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Protein

Cerebellin-1

Gene

Cbln1

Organism
Rattus norvegicus (Rat)
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 matching and maintenance of pre- and post-synaptic elements at parallel fiber-Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses. Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post-synaptic components. On the one hand induces accumulation of synaptic vesicles in the pre-synaptic part by binding with NRXN1 and in other hand induces clustering of GRID2 and its associated proteins at the post-synaptic site through association of GRID2. NRXN1-CBLN1-GRID2 complex directly induces parallel fiber protrusions that encapsulate spines of Purkinje cells leading to accumulation of GRID2 and synaptic vesicles. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). NRXN1-CBLN1-GRID2 complex mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (By similarity).By similarity
The cerebellin 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. A conversion to [des-Ser1]-cerebellin by endopeptidases seems to be required for its autocrine-paracrine regulatory functions.2 Publications

GO - Molecular functioni

GO - Biological processi

Names & Taxonomyi

Protein namesi
Recommended name:
Cerebellin-1
Alternative name(s):
Precerebellin
Cleaved into the following 2 chains:
Cerebellin
Short name:
CER
Alternative name(s):
des-Ser(1)-cerebellin
Short name:
[des-Ser1]CER
Short name:
des-CER
Short name:
des-Ser1CER
Gene namesi
Name:Cbln1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi1562813. Cbln1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000027421522 – 193Cerebellin-1Add BLAST172
PeptideiPRO_000004358857 – 72CerebellinAdd BLAST16
PeptideiPRO_000027421658 – 72[des-Ser1]-cerebellinAdd BLAST15

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi23N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi34InterchainBy similarity
Disulfide bondi38InterchainBy similarity
Glycosylationi79N-linked (GlcNAc...) asparagineSequence analysis1

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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP63182.
PRIDEiP63182.

Expressioni

Tissue specificityi

Localized in the Purkinje cells. Cerebellin is expressed in adrenal gland /adrenal cortex (at protein level). In the cerebellum, [des-Ser1]-cerebellin is more abundant than cerebellin. At lower levels also found in heart, kidney stomach and gastrointestinal tract.3 Publications

Gene expression databases

BgeeiENSRNOG00000000010.
GenevisibleiP63182. RN.

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. 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 (By similarity). Interacts (via C1q domain) with GRID2; GRID2-binding is calcium-independent; CBLN1 hexamers anchor GRID2 N-terminal domain dimers to monomeric NRXN1 isoform beta; promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi270231. 1 interactor.
STRINGi10116.ENSRNOP00000000011.

Structurei

Secondary structure

1193
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi58 – 60Combined sources3
Beta strandi63 – 67Combined sources5
Helixi76 – 81Combined sources6
Beta strandi87 – 93Combined sources7
Turni99 – 102Combined sources4
Beta strandi103 – 105Combined sources3
Beta strandi107 – 120Combined sources14
Beta strandi127 – 133Combined sources7
Beta strandi136 – 143Combined sources8
Beta strandi147 – 149Combined sources3
Beta strandi151 – 161Combined sources11
Beta strandi166 – 174Combined sources9
Beta strandi184 – 192Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5H48X-ray2.20A22-193[»]
5H49X-ray2.80A/B/C22-193[»]
5KWRX-ray1.79A57-193[»]
SMRiP63182.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini57 – 193C1qPROSITE-ProRule annotationAdd BLAST137

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni34 – 38Essential for interaction with NRXN1 and linker of two C1q trimers into disulfide-linked hexamersBy similarity5
Regioni62 – 193Necessary for interaction with CBLN3, and homotrimerizationBy similarityAdd BLAST132
Regioni122 – 147Essentiel for interaction with GRID2By similarityAdd BLAST26

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFXA. Eukaryota.
ENOG410Y16R. LUCA.
GeneTreeiENSGT00760000119052.
HOGENOMiHOG000085657.
HOVERGENiHBG108329.
InParanoidiP63182.
OMAiMVIYFDR.
OrthoDBiEOG091G0XK2.
PhylomeDBiP63182.
TreeFamiTF329591.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiView protein in InterPro
IPR001073. C1q_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
PfamiView protein in Pfam
PF00386. C1q. 1 hit.
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiView protein in SMART
SM00110. C1Q. 1 hit.
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiView protein in PROSITE
PS50871. C1Q. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P63182-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGVVELLLL GAAWLAGPAR 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):21,083
Last modified:February 6, 2007 - v2
Checksum:i5E451C6C681E0E50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03113474 Genomic DNA. No translation available.
PIRiA03135. CQRT.
RefSeqiNP_001102597.1. NM_001109127.1.
UniGeneiRn.24402.

Genome annotation databases

EnsembliENSRNOT00000000011; ENSRNOP00000000011; ENSRNOG00000000010.
GeneIDi498922.
KEGGirno:498922.

Similar proteinsi

Entry informationi

Entry nameiCBLN1_RAT
AccessioniPrimary (citable) accession number: P63182
Secondary accession number(s): P02682, P23436
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 6, 2007
Last modified: November 22, 2017
This is version 90 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Initially the cerebellin peptide was thought to present the biological active entity.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references