CBLN3_HUMAN
ID CBLN3_HUMAN Reviewed; 205 AA.
AC Q6UW01;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Cerebellin-3;
DE Flags: Precursor;
GN Name=CBLN3; ORFNames=UNQ755/PRO1486;
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].
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 [2]
RP PROTEIN SEQUENCE OF 33-47.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
CC -!- FUNCTION: May be involved in synaptic functions in the CNS.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; disulfide-linked heterotrimers. Interacts with
CC CBLN1. May also form oligomers with CBLN2 AND CBLN4 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JHG0, ECO:0000250|UniProtKB:Q9R171}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi
CC apparatus, cis-Golgi network {ECO:0000250}. Secreted {ECO:0000250}.
CC Synapse {ECO:0000250}. Note=In the absence of CBLN1, remains in the
CC endoplasmic reticulum/cis-Golgi apparatus. Partial secretion depends on
CC an association with CBLN1 and maybe CBLN4, but not on CBLN2 (By
CC similarity). {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY359070; AAQ89429.1; -; mRNA.
DR CCDS; CCDS32057.1; -.
DR RefSeq; NP_001034860.1; NM_001039771.2.
DR AlphaFoldDB; Q6UW01; -.
DR SMR; Q6UW01; -.
DR STRING; 9606.ENSP00000267406; -.
DR GlyGen; Q6UW01; 1 site.
DR iPTMnet; Q6UW01; -.
DR PhosphoSitePlus; Q6UW01; -.
DR BioMuta; CBLN3; -.
DR DMDM; 52782722; -.
DR MassIVE; Q6UW01; -.
DR PaxDb; Q6UW01; -.
DR PeptideAtlas; Q6UW01; -.
DR PRIDE; Q6UW01; -.
DR ProteomicsDB; 67440; -.
DR Antibodypedia; 50437; 80 antibodies from 18 providers.
DR DNASU; 643866; -.
DR Ensembl; ENST00000267406.11; ENSP00000267406.6; ENSG00000139899.11.
DR GeneID; 643866; -.
DR KEGG; hsa:643866; -.
DR MANE-Select; ENST00000267406.11; ENSP00000267406.6; NM_001039771.3; NP_001034860.1.
DR UCSC; uc001wpg.5; human.
DR CTD; 643866; -.
DR GeneCards; CBLN3; -.
DR HGNC; HGNC:20146; CBLN3.
DR HPA; ENSG00000139899; Tissue enriched (brain).
DR MIM; 612978; gene.
DR neXtProt; NX_Q6UW01; -.
DR OpenTargets; ENSG00000139899; -.
DR PharmGKB; PA134885212; -.
DR VEuPathDB; HostDB:ENSG00000139899; -.
DR eggNOG; ENOG502QVN9; Eukaryota.
DR GeneTree; ENSGT00940000162110; -.
DR HOGENOM; CLU_001074_8_2_1; -.
DR InParanoid; Q6UW01; -.
DR OMA; VNEGNGF; -.
DR PhylomeDB; Q6UW01; -.
DR TreeFam; TF329591; -.
DR PathwayCommons; Q6UW01; -.
DR SignaLink; Q6UW01; -.
DR BioGRID-ORCS; 643866; 8 hits in 1074 CRISPR screens.
DR GenomeRNAi; 643866; -.
DR Pharos; Q6UW01; Tdark.
DR PRO; PR:Q6UW01; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q6UW01; protein.
DR Bgee; ENSG00000139899; Expressed in cerebellar vermis and 105 other tissues.
DR ExpressionAtlas; Q6UW01; baseline and differential.
DR Genevisible; Q6UW01; HS.
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; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
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 Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Reference proteome; Secreted; Signal;
KW Synapse.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 33..205
FT /note="Cerebellin-3"
FT /id="PRO_0000003554"
FT DOMAIN 67..205
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT REGION 72..205
FT /note="Necessary for interaction with CBLN3, and
FT homotrimerization"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
FT DISULFID 49
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R171"
SQ SEQUENCE 205 AA; 21521 MW; 500991AFBB834946 CRC64;
MLGAKPHWLP GPLHSPGLPL VLVLLALGAG WAQEGSEPVL LEGECLVVCE PGRAAAGGPG
GAALGEAPPG RVAFAAVRSH HHEPAGETGN GTSGAIYFDQ VLVNEGGGFD RASGSFVAPV
RGVYSFRFHV VKVYNRQTVQ VSLMLNTWPV ISAFANDPDV TREAATSSVL LPLDPGDRVS
LRLRRGNLLG GWKYSSFSGF LIFPL
