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Contactin-6 (Neural recognition molecule NB-3) (mNB-3)

 CNTN6_MOUSE             Reviewed;        1028 AA.
Q9JMB8; Q8C6X1;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 2.
28-FEB-2018, entry version 134.
RecName: Full=Contactin-6;
AltName: Full=Neural recognition molecule NB-3;
Short=mNB-3;
Flags: Precursor;
Name=Cntn6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=129/SvJ; TISSUE=Brain;
PubMed=10717476; DOI=10.1016/S0378-1119(00)00031-7;
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;
PubMed=16141072; DOI=10.1126/science.1112014;
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/6J; TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
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.
PubMed=12884264; DOI=10.1002/neu.10222;
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).
[5]
INTERACTION WITH PTPRG.
PubMed=20133774; DOI=10.1073/pnas.0911235107;
Bouyain S., Watkins D.J.;
"The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct
members of the contactin family of neural recognition molecules.";
Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
-!- 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.
{ECO:0000250, ECO:0000269|PubMed:12884264}.
-!- SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}.
-!- INTERACTION:
P70232:Chl1; NbExp=5; IntAct=EBI-7703151, EBI-7703109;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9JMB8-1; Sequence=Displayed;
Name=2;
IsoId=Q9JMB8-2; 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.
{ECO:0000269|PubMed:10717476}.
-!- 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.
{ECO:0000269|PubMed:10717476}.
-!- 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.
{ECO:0000269|PubMed:12884264}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
family. {ECO:0000305}.
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EMBL; AB032602; BAA92367.1; -; mRNA.
EMBL; AK052972; BAC35227.1; -; mRNA.
EMBL; BC076594; AAH76594.1; -; mRNA.
CCDS; CCDS20394.1; -. [Q9JMB8-1]
RefSeq; NP_059079.2; NM_017383.3. [Q9JMB8-1]
RefSeq; XP_006506444.1; XM_006506381.3. [Q9JMB8-1]
RefSeq; XP_006506445.1; XM_006506382.3. [Q9JMB8-1]
RefSeq; XP_006506446.1; XM_006506383.3. [Q9JMB8-1]
RefSeq; XP_006506447.1; XM_006506384.2. [Q9JMB8-2]
RefSeq; XP_017177167.1; XM_017321678.1. [Q9JMB8-1]
RefSeq; XP_017177168.1; XM_017321679.1. [Q9JMB8-1]
UniGene; Mm.321671; -.
PDB; 5E55; X-ray; 2.70 A; A/B=597-900.
PDB; 5E5U; X-ray; 2.00 A; B/D=119-316.
PDBsum; 5E55; -.
PDBsum; 5E5U; -.
ProteinModelPortal; Q9JMB8; -.
SMR; Q9JMB8; -.
IntAct; Q9JMB8; 1.
MINT; Q9JMB8; -.
STRING; 10090.ENSMUSP00000086623; -.
PhosphoSitePlus; Q9JMB8; -.
PaxDb; Q9JMB8; -.
PRIDE; Q9JMB8; -.
Ensembl; ENSMUST00000089215; ENSMUSP00000086623; ENSMUSG00000030092. [Q9JMB8-1]
Ensembl; ENSMUST00000162872; ENSMUSP00000124025; ENSMUSG00000030092. [Q9JMB8-1]
GeneID; 53870; -.
KEGG; mmu:53870; -.
UCSC; uc009dco.1; mouse. [Q9JMB8-1]
CTD; 27255; -.
MGI; MGI:1858223; Cntn6.
eggNOG; KOG3513; Eukaryota.
eggNOG; ENOG410XSVG; LUCA.
GeneTree; ENSGT00760000118840; -.
HOGENOM; HOG000059617; -.
HOVERGEN; HBG051047; -.
InParanoid; Q9JMB8; -.
KO; K06764; -.
OMA; CLNWEHV; -.
OrthoDB; EOG091G00X7; -.
PhylomeDB; Q9JMB8; -.
TreeFam; TF351103; -.
ChiTaRS; Cntn6; mouse.
PRO; PR:Q9JMB8; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030092; -.
CleanEx; MM_CNTN6; -.
ExpressionAtlas; Q9JMB8; baseline and differential.
Genevisible; Q9JMB8; MM.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005112; F:Notch binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0030182; P:neuron differentiation; IEA:InterPro.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:MGI.
CDD; cd00063; FN3; 4.
Gene3D; 2.60.40.10; -; 10.
InterPro; IPR033009; Contactin-6.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
PANTHER; PTHR43905:SF6; PTHR43905:SF6; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07679; I-set; 2.
SMART; SM00060; FN3; 4.
SMART; SM00409; IG; 6.
SMART; SM00408; IGc2; 6.
SUPFAM; SSF48726; SSF48726; 6.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 4.
PROSITE; PS50835; IG_LIKE; 6.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; GPI-anchor;
Immunoglobulin domain; Lipoprotein; Membrane; Notch signaling pathway;
Phosphoprotein; Reference proteome; Repeat; Signal.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 999 Contactin-6.
/FTId=PRO_0000014729.
PROPEP 1000 1028 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000014730.
DOMAIN 32 117 Ig-like C2-type 1.
DOMAIN 122 208 Ig-like C2-type 2.
DOMAIN 227 308 Ig-like C2-type 3.
DOMAIN 318 402 Ig-like C2-type 4.
DOMAIN 408 502 Ig-like C2-type 5.
DOMAIN 500 587 Ig-like C2-type 6.
DOMAIN 600 698 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 703 800 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 805 901 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 902 996 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOD_RES 882 882 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9UQ52}.
LIPID 999 999 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 193 193 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 377 377 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 659 659 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 765 765 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 860 860 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 865 865 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 895 895 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 931 931 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 956 956 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 957 957 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 50 100 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 144 196 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 249 297 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 339 386 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 431 479 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 521 577 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 62 78 Missing (in isoform 2).
{ECO:0000303|PubMed:10717476}.
/FTId=VSP_011968.
CONFLICT 262 262 K -> R (in Ref. 1; BAA92367).
{ECO:0000305}.
CONFLICT 892 892 L -> P (in Ref. 1; BAA92367).
{ECO:0000305}.
CONFLICT 921 921 L -> V (in Ref. 1; BAA92367).
{ECO:0000305}.
STRAND 132 134 {ECO:0000244|PDB:5E5U}.
STRAND 140 142 {ECO:0000244|PDB:5E5U}.
STRAND 148 151 {ECO:0000244|PDB:5E5U}.
STRAND 153 159 {ECO:0000244|PDB:5E5U}.
STRAND 172 174 {ECO:0000244|PDB:5E5U}.
TURN 176 178 {ECO:0000244|PDB:5E5U}.
STRAND 181 185 {ECO:0000244|PDB:5E5U}.
HELIX 188 190 {ECO:0000244|PDB:5E5U}.
STRAND 192 200 {ECO:0000244|PDB:5E5U}.
TURN 201 204 {ECO:0000244|PDB:5E5U}.
STRAND 205 208 {ECO:0000244|PDB:5E5U}.
STRAND 212 216 {ECO:0000244|PDB:5E5U}.
STRAND 225 231 {ECO:0000244|PDB:5E5U}.
STRAND 235 240 {ECO:0000244|PDB:5E5U}.
STRAND 245 248 {ECO:0000244|PDB:5E5U}.
STRAND 250 255 {ECO:0000244|PDB:5E5U}.
STRAND 258 263 {ECO:0000244|PDB:5E5U}.
STRAND 274 276 {ECO:0000244|PDB:5E5U}.
TURN 277 280 {ECO:0000244|PDB:5E5U}.
STRAND 281 284 {ECO:0000244|PDB:5E5U}.
HELIX 289 291 {ECO:0000244|PDB:5E5U}.
STRAND 293 301 {ECO:0000244|PDB:5E5U}.
STRAND 304 315 {ECO:0000244|PDB:5E5U}.
STRAND 602 609 {ECO:0000244|PDB:5E55}.
STRAND 611 619 {ECO:0000244|PDB:5E55}.
STRAND 630 636 {ECO:0000244|PDB:5E55}.
STRAND 640 642 {ECO:0000244|PDB:5E55}.
STRAND 647 654 {ECO:0000244|PDB:5E55}.
STRAND 659 663 {ECO:0000244|PDB:5E55}.
STRAND 670 678 {ECO:0000244|PDB:5E55}.
STRAND 683 686 {ECO:0000244|PDB:5E55}.
STRAND 705 709 {ECO:0000244|PDB:5E55}.
STRAND 716 722 {ECO:0000244|PDB:5E55}.
HELIX 726 728 {ECO:0000244|PDB:5E55}.
STRAND 731 733 {ECO:0000244|PDB:5E55}.
STRAND 735 742 {ECO:0000244|PDB:5E55}.
STRAND 749 755 {ECO:0000244|PDB:5E55}.
STRAND 760 764 {ECO:0000244|PDB:5E55}.
STRAND 773 782 {ECO:0000244|PDB:5E55}.
STRAND 793 796 {ECO:0000244|PDB:5E55}.
STRAND 810 812 {ECO:0000244|PDB:5E55}.
STRAND 814 817 {ECO:0000244|PDB:5E55}.
STRAND 819 822 {ECO:0000244|PDB:5E55}.
STRAND 837 845 {ECO:0000244|PDB:5E55}.
STRAND 850 858 {ECO:0000244|PDB:5E55}.
STRAND 863 866 {ECO:0000244|PDB:5E55}.
STRAND 874 883 {ECO:0000244|PDB:5E55}.
STRAND 894 897 {ECO:0000244|PDB:5E55}.
SEQUENCE 1028 AA; 113761 MW; B233ED300881B101 CRC64;
MRLLWKLVIL LPLINSCAGE GRFSRPIFIQ EPQDVIFPLD LSRSEIILTC TANGYPSPHY
RWKQNGTDID FGMTYHYRLD GGSLAISSPR TDQDIGIYQC LATNPVGTIL SRKAKLQFAY
IEDFETKTRS TVSVREGQGV VLLCGPPPHF GELSYAWTFN DSPLYVQEDK RRFVSQDTGN
LYFAKVEPSD VGNYTCFVTN KEAHRSVQGP PTPLVLRTDG VMGEYEPKIE VRFPETIQAA
KDSSIKLECF ALGNPVPDIS WKRLDGSPMP GKIKYSKSQA ILEIPKFQQE DEGFYECIAG
NLRGRNLAKG QLIFYAPPEW EQKIQNTYLS IYDSLFWECK ASGNPNPSYT WLKNGQRLNT
EERIQIENGT LIITMLNISD SGIYQCAAEN KYQTIYANAE LRVLASAPDF SKNPIKKISV
VQVGGDISIE CKPNAFPKAS ISWKRGTENL KQSKRVLFLE DGSLKICNVT RADAGSYTCV
ATNQFGNGKS SGGLVVKERT IITVPPSKMD VTVGESIVLP CQVSHDPTME VLFVWYFNGD
IIDLKKGVAH FERIGGESVG DLMIRNIQLG HSGKYLCTVQ TTLERLSAVA DIIVRGPPGP
PEDVKVEHIS STTSQLSWRP GPDNNSPIQI FTIQTRTPFS VGWQAVATVP EILNGQTYNA
TVVGLSPWVE YEFRVVAGNN IGIGEPSKPS ELLRTKASVP NVAPGNINGG GGSRSELVIT
WEAIPEELQN GEGFGYIVMF RPVGTTAWMK ERVALVESSK FIYRNESIMP LSPFEVKVGV
YNNEGEGSLS TVTIVYSGED EPQLAPRGTS VQSFSASEME VSWNAIAWNR NTGRVLGYEV
LYWTDNSKES MIGKIRVSGN VTTKNITGLR ANTIYFASVR AYNTAGTGPS SLPVNVTTKK
SPPSQPPANI AWKLSNSKLC LNWEHVKTME NESEVLGYKI LYRQNRQSKT HILETNNTSA
ELLVPFEEDY LIEIRTVSDG GDGSSSEEIR IPKMSSLSST GVQISKPSTQ SLSMVGVFYC
FAIHPLSR


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