CBLN2_HUMAN
ID CBLN2_HUMAN Reviewed; 224 AA.
AC Q8IUK8; Q53Z56;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cerebellin-2;
DE Flags: Precursor;
GN Name=CBLN2; ORFNames=UNQ1892/PRO4338;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
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}.
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DR EMBL; AK291364; BAF84053.1; -; mRNA.
DR EMBL; AY359074; AAQ89433.1; -; mRNA.
DR EMBL; CH471117; EAW66527.1; -; Genomic_DNA.
DR EMBL; BC035789; AAH35789.1; -; mRNA.
DR CCDS; CCDS11999.1; -.
DR RefSeq; NP_872317.1; NM_182511.3.
DR RefSeq; XP_006722457.1; XM_006722394.3.
DR RefSeq; XP_011524126.1; XM_011525824.2.
DR RefSeq; XP_016881048.1; XM_017025559.1.
DR RefSeq; XP_016881049.1; XM_017025560.1.
DR AlphaFoldDB; Q8IUK8; -.
DR SMR; Q8IUK8; -.
DR STRING; 9606.ENSP00000269503; -.
DR GlyGen; Q8IUK8; 2 sites.
DR iPTMnet; Q8IUK8; -.
DR PhosphoSitePlus; Q8IUK8; -.
DR BioMuta; CBLN2; -.
DR DMDM; 46395886; -.
DR EPD; Q8IUK8; -.
DR MassIVE; Q8IUK8; -.
DR PaxDb; Q8IUK8; -.
DR PeptideAtlas; Q8IUK8; -.
DR PRIDE; Q8IUK8; -.
DR ProteomicsDB; 70583; -.
DR Antibodypedia; 42209; 168 antibodies from 26 providers.
DR DNASU; 147381; -.
DR Ensembl; ENST00000269503.9; ENSP00000269503.4; ENSG00000141668.10.
DR Ensembl; ENST00000585159.5; ENSP00000463771.1; ENSG00000141668.10.
DR GeneID; 147381; -.
DR KEGG; hsa:147381; -.
DR MANE-Select; ENST00000269503.9; ENSP00000269503.4; NM_182511.4; NP_872317.1.
DR UCSC; uc002lku.4; human.
DR CTD; 147381; -.
DR DisGeNET; 147381; -.
DR GeneCards; CBLN2; -.
DR HGNC; HGNC:1544; CBLN2.
DR HPA; ENSG00000141668; Tissue enriched (brain).
DR MIM; 600433; gene.
DR neXtProt; NX_Q8IUK8; -.
DR OpenTargets; ENSG00000141668; -.
DR PharmGKB; PA26119; -.
DR VEuPathDB; HostDB:ENSG00000141668; -.
DR eggNOG; ENOG502QT93; Eukaryota.
DR GeneTree; ENSGT00940000159988; -.
DR InParanoid; Q8IUK8; -.
DR OMA; ACYPVRA; -.
DR OrthoDB; 1398761at2759; -.
DR PhylomeDB; Q8IUK8; -.
DR TreeFam; TF329591; -.
DR PathwayCommons; Q8IUK8; -.
DR BioGRID-ORCS; 147381; 13 hits in 1070 CRISPR screens.
DR ChiTaRS; CBLN2; human.
DR GenomeRNAi; 147381; -.
DR Pharos; Q8IUK8; Tbio.
DR PRO; PR:Q8IUK8; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q8IUK8; protein.
DR Bgee; ENSG00000141668; Expressed in superior frontal gyrus and 117 other tissues.
DR ExpressionAtlas; Q8IUK8; baseline and differential.
DR Genevisible; Q8IUK8; HS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
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 Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..51
FT /evidence="ECO:0000255"
FT CHAIN 52..224
FT /note="Cerebellin-2"
FT /id="PRO_0000003551"
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; 24084 MW; A08C8BB3D686A9C5 CRC64;
MQAPGRGPLG LRLMMPGRRG ALREPGGCGS CLGVALALLL LLLPACCPVR AQNDTEPIVL
EGKCLVVCDS SPSADGAVTS SLGISVRSGS AKVAFSATRS TNHEPSEMSN RTMTIYFDQV
LVNIGNHFDL ASSIFVAPRK GIYSFSFHVV KVYNRQTIQV SLMQNGYPVI SAFAGDQDVT
REAASNGVLL LMEREDKVHL KLERGNLMGG WKYSTFSGFL VFPL
