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Protein

Cerebellin-1

Gene

Cbln1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the formation and maintenance of parallel fiber and Purkinje cell synapses. When parallel fibers make contact with Purkinje spines, CBLN1 interaction with GRID2 triggers the recruitment of NRXN1 and secretory vesicles to the sites of contact. NRXN1-CBLN1-GRID2 signaling induces presynaptic morphological changes, which may further accumulate pre- and postsynaptic components to promote bidirectional maturation of parallel fiber - Purkinje cell functionally active synapses by a positive feedback mechanism. Required for CBLN3 export from the endoplasmic reticulum and secretion.6 Publications
The cerebellin peptide exerts neuromodulatory functions. Directly stimulates norepinephrine release via the adenylate cyclase/PKA-dependent signaling pathway; and indirectly enhances adrenocortical secretion in vivo, through a paracrine mechanism involving medullary catecholamine release (By similarity).By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

GO - Biological processi

  • cerebellar granule cell differentiation Source: BHF-UCL
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: BHF-UCL
  • positive regulation of synapse assembly Source: MGI
  • protein secretion Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Cerebellin-1
Alternative name(s):
Brain protein D3
Precerebellin
Cleaved into the following 2 chains:
Cerebellin
Short name:
CER
[des-Ser1]-cerebellin
Short name:
des-Ser1-cerebellin
Gene namesi
Name:Cbln1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:88281. Cbln1.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • extracellular region Source: UniProtKB-SubCell
  • postsynaptic membrane Source: UniProtKB-SubCell
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Secreted, Synapse

Pathology & Biotechi

Disruption phenotypei

Mice (reeler, weaver and staggerer) show defects in granule cell migration and parallel fiber formation, synaptogenesis, Purkinje cell dendritic maturation and establishment of adult cytoarchitecture show a correlation between the formation and number of parallel fiber-Purkinje cell synapses and cerebellin levels.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231N → Q: Loss of N-glycosylation; when associated with Q-79. 1 Publication
Mutagenesisi34 – 341C → A: Abolishes homohexamer formation from homotrimers; when associated with A-38. 1 Publication
Mutagenesisi38 – 381C → A: Abolishes homohexamer formation from homotrimers; when associated with A-34. 1 Publication
Mutagenesisi79 – 791N → Q: Loss of N-glycosylation; when associated with Q-23. 1 Publication
Mutagenesisi110 – 1101G → E: Retention in the endoplasmic reticulum/cis-Golgi; when associated with H-112. 1 Publication
Mutagenesisi112 – 1121Y → H: Retention in the endoplasmic reticulum/cis-Golgi; when associated with E-110. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 193172Cerebellin-1PRO_0000274211Add
BLAST
Peptidei57 – 7216CerebellinPRO_0000003549Add
BLAST
Peptidei58 – 7215[des-Ser1]-cerebellinPRO_0000274212Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi23 – 231N-linked (GlcNAc...)1 Publication
Disulfide bondi34 – 34Interchain
Disulfide bondi38 – 38Interchain
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication

Post-translational modificationi

The proteolytic processing to yield cerebellin seems to occur either prior to the secretion by presynaptic neurons and subsequent oligomerization or in some other location after release of the mature protein. In the cerebellum, cerebellin is much more abundant than [des-Ser1]-cerebellin.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9R171.
PaxDbiQ9R171.
PRIDEiQ9R171.

PTM databases

iPTMnetiQ9R171.
PhosphoSiteiQ9R171.

Expressioni

Tissue specificityi

Expressed and secreted by presynaptic neurons, such as cerebellar granule cells. Following secretion, the protein binds to GRID2 on the postsynaptic Purkinje cell membranes. Expressed at the highest level in the cerebellar cortex. High levels are also seen in the olfactory bulb, posterior part of the cerebral cortex, certain thalamic nuclei, and deep cerebellar nuclei. Low to moderate levels are detected in some hypothalamic and brainstem nuclei. In the thalamus, expressed in parafascicular nucleus neurons and other regions (at protein level).6 Publications

Developmental stagei

In the developing brain, expressed as early as embryonic day 10-13, and transiently up-regulated during the late embryonic and neonatal periods. Cerebellin and [des-Ser1]-cerebellin are expressed as easly as postnatal day 3-4. The levels of both peptides rise rapidly to a maximum at approximately day 25-30 after birth, whereafter they fall to stable adult values.2 Publications

Gene expression databases

BgeeiENSMUSG00000031654.
CleanExiMM_CBLN1.
ExpressionAtlasiQ9R171. baseline and differential.
GenevisibleiQ9R171. MM.

Interactioni

Subunit structurei

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. May form oligomers with CBLN2, CBLN3 AND CBLN4 prior to secretion. Once secreted, does not interact with other CBLN family members. Interacts with GRID1 and GRID2. GRID2-binding is calcium-independent. Interacts with NRXN1 and NRXN2 long (alpha) and short (beta) isoforms produced by alternative promoter usage. Competes with NLGN1 for NRXN1-binding. Weakly interacts with NRXN3 short isoform and not at all with NRXN3 long isoform.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Grid2Q616258EBI-2794140,EBI-2794106
Nrxn1P0DI974EBI-2794140,EBI-2794440

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

IntActiQ9R171. 3 interactions.
STRINGi10090.ENSMUSP00000034076.

Structurei

3D structure databases

ProteinModelPortaliQ9R171.
SMRiQ9R171. Positions 61-191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 193137C1qPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 193132Necessary for interaction with CBLN3, and homotrimerizationAdd
BLAST

Sequence similaritiesi

Contains 1 C1q domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFXA. Eukaryota.
ENOG410Y16R. LUCA.
GeneTreeiENSGT00760000119052.
HOGENOMiHOG000085657.
HOVERGENiHBG108329.
InParanoidiQ9R171.
OMAiMVIYFDR.
OrthoDBiEOG091G0XK2.
PhylomeDBiQ9R171.
TreeFamiTF329591.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
[Graphical view]
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGVVELLLL GTAWLAGPAR GQNETEPIVL EGKCLVVCDS NPTSDPTGTA
60 70 80 90 100
LGISVRSGSA KVAFSAIRST NHEPSEMSNR TMIIYFDQVL VNIGNNFDSE
110 120 130 140 150
RSTFIAPRKG IYSFNFHVVK VYNRQTIQVS LMLNGWPVIS AFAGDQDVTR
160 170 180 190
EAASNGVLIQ MEKGDRAYLK LERGNLMGGW KYSTFSGFLV FPL
Length:193
Mass (Da):21,113
Last modified:May 1, 2000 - v1
Checksum:iA23C796C7D11BE5F
GO

Sequence cautioni

The sequence CAA43688 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51V → L no nucleotide entry (PubMed:7877445).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164680 Genomic DNA. Translation: AAD47280.1.
X61448 mRNA. Translation: CAA43688.1. Sequence problems.
CCDSiCCDS22506.1.
PIRiS16862.
RefSeqiNP_062600.2. NM_019626.3.
UniGeneiMm.4880.

Genome annotation databases

EnsembliENSMUST00000034076; ENSMUSP00000034076; ENSMUSG00000031654.
ENSMUST00000169693; ENSMUSP00000126575; ENSMUSG00000031654.
GeneIDi12404.
KEGGimmu:12404.
UCSCiuc009mqr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164680 Genomic DNA. Translation: AAD47280.1.
X61448 mRNA. Translation: CAA43688.1. Sequence problems.
CCDSiCCDS22506.1.
PIRiS16862.
RefSeqiNP_062600.2. NM_019626.3.
UniGeneiMm.4880.

3D structure databases

ProteinModelPortaliQ9R171.
SMRiQ9R171. Positions 61-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R171. 3 interactions.
STRINGi10090.ENSMUSP00000034076.

PTM databases

iPTMnetiQ9R171.
PhosphoSiteiQ9R171.

Proteomic databases

MaxQBiQ9R171.
PaxDbiQ9R171.
PRIDEiQ9R171.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034076; ENSMUSP00000034076; ENSMUSG00000031654.
ENSMUST00000169693; ENSMUSP00000126575; ENSMUSG00000031654.
GeneIDi12404.
KEGGimmu:12404.
UCSCiuc009mqr.1. mouse.

Organism-specific databases

CTDi869.
MGIiMGI:88281. Cbln1.

Phylogenomic databases

eggNOGiENOG410IFXA. Eukaryota.
ENOG410Y16R. LUCA.
GeneTreeiENSGT00760000119052.
HOGENOMiHOG000085657.
HOVERGENiHBG108329.
InParanoidiQ9R171.
OMAiMVIYFDR.
OrthoDBiEOG091G0XK2.
PhylomeDBiQ9R171.
TreeFamiTF329591.

Miscellaneous databases

PROiQ9R171.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031654.
CleanExiMM_CBLN1.
ExpressionAtlasiQ9R171. baseline and differential.
GenevisibleiQ9R171. MM.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
[Graphical view]
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBLN1_MOUSE
AccessioniPrimary (citable) accession number: Q9R171
Secondary accession number(s): P28655, Q9QVT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.