CBLN1_PIG
ID CBLN1_PIG Reviewed; 16 AA.
AC P63181; P02682; P23436;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Cerebellin-1;
DE AltName: Full=Precerebellin;
DE Contains:
DE RecName: Full=Cerebellin;
DE Short=CER;
DE Contains:
DE RecName: Full=[des-Ser1]-cerebellin;
DE Flags: Fragment;
GN Name=Cbln1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE (CEREBELLIN AND [DES-SER1]-CEREBELLIN).
RC TISSUE=Brain;
RX PubMed=2760624; DOI=10.1111/j.1471-4159.1989.tb11787.x;
RA Yiangou Y., Burnet P., Nikou G., Chrysanthou B.J., Bloom S.R.;
RT "Purification and characterisation of cerebellins from human and porcine
RT cerebellum.";
RL J. Neurochem. 53:886-889(1989).
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.
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). Interacts with OTOL1 (By similarity).
CC {ECO:0000250|UniProtKB:P23435, ECO:0000250|UniProtKB:Q9R171}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9R171}.
CC Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9R171}.
CC -!- TISSUE SPECIFICITY: Localized in the Purkinje cells. Cerebellin and
CC [des-Ser1]-cerebellin are equally abundant.
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:Q9R171}.
CC -!- PTM: Sialoglycoprotein. {ECO:0000250|UniProtKB:Q9R171}.
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DR PIR; PL0124; PL0124.
DR AlphaFoldDB; P63181; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
DR GO; GO:0099558; P:maintenance of synapse structure; ISS:UniProtKB.
DR GO; GO:1905703; P:negative regulation of inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; ISS:UniProtKB.
DR InterPro; IPR001073; C1q_dom.
DR PROSITE; PS50871; C1Q; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Membrane; Postsynaptic cell membrane; Reference proteome; Secreted;
KW Sialic acid; Synapse.
FT CHAIN <1..>16
FT /note="Cerebellin-1"
FT /id="PRO_0000274213"
FT PEPTIDE 1..16
FT /note="Cerebellin"
FT /id="PRO_0000043587"
FT PEPTIDE 2..16
FT /note="[des-Ser1]-cerebellin"
FT /id="PRO_0000274214"
FT DOMAIN 1..>16
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT NON_TER 1
FT NON_TER 16
SQ SEQUENCE 16 AA; 1633 MW; 3EFA16635343D518 CRC64;
SGSAKVAFSA IRSTNH
