CBLN3_BOVIN
ID CBLN3_BOVIN Reviewed; 205 AA.
AC Q17QF9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Cerebellin-3;
DE Flags: Precursor;
GN Name=CBLN3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC118385; AAI18386.1; -; mRNA.
DR RefSeq; NP_001073071.1; NM_001079603.1.
DR AlphaFoldDB; Q17QF9; -.
DR SMR; Q17QF9; -.
DR STRING; 9913.ENSBTAP00000014103; -.
DR PaxDb; Q17QF9; -.
DR Ensembl; ENSBTAT00000014103; ENSBTAP00000014103; ENSBTAG00000010665.
DR GeneID; 529166; -.
DR KEGG; bta:529166; -.
DR CTD; 643866; -.
DR VEuPathDB; HostDB:ENSBTAG00000010665; -.
DR VGNC; VGNC:26813; CBLN3.
DR eggNOG; ENOG502QVN9; Eukaryota.
DR GeneTree; ENSGT00940000162110; -.
DR InParanoid; Q17QF9; -.
DR OMA; VNEGNGF; -.
DR OrthoDB; 1398761at2759; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000010665; Expressed in abdominal lymph node and 91 other tissues.
DR ExpressionAtlas; Q17QF9; baseline.
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 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Reference proteome; Secreted; Signal; Synapse.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..205
FT /note="Cerebellin-3"
FT /id="PRO_0000274217"
FT DOMAIN 67..205
FT /note="C1q"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
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; 21747 MW; E69E7D7F1C96DB80 CRC64;
MLGTKRHWPP GPSLSLELPL ALTLLALRAG WAQEGTEPVL LEGECLVVCE PGRAAAGGPG
GAALGEAPPG RVAFAAVRSH HHEPAGEIGN GTSGAIYFDQ VLVNEGGGFD RTSGSFVAPV
RGVYSFRFHV VKVYNRQTVQ VSLMLNTWPV VSAFANDPDV TREAATSSVL LPLDPGDRVS
LRLRRGNLLG GWKYSSFSGF LIFPL
