CBLN2_RAT
ID CBLN2_RAT Reviewed; 224 AA.
AC P98087; Q5BJT3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Cerebellin-2;
DE AltName: Full=Cerebellin-like protein;
DE Flags: Precursor;
GN Name=Cbln2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1850079; DOI=10.1016/0169-328x(91)90131-g;
RA Wada C., Ohtani H.;
RT "Molecular cloning of rat cerebellin-like protein cDNA which encodes a
RT novel membrane-associated glycoprotein.";
RL Brain Res. Mol. Brain Res. 9:71-77(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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.
RX PubMed=15702230;
RA Rucinski M., Albertin G., Spinazzi R., Ziolkowska A., Nussdorfer G.G.,
RA Malendowicz L.K.;
RT "Cerebellin in the rat adrenal gland: gene expression and effects of CER
RT and [des-Ser1]CER on the secretion and growth of cultured adrenocortical
RT cells.";
RL Int. J. Mol. Med. 15:411-415(2005).
CC -!- FUNCTION: Acts as a synaptic organizer in specific subsets of neurons
CC in the brain (By similarity). Essential for long-term maintenance but
CC not establishment of excitatory synapses (By similarity).
CC {ECO:0000250|UniProtKB:Q8BGU2}.
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 homooligomers or heterooligomers with CBLN1 and CBLN3 prior to
CC secretion. Once secreted, does not interact with other CBLN family
CC members. Interacts with GRID2, and more weakly with GRID1. Interacts
CC with NRXN1 and NRXN2 long and short isoforms produced by alternative
CC promoter usage. Weakly interacts with NRXN3 short isoform and not at
CC all with NRXN3 long isoform (By similarity).
CC {ECO:0000250|UniProtKB:Q8BGU2, ECO:0000250|UniProtKB:Q9R171}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8BGU2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=P98087-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Brain (cerebellum), adrenal gland and spleen. In
CC the adrenal gland, expressed at high levels in the zona glomerulosa and
CC at low levels in the zona fasciculata-reticularis.
CC {ECO:0000269|PubMed:15702230}.
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DR EMBL; BC091341; AAH91341.1; -; mRNA.
DR PIR; A60032; A60032.
DR RefSeq; NP_001012758.1; NM_001012740.1. [P98087-1]
DR RefSeq; XP_006255085.1; XM_006255023.3. [P98087-1]
DR RefSeq; XP_006255086.1; XM_006255024.3. [P98087-1]
DR AlphaFoldDB; P98087; -.
DR SMR; P98087; -.
DR STRING; 10116.ENSRNOP00000018682; -.
DR GlyGen; P98087; 2 sites.
DR PhosphoSitePlus; P98087; -.
DR PaxDb; P98087; -.
DR Ensembl; ENSRNOT00000018682; ENSRNOP00000018682; ENSRNOG00000013654. [P98087-1]
DR GeneID; 291388; -.
DR KEGG; rno:291388; -.
DR CTD; 147381; -.
DR RGD; 1309715; Cbln2.
DR eggNOG; ENOG502QT93; Eukaryota.
DR GeneTree; ENSGT00940000159988; -.
DR HOGENOM; CLU_001074_8_2_1; -.
DR InParanoid; P98087; -.
DR OMA; ACYPVRA; -.
DR OrthoDB; 1398761at2759; -.
DR PhylomeDB; P98087; -.
DR TreeFam; TF329591; -.
DR PRO; PR:P98087; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000013654; Expressed in frontal cortex and 8 other tissues.
DR Genevisible; P98087; RN.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0099558; P:maintenance of synapse structure; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:0098814; P:spontaneous synaptic transmission; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..51
FT /evidence="ECO:0000255"
FT CHAIN 52..224
FT /note="Cerebellin-2"
FT /id="PRO_0000003553"
FT DOMAIN 88..224
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 64
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
FT DISULFID 68
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
SQ SEQUENCE 224 AA; 24023 MW; A8C3ED240CEA53A7 CRC64;
MPAPGRGPRG PLLSMPGRRG ALREPADFGS SLGAALALLL LLLPACCPVK AQNDTEPIVL
EGKCLVVCDS SPSGDGAVTS SLGISVRSGS AKVAFSATRS TNHEPSEMSN RTMTIYFDQV
LVNIGNHFDL ASSIFVAPRK GIYSFSFHVV KVYNRQTIQV SLMQNGYPVI SAFAGDQDVT
REAASNGVLL LMEREDKVHL KLERGNLMGG WKYSTFSGFL VFPL
