Cbln1
entrez
498922
canonical
uniprot
P63182
canonical
ensembl
ENSRNOG00000000010
resolver
ensembl
ENSRNOG00055020256
resolver
ensembl
ENSRNOG00060015864
resolver
ensembl
ENSRNOG00065014556
resolver
ensp
ENSRNOP00000000011
resolver
ensp
ENSRNOP00055028022
resolver
ensp
ENSRNOP00060021779
resolver
ensp
ENSRNOP00065018743
resolver
enst
ENSRNOT00000000011
resolver
enst
ENSRNOT00055034586
resolver
enst
ENSRNOT00060027164
resolver
enst
ENSRNOT00065024041
resolver
genesymbol
Cbln1
resolver
uniprot
P02682
resolver
uniprot
P23436
resolver
uniprot_entry
CBLN1_RAT
resolver
uniprot_sec
P02682
resolver
uniprot_sec
P23436
resolver
amino_acid_sequence
MLGVVELLLLGAAWLAGPARGQNETEPIVLEGKCLVVCDSNPTSDPTGTALGISVRSGSAKVAFSAIRSTNHEPSEMSNRTMIIYFDQVLVNIGNNFDSERSTFIAPRKGIYSFNFHVVKVYNRQTIQVSLMLNGWPVISAFAGDQDVTREAASNGVLIQMEKGDRAYLKLERGNLMGGWKYSTFSGFLVFPL
uniprot
proteins
function
FUNCTION: 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). Essential for long-term maintenance but not establishment of excitatory synapses (By similarity). Inhibits the formation and function of inhibitory GABAergic synapses in cerebellar Purkinje cells (By similarity). {ECO:0000250|UniProtKB:P23435, ECO:0000250|UniProtKB:Q9R171}.; FUNCTION: 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. {ECO:0000269|PubMed:10688962, ECO:0000269|PubMed:15702230}.
uniprot
proteins
mass_dalton
21083
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000250|UniProtKB:Q9R171}.; PTM: Sialoglycoprotein. {ECO:0000250|UniProtKB:Q9R171}.
uniprot
proteins
pubmed
10688962
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15702230
uniprot
proteins
pubmed
16593526
uniprot
proteins
pubmed
3399060
uniprot
proteins
pubmed
3420533
uniprot
proteins
sequence_length
193
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3399060}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9R171}.
uniprot
proteins