CBLN1_BOVIN
ID CBLN1_BOVIN Reviewed; 193 AA.
AC P86437;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Cerebellin-1 {ECO:0000250|UniProtKB:Q9R171};
DE AltName: Full=Precerebellin {ECO:0000250|UniProtKB:Q9R171};
DE Contains:
DE RecName: Full=Cerebellin {ECO:0000303|Ref.2};
DE Short=CER {ECO:0000250|UniProtKB:Q9R171};
DE Contains:
DE RecName: Full=[des-Ser1]-cerebellin;
DE Flags: Precursor;
GN Name=CBLN1 {ECO:0000250|UniProtKB:Q9R171};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000269|PubMed:19390049};
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Colgrave M.;
RT "Neuropeptidomics of the bovine hypothalamus.";
RL Submitted (JAN-2010) to UniProtKB.
CC -!- FUNCTION: Required for synapse integrity and synaptic plasticity.
CC During cerebellar synapse formation, essential for the matching and
CC maintenance of pre- and post-synaptic elements at parallel fiber-
CC Purkinje cell synapses, the establishment of the proper pattern of
CC climbing fiber-Purkinje cell innervation, and induction of long-term
CC depression at parallel fiber-Purkinje cell synapses. Plays a role as a
CC synaptic organizer that acts bidirectionally on both pre- and post-
CC synaptic components. On the one hand induces accumulation of synaptic
CC vesicles in the pre-synaptic part by binding with NRXN1 and in other
CC hand induces clustering of GRID2 and its associated proteins at the
CC post-synaptic site through association of GRID2. NRXN1-CBLN1-GRID2
CC complex directly induces parallel fiber protrusions that encapsulate
CC spines of Purkinje cells leading to accumulation of GRID2 and synaptic
CC vesicles. Required for CBLN3 export from the endoplasmic reticulum and
CC secretion (By similarity). NRXN1-CBLN1-GRID2 complex mediates the D-
CC Serine-dependent long term depression signals and AMPA receptor
CC endocytosis (By similarity). Essential for long-term maintenance but
CC not establishment of excitatory synapses (By similarity). Inhibits the
CC formation and function of inhibitory GABAergic synapses in cerebellar
CC Purkinje cells (By similarity). {ECO:0000250|UniProtKB:P23435,
CC ECO:0000250|UniProtKB:Q9R171}.
CC -!- FUNCTION: The cerebellin peptide exerts neuromodulatory functions.
CC Directly stimulates norepinephrine release via the adenylate
CC cyclase/PKA-dependent signaling pathway; and indirectly enhances
CC adrenocortical secretion in vivo, through a paracrine mechanism
CC involving medullary catecholamine release (By similarity).
CC {ECO:0000250|UniProtKB:P63182}.
CC -!- SUBUNIT: Homohexamer; disulfide-linked homotrimers. The trimers are
CC assembled via the globular C1q domains. The trimers associate via N-
CC terminal cysteine residues to form disulfide-linked hexamers. May form
CC oligomers with CBLN2, CBLN3 AND CBLN4 prior to secretion. Once
CC secreted, does not interact with other CBLN family members. Interacts
CC with GRID1. Interacts with NRXN1 and NRXN2 long (alpha) and short
CC (beta) isoforms produced by alternative promoter usage. Competes with
CC NLGN1 for NRXN1-binding. Weakly interacts with NRXN3 short isoform and
CC not at all with NRXN3 long isoform (By similarity). Interacts (via C1q
CC domain) with GRID2; GRID2-binding is calcium-independent; CBLN1
CC hexamers anchor GRID2 N-terminal domain dimers to monomeric NRXN1
CC isoform beta; promotes synaptogenesis and mediates the D-Serine-
CC dependent long term depression signals and AMPA receptor endocytosis
CC (By similarity). {ECO:0000250|UniProtKB:P23435,
CC ECO:0000250|UniProtKB:Q9R171}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9R171}.
CC Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9R171}.
CC -!- PTM: The proteolytic processing to yield cerebellin seems to occur
CC either prior to the secretion by presynaptic neurons and subsequent
CC oligomerization or in some other location after release of the mature
CC protein. {ECO:0000250|UniProtKB:P23435}.
CC -!- PTM: Sialoglycoprotein. {ECO:0000250|UniProtKB:Q9R171}.
CC -!- MASS SPECTROMETRY: [Cerebellin]: Mass=1631.85; Mass_error=0.16;
CC Method=Electrospray; Evidence={ECO:0000269|Ref.2};
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DR EMBL; AAFC03072883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001181981.1; NM_001195052.1.
DR AlphaFoldDB; P86437; -.
DR SMR; P86437; -.
DR STRING; 9913.ENSBTAP00000020212; -.
DR PaxDb; P86437; -.
DR Ensembl; ENSBTAT00000020212; ENSBTAP00000020212; ENSBTAG00000015194.
DR GeneID; 618604; -.
DR KEGG; bta:618604; -.
DR CTD; 869; -.
DR VEuPathDB; HostDB:ENSBTAG00000015194; -.
DR VGNC; VGNC:26811; CBLN1.
DR eggNOG; ENOG502QVN9; Eukaryota.
DR GeneTree; ENSGT00940000159811; -.
DR HOGENOM; CLU_001074_8_2_1; -.
DR InParanoid; P86437; -.
DR OMA; NRTMLIY; -.
DR OrthoDB; 1398761at2759; -.
DR TreeFam; TF329591; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000015194; Expressed in prefrontal cortex and 26 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043083; C:synaptic cleft; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0099558; P:maintenance of synapse structure; ISS:UniProtKB.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:1905703; P:negative regulation of inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; IEA:Ensembl.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IEA:Ensembl.
DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
DR Gene3D; 2.60.120.40; -; 1.
DR InterPro; IPR001073; C1q_dom.
DR InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR Pfam; PF00386; C1q; 1.
DR PRINTS; PR00007; COMPLEMNTC1Q.
DR SMART; SM00110; C1Q; 1.
DR SUPFAM; SSF49842; SSF49842; 1.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Secreted; Sialic acid;
KW Signal; Synapse.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..193
FT /note="Cerebellin-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000391791"
FT PEPTIDE 57..72
FT /note="Cerebellin"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000391792"
FT PEPTIDE 58..72
FT /note="[des-Ser1]-cerebellin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000391793"
FT DOMAIN 57..193
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 34..38
FT /note="Essential for interaction with NRXN1 and linker of
FT two C1q trimers into disulfide-linked hexamers"
FT /evidence="ECO:0000250|UniProtKB:P23435"
FT REGION 62..193
FT /note="Necessary for interaction with CBLN3, and
FT homotrimerization"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
FT REGION 122..147
FT /note="Essential for interaction with GRID2"
FT /evidence="ECO:0000250|UniProtKB:P23435"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
FT DISULFID 38
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
SQ SEQUENCE 193 AA; 21083 MW; 5E451C6C681E0E50 CRC64;
MLGVVELLLL GAAWLAGPAR GQNETEPIVL EGKCLVVCDS NPTSDPTGTA LGISVRSGSA
KVAFSAIRST NHEPSEMSNR TMIIYFDQVL VNIGNNFDSE RSTFIAPRKG IYSFNFHVVK
VYNRQTIQVS LMLNGWPVIS AFAGDQDVTR EAASNGVLIQ MEKGDRAYLK LERGNLMGGW
KYSTFSGFLV FPL
