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Q9JMB8 (CNTN6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Contactin-6
Alternative name(s):
Neural recognition molecule NB-3
Short name=mNB-3
Gene names
Name:Cntn6
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1028 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Contactins mediate cell surface interactions during nervous system development. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus By similarity. Involved in motor coordination. Ref.4

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor By similarity.

Tissue specificity

Expressed in brain. In brain, it is preferentially expressed in the accessory olfactory bulb, layers II/III and V of the cerebral cortex, piriform cortex, anterior thalamic nuclei, locus coeruleus of the pons and mesencephalic trigeminal nucleus and in Purkinje cells of the cerebellum. Ref.1

Developmental stage

Highly expressed after birth, reaching a maximum at the postnatal day 7, and declines thereafter in the cerebrum, whereas it increases in the cerebellum to adulthood. Ref.1

Disruption phenotype

Mice are viable and fertile, the formation and organization of all nuclei and layers throughout the brains are apparently normal. They are however slow to learn to stay on the rotating rod in the rotorod test during repeated trials, and display dysfunction of equilibrium and vestibular senses in the wire hang and horizontal rod-walking tests. Ref.4

Sequence similarities

Belongs to the immunoglobulin superfamily. Contactin family.

Contains 4 fibronectin type-III domains.

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JMB8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9JMB8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     62-78: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 999980Contactin-6
PRO_0000014729
Propeptide1000 – 102829Removed in mature form Potential
PRO_0000014730

Regions

Domain32 – 11786Ig-like C2-type 1
Domain122 – 20887Ig-like C2-type 2
Domain227 – 30882Ig-like C2-type 3
Domain318 – 40285Ig-like C2-type 4
Domain408 – 50295Ig-like C2-type 5
Domain500 – 58788Ig-like C2-type 6
Domain597 – 69397Fibronectin type-III 1
Domain700 – 79697Fibronectin type-III 2
Domain802 – 89897Fibronectin type-III 3
Domain903 – 99290Fibronectin type-III 4

Amino acid modifications

Modified residue8821Phosphotyrosine By similarity
Lipidation9991GPI-anchor amidated serine Potential
Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation3771N-linked (GlcNAc...) Potential
Glycosylation4681N-linked (GlcNAc...) Potential
Glycosylation6591N-linked (GlcNAc...) Potential
Glycosylation7651N-linked (GlcNAc...) Potential
Glycosylation8601N-linked (GlcNAc...) Potential
Glycosylation8651N-linked (GlcNAc...) Potential
Glycosylation8951N-linked (GlcNAc...) Potential
Glycosylation9311N-linked (GlcNAc...) Potential
Glycosylation9561N-linked (GlcNAc...) Potential
Glycosylation9571N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 100 By similarity
Disulfide bond144 ↔ 196 By similarity
Disulfide bond249 ↔ 297 By similarity
Disulfide bond339 ↔ 386 By similarity
Disulfide bond431 ↔ 479 By similarity
Disulfide bond521 ↔ 577 By similarity

Natural variations

Alternative sequence62 – 7817Missing in isoform 2.
VSP_011968

Experimental info

Sequence conflict2621K → R in BAA92367. Ref.1
Sequence conflict8921L → P in BAA92367. Ref.1
Sequence conflict9211L → V in BAA92367. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 23, 2004. Version 2.
Checksum: B233ED300881B101

FASTA1,028113,761
        10         20         30         40         50         60 
MRLLWKLVIL LPLINSCAGE GRFSRPIFIQ EPQDVIFPLD LSRSEIILTC TANGYPSPHY 

        70         80         90        100        110        120 
RWKQNGTDID FGMTYHYRLD GGSLAISSPR TDQDIGIYQC LATNPVGTIL SRKAKLQFAY 

       130        140        150        160        170        180 
IEDFETKTRS TVSVREGQGV VLLCGPPPHF GELSYAWTFN DSPLYVQEDK RRFVSQDTGN 

       190        200        210        220        230        240 
LYFAKVEPSD VGNYTCFVTN KEAHRSVQGP PTPLVLRTDG VMGEYEPKIE VRFPETIQAA 

       250        260        270        280        290        300 
KDSSIKLECF ALGNPVPDIS WKRLDGSPMP GKIKYSKSQA ILEIPKFQQE DEGFYECIAG 

       310        320        330        340        350        360 
NLRGRNLAKG QLIFYAPPEW EQKIQNTYLS IYDSLFWECK ASGNPNPSYT WLKNGQRLNT 

       370        380        390        400        410        420 
EERIQIENGT LIITMLNISD SGIYQCAAEN KYQTIYANAE LRVLASAPDF SKNPIKKISV 

       430        440        450        460        470        480 
VQVGGDISIE CKPNAFPKAS ISWKRGTENL KQSKRVLFLE DGSLKICNVT RADAGSYTCV 

       490        500        510        520        530        540 
ATNQFGNGKS SGGLVVKERT IITVPPSKMD VTVGESIVLP CQVSHDPTME VLFVWYFNGD 

       550        560        570        580        590        600 
IIDLKKGVAH FERIGGESVG DLMIRNIQLG HSGKYLCTVQ TTLERLSAVA DIIVRGPPGP 

       610        620        630        640        650        660 
PEDVKVEHIS STTSQLSWRP GPDNNSPIQI FTIQTRTPFS VGWQAVATVP EILNGQTYNA 

       670        680        690        700        710        720 
TVVGLSPWVE YEFRVVAGNN IGIGEPSKPS ELLRTKASVP NVAPGNINGG GGSRSELVIT 

       730        740        750        760        770        780 
WEAIPEELQN GEGFGYIVMF RPVGTTAWMK ERVALVESSK FIYRNESIMP LSPFEVKVGV 

       790        800        810        820        830        840 
YNNEGEGSLS TVTIVYSGED EPQLAPRGTS VQSFSASEME VSWNAIAWNR NTGRVLGYEV 

       850        860        870        880        890        900 
LYWTDNSKES MIGKIRVSGN VTTKNITGLR ANTIYFASVR AYNTAGTGPS SLPVNVTTKK 

       910        920        930        940        950        960 
SPPSQPPANI AWKLSNSKLC LNWEHVKTME NESEVLGYKI LYRQNRQSKT HILETNNTSA 

       970        980        990       1000       1010       1020 
ELLVPFEEDY LIEIRTVSDG GDGSSSEEIR IPKMSSLSST GVQISKPSTQ SLSMVGVFYC 


FAIHPLSR

« Hide

Isoform 2 [UniParc].

Checksum: 2063EDAD11A2B3A6
Show »

FASTA1,011111,647

References

« Hide 'large scale' references
[1]"Expression and regulation of a gene encoding neural recognition molecule NB-3 of the contactin/F3 subgroup in mouse brain."
Lee S., Takeda Y., Kawano H., Hosoya H., Nomoto M., Fujimoto D., Takahashi N., Watanabe K.
Gene 245:253-266(2000) [PubMed: 10717476] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: 129/SvJ.
Tissue: Brain.
[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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Head.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Eye.
[4]"Impaired motor coordination in mice lacking neural recognition molecule NB-3 of the contactin/F3 subgroup."
Takeda Y., Akasaka K., Lee S., Kobayashi S., Kawano H., Murayama S., Takahashi N., Hashimoto K., Kano M., Asano M., Sudo K., Iwakura Y., Watanabe K.
J. Neurobiol. 56:252-265(2003) [PubMed: 12884264] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB032602 mRNA. Translation: BAA92367.1.
AK052972 mRNA. Translation: BAC35227.1.
BC076594 mRNA. Translation: AAH76594.1.
IPIIPI00312433.
IPI00480564.
RefSeqNP_059079.2. NM_017383.3.
UniGeneMm.321671.

3D structure databases

ProteinModelPortalQ9JMB8.
SMRQ9JMB8. Positions 24-999.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-6439843.
STRINGQ9JMB8.

PTM databases

PhosphoSiteQ9JMB8.

Proteomic databases

PRIDEQ9JMB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089215; ENSMUSP00000086623; ENSMUSG00000030092.
ENSMUST00000162872; ENSMUSP00000124025; ENSMUSG00000030092.
GeneID53870.
KEGGmmu:53870.
UCSCuc009dco.1. mouse.

Organism-specific databases

CTD27255.
MGIMGI:1858223. Cntn6.

Phylogenomic databases

eggNOGroNOG05909.
GeneTreeENSGT00550000074380.
HOGENOMHBG444805.
HOVERGENHBG051047.
InParanoidQ9JMB8.
OMAKLQFAYI.
OrthoDBEOG4PNXG6.
PhylomeDBQ9JMB8.

Gene expression databases

ArrayExpressQ9JMB8.
BgeeQ9JMB8.
CleanExMM_CNTN6.
GenevestigatorQ9JMB8.
GermOnlineENSMUSG00000030092. Mus musculus.

Family and domain databases

InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 10 hits.
KOK06764.
PfamPF00041. fn3. 2 hits.
PF07679. I-set. 6 hits.
[Graphical view]
SMARTSM00060. FN3. 4 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 5 hits.
[Graphical view]
SUPFAMSSF49265. FN_III-like. 4 hits.
PROSITEPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio310721.
SOURCESearch...

Entry information

Entry nameCNTN6_MOUSE
AccessionPrimary (citable) accession number: Q9JMB8
Secondary accession number(s): Q8C6X1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: November 16, 2011
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents