Cbln1
entrez
12404
canonical
uniprot
Q9R171
canonical
ensembl
ENSMUSG00000031654
resolver
ensp
ENSMUSP00000034076
resolver
ensp
ENSMUSP00000126575
resolver
enst
ENSMUST00000034076
resolver
enst
ENSMUST00000169693
resolver
genesymbol
Cbln1
resolver
uniprot
A2RSI1
resolver
uniprot
P28655
resolver
uniprot
Q7TNF5
resolver
uniprot
Q9QVT5
resolver
uniprot_entry
CBLN1_MOUSE
resolver
uniprot_entry
Q7TNF5_MOUSE
resolver
uniprot_sec
A2RSI1
resolver
uniprot_sec
P28655
resolver
uniprot_sec
Q9QVT5
resolver
amino_acid_sequence
MLGVVELLLLGTAWLAGPARGQNETEPIVLEGKCLVVCDSNPTSDPTGTALGISVRSGSAKVAFSAIRSTNHEPSEMSNRTMIIYFDQVLVNIGNNFDSERSTFIAPRKGIYSFNFHVVKVYNRQTIQVSLMLNGWPVISAFAGDQDVTREAASNGVLIQMEKGDRAYLKLERGNLMGGWKYSTFSGFLVFPL
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 (PubMed:16234806). Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post-synaptic components (PubMed:20395510). 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 (PubMed:21410790). NRXN1-CBLN1-GRID2 complex directly induces parallel fiber protrusions that encapsulate spines of Purkinje cells leading to accumulation of GRID2 and synaptic vesicles (PubMed:23141067). Required for CBLN3 export from the endoplasmic reticulum and secretion (PubMed:17030622, PubMed:17331201). 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 (PubMed:29691328). Inhibits the formation and function of inhibitory GABAergic synapses in cerebellar Purkinje cells (PubMed:24467251). {ECO:0000250|UniProtKB:P23435, ECO:0000269|PubMed:16234806, ECO:0000269|PubMed:17030622, ECO:0000269|PubMed:17331201, ECO:0000269|PubMed:20395510, ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:23141067, ECO:0000269|PubMed:24467251, ECO:0000269|PubMed:29691328}.; 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
21113
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="N->Q: No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with GRID2, NRXN1 and NRXN3. Loss of N-glycosylation; when associated with Q-79."; /evidence="ECO:0000269|PubMed:16234806, ECO:0000269|PubMed:29782851"; MUTAGEN 34; /note="C->A: Abolishes homohexamer formation from homotrimers; when associated with A-38."; /evidence="ECO:0000269|PubMed:16135095"; MUTAGEN 38; /note="C->A: Abolishes homohexamer formation from homotrimers; when associated with A-34."; /evidence="ECO:0000269|PubMed:16135095"; MUTAGEN 79; /note="N->Q: No effect on its ability to form homohexameric or heteromeric complexes with other CBLN family members. Increased interaction with GRID2, NRXN1 and NRXN3. Loss of N-glycosylation; when associated with Q-23."; /evidence="ECO:0000269|PubMed:16234806, ECO:0000269|PubMed:29782851"; MUTAGEN 110; /note="G->E: Retention in the endoplasmic reticulum/cis-Golgi; when associated with H-112."; /evidence="ECO:0000269|PubMed:17331201"; MUTAGEN 112; /note="Y->H: Retention in the endoplasmic reticulum/cis-Golgi; when associated with E-110."; /evidence="ECO:0000269|PubMed:17331201
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. In the cerebellum, cerebellin is much more abundant than [des-Ser1]-cerebellin. {ECO:0000269|PubMed:16135095}.; PTM: Sialoglycoprotein. {ECO:0000269|PubMed:29782851}.
uniprot
proteins
pubmed
10964938
uniprot
proteins
pubmed
12106288
uniprot
proteins
pubmed
16135095
uniprot
proteins
pubmed
16234806
uniprot
proteins
pubmed
16930405
uniprot
proteins
pubmed
17030622
uniprot
proteins
pubmed
17331201
uniprot
proteins
pubmed
19200061
uniprot
proteins
pubmed
20395510
uniprot
proteins
pubmed
20856818
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21410790
uniprot
proteins
pubmed
22220752
uniprot
proteins
pubmed
23141067
uniprot
proteins
pubmed
24467251
uniprot
proteins
pubmed
29691328
uniprot
proteins
pubmed
29782851
uniprot
proteins
pubmed
3199194
uniprot
proteins
pubmed
3420533
uniprot
proteins
pubmed
7877445
uniprot
proteins
pubmed
9838062
uniprot
proteins
sequence_length
193
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17331201, ECO:0000269|PubMed:29782851}. Postsynaptic cell membrane {ECO:0000269|PubMed:19200061}. Note=Interaction with CBLN3 may cause partial retention in the endoplasmic reticulum. {ECO:0000269|PubMed:17331201}.
uniprot
proteins