CBLN1
entrez
869
canonical
uniprot
P23435
canonical
ensembl
ENSG00000102924
resolver
ensp
ENSP00000219197
resolver
enst
ENST00000219197
resolver
genesymbol
CBLN1
resolver
hgnc
HGNC:1543
resolver
uniprot
B2RAN9
resolver
uniprot
P02682
resolver
uniprot
Q52M09
resolver
uniprot_entry
CBLN1_HUMAN
resolver
uniprot_sec
B2RAN9
resolver
uniprot_sec
P02682
resolver
uniprot_sec
Q52M09
resolver
amino_acid_sequence
MLGVLELLLLGAAWLAGPARGQNETEPIVLEGKCLVVCDSNPTSDPTGTALGISVRSGSAKVAFSAIRSTNHEPSEMSNRTMIIYFDQVLVNIGNNFDSERSTFIAPRKGIYSFNFHVVKVYNRQTIQVSLMLNGWPVISAFAGDQDVTREAASNGVLIQMEKGDRAYLKLERGNLMGGWKYSTFSGFLVFPL
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 (PubMed:27418511). 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:Q9R171, ECO:0000269|PubMed:27418511}.; FUNCTION: 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). {ECO:0000250|UniProtKB:P63182}.
uniprot
proteins
mass_dalton
21097
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="C->S: Abolishes hexamer formation; when associated with S-38. Abolishes interaction with NRXN1; when associated with S-38. Abolishes GRID2 interaction; when associated with S-38."; /evidence="ECO:0000269|PubMed:27418511"; MUTAGEN 38; /note="C->S: Abolishes hexamer formation; when associated with S-34. Abolishes interaction with NRXN1 isoform 3B; when associated with S-34. Abolishes GRID2 interaction.; when associated with S-34."; /evidence="ECO:0000269|PubMed:27418511"; MUTAGEN 122; /note="Y->A: Abolishes GRID2 interaction.; when associated with A-124 and A-147."; /evidence="ECO:0000269|PubMed:27418511"; MUTAGEN 124; /note="R->A: Abolishes GRID2 interaction.; when associated with A-122 and A-147."; /evidence="ECO:0000269|PubMed:27418511"; MUTAGEN 147; /note="D->A: Abolishes GRID2 interaction.; when associated with A-122 and A-124."; /evidence="ECO:0000269|PubMed:27418511
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
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1704129
uniprot
proteins
pubmed
27418511
uniprot
proteins
pubmed
2760624
uniprot
proteins
sequence_length
193
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9R171}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9R171}.
uniprot
proteins