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Protein

Cerebellin-4

Gene

Cbln4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in synaptic functions in the CNS. May play a role in CBLN3 export from the endoplasmic reticulum and secretion.

GO - Biological processi

  • protein secretion Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Cerebellin-4
Alternative name(s):
Cerebellin-like glycoprotein 1
Gene namesi
Name:Cbln4
Synonyms:Cblnl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2154433. Cbln4.

Subcellular locationi

GO - Cellular componenti

  • cell Source: GOC
  • cell junction Source: UniProtKB-KW
  • extracellular space Source: MGI
  • synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Secreted, Synapse

Pathology & Biotechi

Disruption phenotypei

Mutant animals are fertile, have normal life spans and have no overt anatomical abnormalities. They have a normal corpus callosum, hippocampal commisure and pontine nucleus and no other gross neuroanatomical abnormalities.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 261N → Q: Total loss of N-glycosylation; when associated with Q-110. 1 Publication
Mutagenesisi85 – 851N → Q: Total loss of N-glycosylation; when associated with Q-53. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 198174Cerebellin-4PRO_0000003557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi26 – 261N-linked (GlcNAc...)1 Publication
Disulfide bondi37 – 37InterchainBy similarity
Disulfide bondi41 – 41InterchainBy similarity
Glycosylationi85 – 851N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8BME9.
PaxDbiQ8BME9.
PRIDEiQ8BME9.

Expressioni

Tissue specificityi

Expressed in brain with high levels in particular thalamic nuclei. In the thalamus, predominantly expressed in neurons within the parafascicular nucleus (at protein level). Very low or no expression in most other brain regions.2 Publications

Developmental stagei

In the developing brain, expressed as early as 10-13 dpc. Expression level peaks at 18 dpc and gradually decreases afterwards.1 Publication

Gene expression databases

BgeeiQ8BME9.
CleanExiMM_CBLN4.
GenevisibleiQ8BME9. MM.

Interactioni

Subunit structurei

Homohexamer; disulfide-linked homotrimers. The trimers are assembled via the globular C1q domains. The trimers associate via N-terminal cysteine residues to form disulfide-linked hexamers (By similarity). May form oligomers with CBLN1, CBLN2 and CBLN3 prior to secretion. Once secreted, does not interact with other CBLN family members. Strongly interacts with DCC in a NTN1-displaceable fashion. Weakly binds to NRXN1 and NRXN2 long and short isoforms produced by alternative promoter usage. Interaction with NRXN3 short isoform is hardly detectable; no interaction at all with NRXN3 long isoform. Does not interact with GRID1 and GRID2.By similarity2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000085263.

Structurei

3D structure databases

ProteinModelPortaliQ8BME9.
SMRiQ8BME9. Positions 67-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 198136C1qPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C1q domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFXA. Eukaryota.
ENOG410Y16R. LUCA.
GeneTreeiENSGT00760000119052.
HOGENOMiHOG000085657.
HOVERGENiHBG108329.
InParanoidiQ8BME9.
OMAiRSNNHEP.
OrthoDBiEOG7MD4R8.
PhylomeDBiQ8BME9.
TreeFamiTF329591.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
[Graphical view]
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BME9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSARRALSV VPAVLLILVL PVWAQNDTEP IVLEGKCLVV CDSNPATDSK
60 70 80 90 100
GSSSSPLGIS VRAANSKVAF SAVRSTNHEP SEMSNKTRII YFDQILVNVG
110 120 130 140 150
NFFTLESVFV APRKGIYSFS FHVIKVYQSQ TIQVNLMLNG KPVISAFAGD
160 170 180 190
KDVTREAATN GVLLYLDKED KVYLKLEKGN LLGGWQYSTF SGFLVFPL
Length:198
Mass (Da):21,609
Last modified:March 1, 2003 - v1
Checksum:i5A35ACC1354C70D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121P → T in BAC27855 (PubMed:12617826).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY134663 mRNA. Translation: AAN08614.1.
AK032406 mRNA. Translation: BAC27855.1.
AK032621 mRNA. Translation: BAC27954.1.
CH466551 Genomic DNA. Translation: EDL06594.1.
BC094540 mRNA. Translation: AAH94540.1.
BC132025 mRNA. Translation: AAI32026.1.
BC132027 mRNA. Translation: AAI32028.1.
CCDSiCCDS17126.1.
RefSeqiNP_783439.1. NM_175631.3.
UniGeneiMm.40555.

Genome annotation databases

EnsembliENSMUST00000087950; ENSMUSP00000085263; ENSMUSG00000067578.
GeneIDi228942.
KEGGimmu:228942.
UCSCiuc008ock.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY134663 mRNA. Translation: AAN08614.1.
AK032406 mRNA. Translation: BAC27855.1.
AK032621 mRNA. Translation: BAC27954.1.
CH466551 Genomic DNA. Translation: EDL06594.1.
BC094540 mRNA. Translation: AAH94540.1.
BC132025 mRNA. Translation: AAI32026.1.
BC132027 mRNA. Translation: AAI32028.1.
CCDSiCCDS17126.1.
RefSeqiNP_783439.1. NM_175631.3.
UniGeneiMm.40555.

3D structure databases

ProteinModelPortaliQ8BME9.
SMRiQ8BME9. Positions 67-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000085263.

Proteomic databases

MaxQBiQ8BME9.
PaxDbiQ8BME9.
PRIDEiQ8BME9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087950; ENSMUSP00000085263; ENSMUSG00000067578.
GeneIDi228942.
KEGGimmu:228942.
UCSCiuc008ock.1. mouse.

Organism-specific databases

CTDi140689.
MGIiMGI:2154433. Cbln4.

Phylogenomic databases

eggNOGiENOG410IFXA. Eukaryota.
ENOG410Y16R. LUCA.
GeneTreeiENSGT00760000119052.
HOGENOMiHOG000085657.
HOVERGENiHBG108329.
InParanoidiQ8BME9.
OMAiRSNNHEP.
OrthoDBiEOG7MD4R8.
PhylomeDBiQ8BME9.
TreeFamiTF329591.

Miscellaneous databases

NextBioi379255.
PROiQ8BME9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BME9.
CleanExiMM_CBLN4.
GenevisibleiQ8BME9. MM.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q_dom.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
[Graphical view]
PRINTSiPR00007. COMPLEMNTC1Q.
SMARTiSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sexually dimorphic gene expression in the developing mouse gonad."
    Menke D.B., Page D.C.
    Gene Expr. Patterns 2:359-367(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Olfactory bulb.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Embryonic brain.
  5. "Distinct expression of Cbln family mRNAs in developing and adult mouse brains."
    Miura E., Iijima T., Yuzaki M., Watanabe M.
    Eur. J. Neurosci. 24:750-760(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  6. "Cbln1 is essential for interaction-dependent secretion of cbln3."
    Bao D., Pang Z., Morgan M.A., Parris J., Rong Y., Li L., Morgan J.I.
    Mol. Cell. Biol. 26:9327-9337(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, SUBCELLULAR LOCATION, INTERACTION WITH CBLN1; CBLN2 AND CBLN3.
  7. "Characterization of a transneuronal cytokine family Cbln - regulation of secretion by heteromeric assembly."
    Iijima T., Miura E., Matsuda K., Kamekawa Y., Watanabe M., Yuzaki M.
    Eur. J. Neurosci. 25:1049-1057(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: OLIGOMERIZATION WITH CBLN1; CBLN2; CBLN3 AND CBLN4, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-26 AND ASN-85, MUTAGENESIS OF ASN-26 AND ASN-85.
  8. "The Cbln family of proteins interact with multiple signaling pathways."
    Wei P., Pattarini R., Rong Y., Guo H., Bansal P.K., Kusnoor S.V., Deutch A.Y., Parris J., Morgan J.I.
    J. Neurochem. 121:717-729(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCC; NRXN1; NRXN2 AND NRXN3, LACK OF INTERACTION WITH GRID1 AND GRID2, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCBLN4_MOUSE
AccessioniPrimary (citable) accession number: Q8BME9
Secondary accession number(s): Q505H5, Q8BMF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2003
Last modified: November 11, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.