CBLN1_MOUSE
ID CBLN1_MOUSE Reviewed; 193 AA.
AC Q9R171; P28655; Q9QVT5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cerebellin-1;
DE AltName: Full=Brain protein D3;
DE AltName: Full=Precerebellin;
DE Contains:
DE RecName: Full=Cerebellin;
DE Short=CER;
DE Contains:
DE RecName: Full=[des-Ser1]-cerebellin;
DE Short=des-Ser1-cerebellin;
DE Flags: Precursor;
GN Name=Cbln1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=7877445; DOI=10.1016/0169-328x(94)90196-1;
RA Kavety B., Jenkins N.A., Fletcher C.F., Copeland N.G., Morgan J.I.;
RT "Genomic structure and mapping of precerebellin and a precerebellin-related
RT gene.";
RL Brain Res. Mol. Brain Res. 27:152-156(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129; TISSUE=Cerebellum;
RX PubMed=9838062; DOI=10.1016/s0169-328x(98)00264-2;
RA Kavety B., Morgan J.I.;
RT "Characterization of transcript processing of the gene encoding
RT precerebellin-1.";
RL Brain Res. Mol. Brain Res. 63:98-104(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-193.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA Kato K.;
RT "A collection of cDNA clones with specific expression patterns in mouse
RT brain.";
RL Eur. J. Neurosci. 2:704-711(1990).
RN [4]
RP PROTEIN SEQUENCE OF 57-72, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE
RP (CEREBELLIN AND [DES-SER1]-CEREBELLIN), AND DISRUPTION PHENOTYPE.
RC STRAIN=BALB/cJ; TISSUE=Cerebellum;
RX PubMed=3199194; DOI=10.1523/jneurosci.08-12-04603.1988;
RA Slemmon J.R., Goldowitz D., Blacher R., Morgan J.I.;
RT "Evidence for the transneuronal regulation of cerebellin biosynthesis in
RT developing Purkinje cells.";
RL J. Neurosci. 8:4603-4611(1988).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=3420533; DOI=10.1002/syn.890020203;
RA Morgan J.I., Slemmon J.R., Danho W., Hempstead J., Berrebi A.S.,
RA Mugnaini E.;
RT "Cerebellin and related postsynaptic peptides in the brain of normal and
RT neurodevelopmentally mutant vertebrates.";
RL Synapse 2:117-124(1988).
RN [6]
RP INTERACTION WITH CBLN3.
RX PubMed=10964938; DOI=10.1523/jneurosci.20-17-06333.2000;
RA Pang Z., Zuo J., Morgan J.I.;
RT "Cbln3, a novel member of the precerebellin family that binds specifically
RT to Cbln1.";
RL J. Neurosci. 20:6333-6339(2000).
RN [7]
RP SUBUNIT, MUTAGENESIS OF CYS-34 AND CYS-38, DISULFIDE BOND, AND PROTEOLYTIC
RP PROCESSING.
RX PubMed=16135095; DOI=10.1111/j.1471-4159.2005.03385.x;
RA Bao D., Pang Z., Morgan J.I.;
RT "The structure and proteolytic processing of Cbln1 complexes.";
RL J. Neurochem. 95:618-629(2005).
RN [8]
RP FUNCTION, MUTAGENESIS OF ASN-23 AND ASN-79, AND GLYCOSYLATION AT ASN-23 AND
RP ASN-79.
RX PubMed=16234806; DOI=10.1038/nn1576;
RA Hirai H., Pang Z., Bao D., Miyazaki T., Li L., Miura E., Parris J.,
RA Rong Y., Watanabe M., Yuzaki M., Morgan J.I.;
RT "Cbln1 is essential for synaptic integrity and plasticity in the
RT cerebellum.";
RL Nat. Neurosci. 8:1534-1541(2005).
RN [9]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16930405; DOI=10.1111/j.1460-9568.2006.04950.x;
RA Miura E., Iijima T., Yuzaki M., Watanabe M.;
RT "Distinct expression of Cbln family mRNAs in developing and adult mouse
RT brains.";
RL Eur. J. Neurosci. 24:750-760(2006).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, SELF-ASSOCIATION, INTERACTION WITH CBLN2;
RP CBLN3 AND CBLN4, AND REGION.
RX PubMed=17030622; DOI=10.1128/mcb.01161-06;
RA Bao D., Pang Z., Morgan M.A., Parris J., Rong Y., Li L., Morgan J.I.;
RT "Cbln1 is essential for interaction-dependent secretion of cbln3.";
RL Mol. Cell. Biol. 26:9327-9337(2006).
RN [11]
RP FUNCTION, OLIGOMERIZATION WITH CBLN1; CBLN2; CBLN3 AND CBLN4, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLY-110 AND TYR-112.
RX PubMed=17331201; DOI=10.1111/j.1460-9568.2007.05361.x;
RA Iijima T., Miura E., Matsuda K., Kamekawa Y., Watanabe M., Yuzaki M.;
RT "Characterization of a transneuronal cytokine family Cbln - regulation of
RT secretion by heteromeric assembly.";
RL Eur. J. Neurosci. 25:1049-1057(2007).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=19200061; DOI=10.1111/j.1460-9568.2009.06639.x;
RA Matsuda K., Kondo T., Iijima T., Matsuda S., Watanabe M., Yuzaki M.;
RT "Cbln1 binds to specific postsynaptic sites at parallel fiber-Purkinje cell
RT synapses in the cerebellum.";
RL Eur. J. Neurosci. 29:707-717(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP INTERACTION WITH OTOL1.
RX PubMed=20856818; DOI=10.1371/journal.pone.0012765;
RA Deans M.R., Peterson J.M., Wong G.W.;
RT "Mammalian Otolin: a multimeric glycoprotein specific to the inner ear that
RT interacts with otoconial matrix protein Otoconin-90 and Cerebellin-1.";
RL PLoS ONE 5:E12765-E12765(2010).
RN [15]
RP FUNCTION, AND INTERACTION WITH GRID2.
RX PubMed=20395510; DOI=10.1126/science.1185152;
RA Matsuda K., Miura E., Miyazaki T., Kakegawa W., Emi K., Narumi S.,
RA Fukazawa Y., Ito-Ishida A., Kondo T., Shigemoto R., Watanabe M., Yuzaki M.;
RT "Cbln1 is a ligand for an orphan glutamate receptor delta2, a bidirectional
RT synapse organizer.";
RL Science 328:363-368(2010).
RN [16]
RP FUNCTION, AND INTERACTION WITH GRID2; NRXN1; NRXN2 AND NRXN3.
RX PubMed=21410790; DOI=10.1111/j.1460-9568.2011.07638.x;
RA Matsuda K., Yuzaki M.;
RT "Cbln family proteins promote synapse formation by regulating distinct
RT neurexin signaling pathways in various brain regions.";
RL Eur. J. Neurosci. 33:1447-1461(2011).
RN [17]
RP INTERACTION WITH GRID1; GRID2; NRXN1; NRXN2 AND NRXN3, AND TISSUE
RP SPECIFICITY.
RX PubMed=22220752; DOI=10.1111/j.1471-4159.2012.07648.x;
RA Wei P., Pattarini R., Rong Y., Guo H., Bansal P.K., Kusnoor S.V.,
RA Deutch A.Y., Parris J., Morgan J.I.;
RT "The Cbln family of proteins interact with multiple signaling pathways.";
RL J. Neurochem. 121:717-729(2012).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23141067; DOI=10.1016/j.neuron.2012.07.027;
RA Ito-Ishida A., Miyazaki T., Miura E., Matsuda K., Watanabe M., Yuzaki M.,
RA Okabe S.;
RT "Presynaptically released Cbln1 induces dynamic axonal structural changes
RT by interacting with GluD2 during cerebellar synapse formation.";
RL Neuron 76:549-564(2012).
RN [19]
RP FUNCTION.
RX PubMed=24467251; DOI=10.1111/ejn.12487;
RA Ito-Ishida A., Kakegawa W., Kohda K., Miura E., Okabe S., Yuzaki M.;
RT "Cbln1 downregulates the formation and function of inhibitory synapses in
RT mouse cerebellar Purkinje cells.";
RL Eur. J. Neurosci. 39:1268-1280(2014).
RN [20]
RP GLYCOSYLATION AT ASN-23 AND ASN-79, INTERACTION WITH GRID2; NRXN1 AND
RP NRXN3, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-23 AND ASN-79.
RX PubMed=29782851; DOI=10.1016/j.brainres.2018.05.022;
RA Rong Y., Bansal P.K., Wei P., Guo H., Correia K., Parris J., Morgan J.I.;
RT "Glycosylation of Cblns attenuates their receptor binding.";
RL Brain Res. 1694:129-139(2018).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29691328; DOI=10.1523/jneurosci.0360-18.2018;
RA Seigneur E., Suedhof T.C.;
RT "Genetic Ablation of All Cerebellins Reveals Synapse Organizer Functions in
RT Multiple Regions Throughout the Brain.";
RL J. Neurosci. 38:4774-4790(2018).
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 (PubMed:16234806).
CC Plays a role as a synaptic organizer that acts bidirectionally on both
CC pre- and post-synaptic components (PubMed:20395510). On the one hand
CC induces accumulation of synaptic vesicles in the pre-synaptic part by
CC binding with NRXN1 and in other hand induces clustering of GRID2 and
CC its associated proteins at the post-synaptic site through association
CC of GRID2 (PubMed:21410790). NRXN1-CBLN1-GRID2 complex directly induces
CC parallel fiber protrusions that encapsulate spines of Purkinje cells
CC leading to accumulation of GRID2 and synaptic vesicles
CC (PubMed:23141067). Required for CBLN3 export from the endoplasmic
CC reticulum and secretion (PubMed:17030622, PubMed:17331201). NRXN1-
CC CBLN1-GRID2 complex mediates the D-Serine-dependent long term
CC depression signals and AMPA receptor endocytosis (By similarity).
CC Essential for long-term maintenance but not establishment of excitatory
CC synapses (PubMed:29691328). Inhibits the formation and function of
CC inhibitory GABAergic synapses in cerebellar Purkinje cells
CC (PubMed:24467251). {ECO:0000250|UniProtKB:P23435,
CC ECO:0000269|PubMed:16234806, ECO:0000269|PubMed:17030622,
CC ECO:0000269|PubMed:17331201, ECO:0000269|PubMed:20395510,
CC ECO:0000269|PubMed:21410790, ECO:0000269|PubMed:23141067,
CC ECO:0000269|PubMed:24467251, ECO:0000269|PubMed:29691328}.
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
CC (PubMed:16135095). May form oligomers with CBLN2, CBLN3 AND CBLN4 prior
CC to secretion (PubMed:29782851). Once secreted, does not interact with
CC other CBLN family members (PubMed:17030622, PubMed:17331201,
CC PubMed:10964938). Interacts with GRID1 (PubMed:22220752). Interacts
CC with NRXN1 and NRXN2 long (alpha) and short (beta) isoforms produced by
CC alternative promoter usage (PubMed:21410790, PubMed:22220752,
CC PubMed:29782851). Competes with NLGN1 for NRXN1-binding. Weakly
CC interacts with NRXN3 short isoform and not at all with NRXN3 long
CC isoform (PubMed:21410790, PubMed:22220752, PubMed:29782851). Interacts
CC (via C1q domain) with GRID2; GRID2-binding is calcium-independent;
CC CBLN1 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 (PubMed:20395510, PubMed:21410790, PubMed:22220752, PubMed:29782851).
CC Interacts with OTOL1 (PubMed:20856818). {ECO:0000269|PubMed:10964938,
CC ECO:0000269|PubMed:16135095, ECO:0000269|PubMed:17030622,
CC ECO:0000269|PubMed:17331201, ECO:0000269|PubMed:20395510,
CC ECO:0000269|PubMed:20856818, ECO:0000269|PubMed:21410790,
CC ECO:0000269|PubMed:22220752, ECO:0000269|PubMed:29782851}.
CC -!- INTERACTION:
CC Q9R171; Q61625: Grid2; NbExp=8; IntAct=EBI-2794140, EBI-2794106;
CC Q9R171; P0DI97: Nrxn1; NbExp=4; IntAct=EBI-2794140, EBI-2794440;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17331201,
CC ECO:0000269|PubMed:29782851}. Postsynaptic cell membrane
CC {ECO:0000269|PubMed:19200061}. Note=Interaction with CBLN3 may cause
CC partial retention in the endoplasmic reticulum.
CC {ECO:0000269|PubMed:17331201}.
CC -!- TISSUE SPECIFICITY: Expressed and secreted by presynaptic neurons, such
CC as cerebellar granule cells. Following secretion, the protein binds to
CC GRID2 on the postsynaptic Purkinje cell membranes. Expressed at the
CC highest level in the cerebellar cortex. High levels are also seen in
CC the olfactory bulb, posterior part of the cerebral cortex, certain
CC thalamic nuclei, and deep cerebellar nuclei. Low to moderate levels are
CC detected in some hypothalamic and brainstem nuclei. In the thalamus,
CC expressed in parafascicular nucleus neurons and other regions (at
CC protein level). {ECO:0000269|PubMed:16930405,
CC ECO:0000269|PubMed:17030622, ECO:0000269|PubMed:22220752,
CC ECO:0000269|PubMed:23141067, ECO:0000269|PubMed:3199194,
CC ECO:0000269|PubMed:3420533}.
CC -!- DEVELOPMENTAL STAGE: In the developing brain, expressed as early as
CC embryonic day 10-13, and transiently up-regulated during the late
CC embryonic and neonatal periods. Cerebellin and [des-Ser1]-cerebellin
CC are expressed as easly as postnatal day 3-4. The levels of both
CC peptides rise rapidly to a maximum at approximately day 25-30 after
CC birth, whereafter they fall to stable adult values.
CC {ECO:0000269|PubMed:16930405, ECO:0000269|PubMed:3199194}.
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. In the cerebellum, cerebellin is much more abundant than [des-
CC Ser1]-cerebellin. {ECO:0000269|PubMed:16135095}.
CC -!- PTM: Sialoglycoprotein. {ECO:0000269|PubMed:29782851}.
CC -!- DISRUPTION PHENOTYPE: Mice (reeler, weaver and staggerer) show defects
CC in granule cell migration and parallel fiber formation, synaptogenesis,
CC Purkinje cell dendritic maturation and establishment of adult
CC cytoarchitecture show a correlation between the formation and number of
CC parallel fiber-Purkinje cell synapses and cerebellin levels
CC (PubMed:3199194). CBLN1 single knockout mice show a major impairment in
CC motor behaviors (PubMed:3420533). Double CBLN1 and CBLN2 knockout mice
CC exhibit gait abnormalities, impairments in balance and coordination and
CC develop seizures (PubMed:3420533). Synapse density in the hippocampus
CC is normal in 1-2 months old mice, but severely decreased in 6 month old
CC mice (PubMed:3420533). Triple CBLN1, CBLN2 and CBLN4 knockout mice
CC exhibit impairments in sensory processing and sensorimotor gating, in
CC addition to severe motor deficits, seizures and reduced synapse density
CC in the hippocampus of aging mice (PubMed:3420533).
CC {ECO:0000269|PubMed:3199194, ECO:0000269|PubMed:3420533}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43688.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AF164680; AAD47280.1; -; Genomic_DNA.
DR EMBL; X61448; CAA43688.1; ALT_SEQ; mRNA.
DR CCDS; CCDS22506.1; -.
DR PIR; S16862; S16862.
DR RefSeq; NP_062600.2; NM_019626.3.
DR AlphaFoldDB; Q9R171; -.
DR SMR; Q9R171; -.
DR BioGRID; 198528; 3.
DR IntAct; Q9R171; 3.
DR STRING; 10090.ENSMUSP00000034076; -.
DR GlyGen; Q9R171; 2 sites.
DR iPTMnet; Q9R171; -.
DR PhosphoSitePlus; Q9R171; -.
DR MaxQB; Q9R171; -.
DR PaxDb; Q9R171; -.
DR PRIDE; Q9R171; -.
DR ProteomicsDB; 265281; -.
DR Antibodypedia; 14491; 220 antibodies from 32 providers.
DR DNASU; 12404; -.
DR Ensembl; ENSMUST00000034076; ENSMUSP00000034076; ENSMUSG00000031654.
DR Ensembl; ENSMUST00000169693; ENSMUSP00000126575; ENSMUSG00000031654.
DR GeneID; 12404; -.
DR KEGG; mmu:12404; -.
DR UCSC; uc009mqr.1; mouse.
DR CTD; 869; -.
DR MGI; MGI:88281; Cbln1.
DR VEuPathDB; HostDB:ENSMUSG00000031654; -.
DR eggNOG; ENOG502QVN9; Eukaryota.
DR GeneTree; ENSGT00940000159811; -.
DR HOGENOM; CLU_001074_8_2_1; -.
DR InParanoid; Q9R171; -.
DR OMA; NRTMLIY; -.
DR OrthoDB; 1398761at2759; -.
DR PhylomeDB; Q9R171; -.
DR TreeFam; TF329591; -.
DR BioGRID-ORCS; 12404; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Cbln1; mouse.
DR PRO; PR:Q9R171; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9R171; protein.
DR Bgee; ENSMUSG00000031654; Expressed in cerebellum lobe and 134 other tissues.
DR ExpressionAtlas; Q9R171; baseline and differential.
DR Genevisible; Q9R171; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0021707; P:cerebellar granule cell differentiation; IGI:BHF-UCL.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IGI:BHF-UCL.
DR GO; GO:0099558; P:maintenance of synapse structure; IMP:UniProtKB.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:1905703; P:negative regulation of inhibitory synapse assembly; IMP:UniProtKB.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; ISO:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:0009306; P:protein secretion; IMP:MGI.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0007416; P:synapse assembly; IDA:MGI.
DR GO; GO:0050808; P:synapse organization; IMP: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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Membrane; Postsynaptic cell membrane; Reference proteome; Secreted;
KW Sialic acid; Signal; Synapse.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..193
FT /note="Cerebellin-1"
FT /id="PRO_0000274211"
FT PEPTIDE 57..72
FT /note="Cerebellin"
FT /id="PRO_0000003549"
FT PEPTIDE 58..72
FT /note="[des-Ser1]-cerebellin"
FT /id="PRO_0000274212"
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:0000269|PubMed:17030622"
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:0000269|PubMed:16234806,
FT ECO:0000269|PubMed:29782851"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16234806,
FT ECO:0000269|PubMed:29782851"
FT DISULFID 34
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:16135095"
FT DISULFID 38
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:16135095"
FT MUTAGEN 23
FT /note="N->Q: No effect on its ability to form homohexameric
FT or heteromeric complexes with other CBLN family members.
FT Increased interaction with GRID2, NRXN1 and NRXN3. Loss of
FT N-glycosylation; when associated with Q-79."
FT /evidence="ECO:0000269|PubMed:16234806,
FT ECO:0000269|PubMed:29782851"
FT MUTAGEN 34
FT /note="C->A: Abolishes homohexamer formation from
FT homotrimers; when associated with A-38."
FT /evidence="ECO:0000269|PubMed:16135095"
FT MUTAGEN 38
FT /note="C->A: Abolishes homohexamer formation from
FT homotrimers; when associated with A-34."
FT /evidence="ECO:0000269|PubMed:16135095"
FT MUTAGEN 79
FT /note="N->Q: No effect on its ability to form homohexameric
FT or heteromeric complexes with other CBLN family members.
FT Increased interaction with GRID2, NRXN1 and NRXN3. Loss of
FT N-glycosylation; when associated with Q-23."
FT /evidence="ECO:0000269|PubMed:16234806,
FT ECO:0000269|PubMed:29782851"
FT MUTAGEN 110
FT /note="G->E: Retention in the endoplasmic reticulum/cis-
FT Golgi; when associated with H-112."
FT /evidence="ECO:0000269|PubMed:17331201"
FT MUTAGEN 112
FT /note="Y->H: Retention in the endoplasmic reticulum/cis-
FT Golgi; when associated with E-110."
FT /evidence="ECO:0000269|PubMed:17331201"
FT CONFLICT 5
FT /note="V -> L (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 193 AA; 21113 MW; A23C796C7D11BE5F CRC64;
MLGVVELLLL GTAWLAGPAR GQNETEPIVL EGKCLVVCDS NPTSDPTGTA LGISVRSGSA
KVAFSAIRST NHEPSEMSNR TMIIYFDQVL VNIGNNFDSE RSTFIAPRKG IYSFNFHVVK
VYNRQTIQVS LMLNGWPVIS AFAGDQDVTR EAASNGVLIQ MEKGDRAYLK LERGNLMGGW
KYSTFSGFLV FPL
