBLN1, CBLN2 and CBLN3 prior to secretion (PubMed:17030622, PubMed:29782851).
Once secreted, does not interact with other CBLN family members (PubMed:17030622).
Strongly interacts with DCC in a NTN1-displaceable fashion (PubMed:22220752, PubMed:29782851).
Weakly binds to NRXN1 and NRXN2 long and short isoforms produced by alternative promoter usage (PubMed:22220752, PubMed:29782851).
Interaction with NRXN3 short isoform is hardly detectable; no interaction at all with NRXN3 long isoform (PubMed:22220752, PubMed:29782851).
Does not interact with NEO1, GRID1 and GRID2 (PubMed:22220752, PubMed:29782851).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain63-198C1q

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    198
  • Mass (Da)
    21,609
  • Last updated
    2003-03-01 v1
  • Checksum
    5A35ACC1354C70D6
MGSARRALSVVPAVLLILVLPVWAQNDTEPIVLEGKCLVVCDSNPATDSKGSSSSPLGISVRAANSKVAFSAVRSTNHEPSEMSNKTRIIYFDQILVNVGNFFTLESVFVAPRKGIYSFSFHVIKVYQSQTIQVNLMLNGKPVISAFAGDKDVTREAATNGVLLYLDKEDKVYLKLEKGNLLGGWQYSTFSGFLVFPL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict112in Ref. 1; BAC27855

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY134663
EMBL· GenBank· DDBJ
AAN08614.1
EMBL· GenBank· DDBJ
mRNA
AK032406
EMBL· GenBank· DDBJ
BAC27855.1
EMBL· GenBank· DDBJ
mRNA
AK032621
EMBL· GenBank· DDBJ
BAC27954.1
EMBL· GenBank· DDBJ
mRNA
CH466551
EMBL· GenBank· DDBJ
EDL06594.1
EMBL· GenBank· DDBJ
Genomic DNA
BC094540
EMBL· GenBank· DDBJ
AAH94540.1
EMBL· GenBank· DDBJ
mRNA
BC132025
EMBL· GenBank· DDBJ
AAI32026.1
EMBL· GenBank· DDBJ
mRNA
BC132027
EMBL· GenBank· DDBJ
AAI32028.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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.
FeedbackHelp