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Protein

Contactin-6

Gene

Cntn6

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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. May be involved in motor coordination.1 Publication

GO - Biological processi

  • cell adhesion Source: RGD
  • neuron differentiation Source: InterPro
  • Notch signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Notch signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Contactin-6
Alternative name(s):
Neural recognition molecule NB-3
Gene namesi
Name:Cntn6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi62008. Cntn6.

Subcellular locationi

GO - Cellular componenti

  • anchored component of plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 999980Contactin-6PRO_0000014731Add
BLAST
Propeptidei1000 – 102829Removed in mature formSequence analysisPRO_0000014732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi50 ↔ 100PROSITE-ProRule annotation
Glycosylationi65 – 651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi144 ↔ 196PROSITE-ProRule annotation
Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence analysis
Disulfide bondi249 ↔ 297PROSITE-ProRule annotation
Disulfide bondi339 ↔ 386PROSITE-ProRule annotation
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence analysis
Glycosylationi377 – 3771N-linked (GlcNAc...)Sequence analysis
Disulfide bondi431 ↔ 479PROSITE-ProRule annotation
Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence analysis
Disulfide bondi521 ↔ 577PROSITE-ProRule annotation
Glycosylationi659 – 6591N-linked (GlcNAc...)Sequence analysis
Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence analysis
Glycosylationi860 – 8601N-linked (GlcNAc...)Sequence analysis
Glycosylationi865 – 8651N-linked (GlcNAc...)Sequence analysis
Modified residuei882 – 8821PhosphotyrosineBy similarity
Glycosylationi895 – 8951N-linked (GlcNAc...)Sequence analysis
Glycosylationi931 – 9311N-linked (GlcNAc...)Sequence analysis
Glycosylationi956 – 9561N-linked (GlcNAc...)Sequence analysis
Glycosylationi957 – 9571N-linked (GlcNAc...)Sequence analysis
Lipidationi999 – 9991GPI-anchor amidated serineSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Phosphoprotein

Proteomic databases

PaxDbiP97528.
PRIDEiP97528.

Expressioni

Tissue specificityi

Specifically expressed in neuronal cells. In brain, it is expressed in spinal cord, cerebrum and cerebellum. At E17, it is expressed hippocampus, cerebellum, and the brain stem. Strongly expressed after birth with a maximum level between postnatal day 0 and 21, which corresponds to the time frame of oligodendrogliogenesis.2 Publications

Developmental stagei

Expressed at low level during embryogenesis. Highly expressed after birth.1 Publication

Interactioni

Subunit structurei

Interacts with PTPRG.By similarity

Protein-protein interaction databases

MINTiMINT-4997031.
STRINGi10116.ENSRNOP00000047690.

Structurei

3D structure databases

ProteinModelPortaliP97528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 11786Ig-like C2-type 1Add
BLAST
Domaini122 – 20887Ig-like C2-type 2Add
BLAST
Domaini227 – 30882Ig-like C2-type 3Add
BLAST
Domaini318 – 40285Ig-like C2-type 4Add
BLAST
Domaini408 – 49588Ig-like C2-type 5Add
BLAST
Domaini499 – 58789Ig-like C2-type 6Add
BLAST
Domaini600 – 69899Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini703 – 80098Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini805 – 90197Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini902 – 99695Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3513. Eukaryota.
ENOG410XSVG. LUCA.
HOGENOMiHOG000059617.
HOVERGENiHBG051047.
InParanoidiP97528.
KOiK06764.
PhylomeDBiP97528.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR033009. Contactin-6.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PANTHERiPTHR10489:SF52. PTHR10489:SF52. 1 hit.
PfamiPF00041. fn3. 2 hits.
PF07679. I-set. 2 hits.
[Graphical view]
SMARTiSM00060. FN3. 4 hits.
SM00409. IG. 6 hits.
SM00408. IGc2. 6 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 6 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P97528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLWKLVIL LPLINSCAGE SRFTRPIFIQ EPQDVIFPLD LSRSEIILSC
60 70 80 90 100
TASGYPSPHY RWKQNGTDID FSMTYHYRLD GGSLAISSPR TDQDIGIYQC
110 120 130 140 150
LATNPVGTIL SRKAKLQFAY IEDFETKSRS TVSVREGQGV VLLCGPPPHF
160 170 180 190 200
GELSYDWTFN DNPLYVQEDK RRFVSQNTGN LYIAKVEPSD VGNYTCFVTN
210 220 230 240 250
KEAHRSVQGP PTPLVQRTDG VMGEYEPKIE VRFPETIQAA KDSSVKLECF
260 270 280 290 300
ALGNPVPDIS WRRLDGSPMP GKVKYSNSQA TLEIPKFQQE DEGFYECVAG
310 320 330 340 350
NLRGRNLAKG QLIFYAPPEW EQKIQNTYLS IYDSLFWECK ASGNPNPSYT
360 370 380 390 400
WLKNGERLNT EERIQTENGT LIITMLNVSD SGIYQCAAEN KYQTIYANAE
410 420 430 440 450
LRVLASAPDF SKNPIKKISV VQVGGDISIE CKPNAFPKAS ISWKRGTENL
460 470 480 490 500
KQSKRVFFLE DGSLKICNVT RSDAGSYTCV ATNQFGNGKS SGSLIVKERT
510 520 530 540 550
VITVPPSKMD VTVGESIVLP CQVSHDPTME VLFVWYFNGD VIDLKKGVAH
560 570 580 590 600
FERIGGESVG DLMIRNIQLG HSGKYLCTVQ TTLERLSAVA DIIVRGPPGP
610 620 630 640 650
PEDVKVEHIS STTSQLSWRP GPDNNSPIQI FTIQTRTPFS VGWQAVATVP
660 670 680 690 700
EILNGQTYNA TVIGLSPWVE YEFRVVAGNN IGIGEPSKPS ELLRTKASIP
710 720 730 740 750
NVAPVNINGG GGSRSELVIT WEPIPEELQN GEGFGYIIMF RPVGSTTWMK
760 770 780 790 800
EKVALVESSK FIYRNESIMP LSPFEVKVGV YNNEGEGSLS TVSIVYSGED
810 820 830 840 850
EPRLAPRGTS VQSFSASDME VSWNAIAWNR NTGRVLGYEV LYWTDNSKES
860 870 880 890 900
MIGKIRVSGN VTTKNITGLR ANTIYFASVR AYNTAGTGPS SPPVNVTTKK
910 920 930 940 950
SPPSQPPANI AWKLSNSKLC LNWEHVKTME NESEVLGYKI LYRQNRQSKT
960 970 980 990 1000
HVLETNNTSA ELLVPFEEDY LIEIRTVSDG GDGSSSEEIR IPKMSSLSSV
1010 1020
GVQILKPSTQ FLTMVGFFYC FVIQPLSR
Length:1,028
Mass (Da):114,065
Last modified:May 1, 1997 - v1
Checksum:i47EFD8A370CF4923
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87248 mRNA. Translation: BAA13320.1.
RefSeqiNP_037357.1. NM_013225.1.
UniGeneiRn.10644.

Genome annotation databases

GeneIDi27256.
KEGGirno:27256.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87248 mRNA. Translation: BAA13320.1.
RefSeqiNP_037357.1. NM_013225.1.
UniGeneiRn.10644.

3D structure databases

ProteinModelPortaliP97528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4997031.
STRINGi10116.ENSRNOP00000047690.

Proteomic databases

PaxDbiP97528.
PRIDEiP97528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi27256.
KEGGirno:27256.

Organism-specific databases

CTDi27255.
RGDi62008. Cntn6.

Phylogenomic databases

eggNOGiKOG3513. Eukaryota.
ENOG410XSVG. LUCA.
HOGENOMiHOG000059617.
HOVERGENiHBG051047.
InParanoidiP97528.
KOiK06764.
PhylomeDBiP97528.

Miscellaneous databases

NextBioi608067.
PROiP97528.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR033009. Contactin-6.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PANTHERiPTHR10489:SF52. PTHR10489:SF52. 1 hit.
PfamiPF00041. fn3. 2 hits.
PF07679. I-set. 2 hits.
[Graphical view]
SMARTiSM00060. FN3. 4 hits.
SM00409. IG. 6 hits.
SM00408. IGc2. 6 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 6 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Novel neural adhesion molecules in the contactin/F3 subgroup of the immunoglobulin superfamily: isolation and characterization of cDNAs from rat brain."
    Ogawa J., Kaneko H., Masuda T., Nagata S., Hosoya H., Watanabe K.
    Neurosci. Lett. 218:173-176(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Wistar.
    Tissue: Brain.
  2. Erratum
    Ogawa J., Kaneko H., Masuda T., Nagata S., Hosoya H., Watanabe K.
    Neurosci. Lett. 221:221-223(1997)
  3. "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] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR.
  4. Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH NOTCH1.

Entry informationi

Entry nameiCNTN6_RAT
AccessioniPrimary (citable) accession number: P97528
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 1997
Last modified: May 11, 2016
This is version 108 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. 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.