Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cerebellin-1

Gene

Cbln1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 (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 - Biological processi

Complete GO annotation...

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi1562813. Cbln1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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...)Sequence analysis1
Disulfide bondi34InterchainBy similarity
Disulfide bondi38InterchainBy similarity
Glycosylationi79N-linked (GlcNAc...)Sequence 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 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 (By similarity).By similarity

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
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
Regioni62 – 193Necessary for interaction with CBLN3, and homotrimerizationBy similarityAdd BLAST132

Sequence similaritiesi

Contains 1 C1q domain.PROSITE-ProRule annotation

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.
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.

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5KWRX-ray1.79A57-193[»]
SMRiP63182.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi270231. 1 interactor.
STRINGi10116.ENSRNOP00000000011.

Proteomic databases

PaxDbiP63182.
PRIDEiP63182.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi869.
RGDi1562813. Cbln1.

Phylogenomic databases

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

Miscellaneous databases

PROiP63182.

Gene expression databases

BgeeiENSRNOG00000000010.
GenevisibleiP63182. RN.

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_RAT
AccessioniPrimary (citable) accession number: P63182
Secondary accession number(s): P02682, P23436
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 6, 2007
Last modified: November 30, 2016
This is version 83 of the entry and version 2 of the sequence. [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
  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.