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UniProtKB/Swiss-Prot entry Q9JMB8


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CNTN6_MOUSE
Primary accession number Q9JMB8
Secondary accession number Q8C6X1
Integrated into Swiss-Prot on November 23, 2004
Sequence was last modified on November 23, 2004 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 63)
Name and origin of the protein
Protein name Contactin-6 [Precursor]
Synonyms Neural recognition molecule NB-3
mNB-3
Gene name
Name: Cntn6
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=129/SvJ;
TISSUE=Brain;
DOI=10.1016/S0378-1119(00)00031-7; PubMed=10717476 [NCBI, ExPASy, EBI, Israel, Japan]
Lee S., Takeda Y., Kawano H., Hosoya H., Nomoto M., Fujimoto D., Takahashi N., Watanabe K.;
"Expression and regulation of a gene encoding neural recognition molecule NB-3 of the contactin/F3 subgroup in mouse brain.";
Gene 245:253-266(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
TISSUE=Head;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6;
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
DOI=10.1002/neu.10222; PubMed=12884264 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Impaired motor coordination in mice lacking neural recognition molecule NB-3 of the contactin/F3 subgroup.";
J. Neurobiol. 56:252-265(2003).
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.
  • SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor (By similarity).
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ9JMB8-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ9JMB8-2
    Features which should be applied to build the isoform sequence: VSP_011968.
  • 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.
  • 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.
  • 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.
  • SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin family.
  • SIMILARITY: Contains 4 fibronectin type-III domains.
  • SIMILARITY: Contains 6 Ig-like C2-type (immunoglobulin-like) domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB032602; BAA92367.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK052972; BAC35227.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC076594; AAH76594.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00312433; -.
IPI00480564; -.
RefSeq NP_059079.2; -.
UniGene Mm.321671
3D structure databases
HSSP Q9UQH9; 1IIL. [HSSP ENTRY / PDB]
ModBase Q9JMB8.
PTM databases
PhosphoSite Q9JMB8; -.
Organism-specific databases
MGI MGI:1858223; Cntn6.
Gene expression databases
ArrayExpress Q9JMB8; -.
Bgee Q9JMB8; -.
CleanEx MM_CNTN6; -.
GermOnline ENSMUSG00000030092; Mus musculus.
Ontologies
GO
GO:0031225; Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005515; Molecular function: protein binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007155; Biological process: cell adhesion (inferred from electronic annotation from UniProtKB-KW).
GO:0007219; Biological process: Notch signaling pathway (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR008957; Fibronectin_typ-III-like_fold.
IPR003961; FN_III.
IPR013151; Ig.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR013098; Ig_I-set.
IPR003599; Ig_sub.
IPR003598; Ig_sub2.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.30; FN_III-like; 2.
G3DSA:2.60.40.10; Ig-like_fold; 6.
Pfam PF00041; fn3; 4.
PF07679; I-set; 4.
PF00047; ig; 2.
Pfam graphical view of domain structure.
SMART SM00060; FN3; 4.
SM00409; IG; 1.
SM00408; IGc2; 5.
SMART graphical view of domain structure.
PROSITE PS50853; FN3; 4.
PS50835; IG_LIKE; 6.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q9JMB8; -.
Genome annotation databases
Ensembl ENSMUSG00000030092; Mus musculus. [Contig view]
GeneID 53870; -.
KEGG mmu:53870; -.
Phylogenomic databases
HOGENOM Q9JMB8; -.
HOVERGEN Q9JMB8; -.
OMA Q9JMB8; CLNWEHV.
Other
NextBio 310721; -.
SOURCE Cntn6; Mus musculus.
ProtoNet Q9JMB8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane; Notch signaling pathway; Repeat; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     19  19     Potential. 
CHAIN   20    999  980     Contactin-6. PRO_0000014729
PROPEP   1000   1028  29     Removed in mature form (Potential). PRO_0000014730
DOMAIN   32    117  86     Ig-like C2-type 1. 
DOMAIN   122    208  87     Ig-like C2-type 2. 
DOMAIN   227    308  82     Ig-like C2-type 3. 
DOMAIN   318    402  85     Ig-like C2-type 4. 
DOMAIN   408    502  95     Ig-like C2-type 5. 
DOMAIN   500    587  88     Ig-like C2-type 6. 
DOMAIN   597    693  97     Fibronectin type-III 1. 
DOMAIN   700    796  97     Fibronectin type-III 2. 
DOMAIN   802    898  97     Fibronectin type-III 3. 
DOMAIN   903    992  90     Fibronectin type-III 4. 
LIPID   999    999        GPI-anchor amidated serine (Potential). 
CARBOHYD   65     65        N-linked (GlcNAc...) (Potential). 
CARBOHYD   193    193        N-linked (GlcNAc...) (Potential). 
CARBOHYD   368    368        N-linked (GlcNAc...) (Potential). 
CARBOHYD   377    377        N-linked (GlcNAc...) (Potential). 
CARBOHYD   468    468        N-linked (GlcNAc...) (Potential). 
CARBOHYD   659    659        N-linked (GlcNAc...) (Potential). 
CARBOHYD   765    765        N-linked (GlcNAc...) (Potential). 
CARBOHYD   860    860        N-linked (GlcNAc...) (Potential). 
CARBOHYD   865    865        N-linked (GlcNAc...) (Potential). 
CARBOHYD   895    895        N-linked (GlcNAc...) (Potential). 
CARBOHYD   931    931        N-linked (GlcNAc...) (Potential). 
CARBOHYD   956    956        N-linked (GlcNAc...) (Potential). 
CARBOHYD   957    957        N-linked (GlcNAc...) (Potential). 
DISULFID   50    100        By similarity. 
DISULFID   144    196        By similarity. 
DISULFID   249    297        By similarity. 
DISULFID   339    386        By similarity. 
DISULFID   431    479        By similarity. 
DISULFID   521    577        By similarity. 
VAR_SEQ   62     78        Missing (in isoform 2). VSP_011968
CONFLICT   262    262        K -> R (in Ref. 1; BAA92367). 
CONFLICT   892    892        L -> P (in Ref. 1; BAA92367). 
CONFLICT   921    921        L -> V (in Ref. 1; BAA92367). 
Sequence information
Length: 1028 AA [This is the length of the unprocessed precursor] Molecular weight: 113761 Da [This is the MW of the unprocessed precursor] CRC64: B233ED300881B101 [This is a checksum on the sequence]
        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 

Q9JMB8 in FASTA format

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