CBLN3_MOUSE
ID CBLN3_MOUSE Reviewed; 197 AA.
AC Q9JHG0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cerebellin-3;
DE Flags: Precursor;
GN Name=Cbln3;
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 / MRNA], AND INTERACTION WITH CBLN1.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH CBLN1; CBLN2 AND CBLN4, AND
RP MUTAGENESIS OF ARG-119.
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 [5]
RP OLIGOMERIZATION WITH CBLN1; CBLN2; CBLN3 AND CBLN4, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: May be involved in synaptic functions in the CNS.
CC -!- SUBUNIT: Heterohexamer; disulfide-linked heterotrimers (By similarity).
CC Interacts with CBLN1. May also form oligomers with CBLN2 AND CBLN4.
CC {ECO:0000250|UniProtKB:Q9R171, ECO:0000269|PubMed:10964938,
CC ECO:0000269|PubMed:17030622}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus, cis-Golgi
CC network. Secreted. Synapse. Note=In the absence of CBLN1, remains in
CC the endoplasmic reticulum/cis-Golgi apparatus. Partial secretion
CC depends on an association with CBLN1 and maybe CBLN4, but not on CBLN2.
CC -!- TISSUE SPECIFICITY: Expressed in brain, restricted to the cerebellar
CC cortex. Within the cerebellum, expressed in granule layers (at protein
CC level). Also detected in postsynaptic Purkinje cell spines (at protein
CC level). {ECO:0000269|PubMed:16930405, ECO:0000269|PubMed:17331201}.
CC -!- DEVELOPMENTAL STAGE: In the developing brain, selectively expressed as
CC early as postnatal day 7-10 in cerebellar granule cells.
CC {ECO:0000269|PubMed:16930405}.
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DR EMBL; AF218380; AAF32315.1; -; Genomic_DNA.
DR EMBL; AF218379; AAF32314.1; -; mRNA.
DR EMBL; BC065108; AAH65108.1; -; mRNA.
DR CCDS; CCDS27133.1; -.
DR RefSeq; NP_062794.1; NM_019820.3.
DR AlphaFoldDB; Q9JHG0; -.
DR SMR; Q9JHG0; -.
DR BioGRID; 207961; 1.
DR STRING; 10090.ENSMUSP00000070494; -.
DR GlyConnect; 2206; 1 N-Linked glycan (1 site).
DR GlyGen; Q9JHG0; 1 site, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q9JHG0; -.
DR PaxDb; Q9JHG0; -.
DR PeptideAtlas; Q9JHG0; -.
DR PRIDE; Q9JHG0; -.
DR ProteomicsDB; 265344; -.
DR Antibodypedia; 50437; 80 antibodies from 18 providers.
DR DNASU; 56410; -.
DR Ensembl; ENSMUST00000063871; ENSMUSP00000070494; ENSMUSG00000040380.
DR Ensembl; ENSMUST00000172378; ENSMUSP00000127798; ENSMUSG00000040380.
DR GeneID; 56410; -.
DR KEGG; mmu:56410; -.
DR UCSC; uc007uba.1; mouse.
DR CTD; 643866; -.
DR MGI; MGI:1889286; Cbln3.
DR VEuPathDB; HostDB:ENSMUSG00000040380; -.
DR eggNOG; ENOG502QVN9; Eukaryota.
DR GeneTree; ENSGT00940000162110; -.
DR HOGENOM; CLU_001074_8_2_1; -.
DR InParanoid; Q9JHG0; -.
DR OMA; VNEGNGF; -.
DR OrthoDB; 1398761at2759; -.
DR PhylomeDB; Q9JHG0; -.
DR TreeFam; TF329591; -.
DR BioGRID-ORCS; 56410; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9JHG0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JHG0; protein.
DR Bgee; ENSMUSG00000040380; Expressed in cerebellar vermis and 37 other tissues.
DR Genevisible; Q9JHG0; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0099558; P:maintenance of synapse structure; IBA:GO_Central.
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 Disulfide bond; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Reference proteome; Secreted; Signal; Synapse.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..197
FT /note="Cerebellin-3"
FT /id="PRO_0000003555"
FT DOMAIN 59..197
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 64..197
FT /note="Necessary for interaction with CBLN3, and
FT homotrimerization"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
FT DISULFID 41
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
FT MUTAGEN 119
FT /note="R->A: Promotes self-association and secretion
FT independent of CBLN1."
FT /evidence="ECO:0000269|PubMed:17030622"
SQ SEQUENCE 197 AA; 21077 MW; DBA8925C9BB11B77 CRC64;
MGTEWHKPKL SLALVLLTLE AGWAQEGSEP VLLEGECLVV CEPGRPTAGG PGGAALGEAP
PGRVAFAAVR SHHHEPAGET GNGTSGAIYF DQVLVNEGEG FDRTSGCFVA PVRGVYSFRF
HVVKVYNRQT VQVSLMLNTW PVISAFANDP DVTREAATSS VLLPLDPGDR VSLRLRRGNL
LGGWKYSSFS GFLIFPL
