CNTN6_RAT
ID CNTN6_RAT Reviewed; 1028 AA.
AC P97528;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Contactin-6;
DE AltName: Full=Neural recognition molecule NB-3;
DE Flags: Precursor;
GN Name=Cntn6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8945756; DOI=10.1016/s0304-3940(96)13156-6;
RA Ogawa J., Kaneko H., Masuda T., Nagata S., Hosoya H., Watanabe K.;
RT "Novel neural adhesion molecules in the contactin/F3 subgroup of the
RT immunoglobulin superfamily: isolation and characterization of cDNAs from
RT rat brain.";
RL Neurosci. Lett. 218:173-176(1996).
RN [2]
RP ERRATUM OF PUBMED:8945756.
RA Ogawa J., Kaneko H., Masuda T., Nagata S., Hosoya H., Watanabe K.;
RL Neurosci. Lett. 221:221-223(1997).
RN [3]
RP GPI-ANCHOR.
RX PubMed=12884264; DOI=10.1002/neu.10222;
RA Takeda Y., Akasaka K., Lee S., Kobayashi S., Kawano H., Murayama S.,
RA Takahashi N., Hashimoto K., Kano M., Asano M., Sudo K., Iwakura Y.,
RA Watanabe K.;
RT "Impaired motor coordination in mice lacking neural recognition molecule
RT NB-3 of the contactin/F3 subgroup.";
RL J. Neurobiol. 56:252-265(2003).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP NOTCH1.
RX PubMed=15082708; DOI=10.1074/jbc.m313505200;
RA Cui X.-Y., Hu Q.-D., Tekaya M., Shimoda Y., Ang B.-T., Nie D.-Y., Sun L.,
RA Hu W.-P., Karsak M., Duka T., Takeda Y., Ou L.-Y., Dawe G.S., Yu F.-G.,
RA Ahmed S., Jin L.-H., Schachner M., Watanabe K., Arsenijevic Y., Xiao Z.-C.;
RT "NB-3/Notch1 pathway via Deltex1 promotes neural progenitor cell
RT differentiation into oligodendrocytes.";
RL J. Biol. Chem. 279:25858-25865(2004).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Participates in oligodendrocytes generation by
CC acting as a ligand of NOTCH1. Its association with NOTCH1 promotes
CC NOTCH1 activation through the released notch intracellular domain
CC (NICD) and subsequent translocation to the nucleus. May be involved in
CC motor coordination. {ECO:0000269|PubMed:15082708}.
CC -!- SUBUNIT: Interacts with PTPRG. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Specifically expressed in neuronal cells. In brain,
CC it is expressed in spinal cord, cerebrum and cerebellum. At E17, it is
CC expressed hippocampus, cerebellum, and the brain stem. Strongly
CC expressed after birth with a maximum level between postnatal day 1 and
CC 21, which corresponds to the time frame of oligodendrogliogenesis.
CC {ECO:0000269|PubMed:15082708, ECO:0000269|PubMed:8945756}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low level during embryogenesis.
CC Highly expressed after birth. {ECO:0000269|PubMed:15082708}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D87248; BAA13320.1; -; mRNA.
DR RefSeq; NP_037357.1; NM_013225.1.
DR AlphaFoldDB; P97528; -.
DR SMR; P97528; -.
DR STRING; 10116.ENSRNOP00000047690; -.
DR GlyGen; P97528; 13 sites.
DR PaxDb; P97528; -.
DR PRIDE; P97528; -.
DR Ensembl; ENSRNOT00000051645; ENSRNOP00000047690; ENSRNOG00000032517.
DR GeneID; 27256; -.
DR KEGG; rno:27256; -.
DR CTD; 27255; -.
DR RGD; 62008; Cntn6.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000160606; -.
DR InParanoid; P97528; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; P97528; -.
DR PRO; PR:P97528; -.
DR Proteomes; UP000002494; Chromosome 4.
DR GO; GO:0046658; C:anchored component of plasma membrane; TAS:RGD.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; TAS:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:RGD.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 3.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Notch signaling pathway;
KW Phosphoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..999
FT /note="Contactin-6"
FT /id="PRO_0000014731"
FT PROPEP 1000..1028
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014732"
FT DOMAIN 32..117
FT /note="Ig-like C2-type 1"
FT DOMAIN 122..208
FT /note="Ig-like C2-type 2"
FT DOMAIN 227..308
FT /note="Ig-like C2-type 3"
FT DOMAIN 318..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 408..495
FT /note="Ig-like C2-type 5"
FT DOMAIN 499..587
FT /note="Ig-like C2-type 6"
FT DOMAIN 600..698
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 703..800
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 805..901
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 902..996
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 887..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 882
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ52"
FT LIPID 999
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 249..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 339..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 431..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 521..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1028 AA; 114065 MW; 47EFD8A370CF4923 CRC64;
MRLLWKLVIL LPLINSCAGE SRFTRPIFIQ EPQDVIFPLD LSRSEIILSC TASGYPSPHY
RWKQNGTDID FSMTYHYRLD GGSLAISSPR TDQDIGIYQC LATNPVGTIL SRKAKLQFAY
IEDFETKSRS TVSVREGQGV VLLCGPPPHF GELSYDWTFN DNPLYVQEDK RRFVSQNTGN
LYIAKVEPSD VGNYTCFVTN KEAHRSVQGP PTPLVQRTDG VMGEYEPKIE VRFPETIQAA
KDSSVKLECF ALGNPVPDIS WRRLDGSPMP GKVKYSNSQA TLEIPKFQQE DEGFYECVAG
NLRGRNLAKG QLIFYAPPEW EQKIQNTYLS IYDSLFWECK ASGNPNPSYT WLKNGERLNT
EERIQTENGT LIITMLNVSD SGIYQCAAEN KYQTIYANAE LRVLASAPDF SKNPIKKISV
VQVGGDISIE CKPNAFPKAS ISWKRGTENL KQSKRVFFLE DGSLKICNVT RSDAGSYTCV
ATNQFGNGKS SGSLIVKERT VITVPPSKMD VTVGESIVLP CQVSHDPTME VLFVWYFNGD
VIDLKKGVAH FERIGGESVG DLMIRNIQLG HSGKYLCTVQ TTLERLSAVA DIIVRGPPGP
PEDVKVEHIS STTSQLSWRP GPDNNSPIQI FTIQTRTPFS VGWQAVATVP EILNGQTYNA
TVIGLSPWVE YEFRVVAGNN IGIGEPSKPS ELLRTKASIP NVAPVNINGG GGSRSELVIT
WEPIPEELQN GEGFGYIIMF RPVGSTTWMK EKVALVESSK FIYRNESIMP LSPFEVKVGV
YNNEGEGSLS TVSIVYSGED EPRLAPRGTS VQSFSASDME VSWNAIAWNR NTGRVLGYEV
LYWTDNSKES MIGKIRVSGN VTTKNITGLR ANTIYFASVR AYNTAGTGPS SPPVNVTTKK
SPPSQPPANI AWKLSNSKLC LNWEHVKTME NESEVLGYKI LYRQNRQSKT HVLETNNTSA
ELLVPFEEDY LIEIRTVSDG GDGSSSEEIR IPKMSSLSSV GVQILKPSTQ FLTMVGFFYC
FVIQPLSR
