CNTN6_HUMAN
ID CNTN6_HUMAN Reviewed; 1028 AA.
AC Q9UQ52; Q2KHM2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Contactin-6;
DE AltName: Full=Neural recognition molecule NB-3;
DE Short=hNB-3;
DE Flags: Precursor;
GN Name=CNTN6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RX PubMed=9486763;
RX DOI=10.1002/(sici)1097-4547(19980201)51:3<275::aid-jnr1>3.0.co;2-d;
RA Kamei Y., Tsutsumi O., Taketani Y., Watanabe K.;
RT "cDNA cloning and chromosomal localization of neural adhesion molecule, NB-
RT 3 in human.";
RL J. Neurosci. Res. 51:275-283(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-882, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [4]
RP INTERACTION WITH PTPRG.
RX PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA Bouyain S., Watkins D.J.;
RT "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members
RT of the contactin family of neural recognition molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
RN [5]
RP VARIANTS [LARGE SCALE ANALYSIS] ALA-108 AND CYS-585.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [6]
RP VARIANTS GLN-303; VAL-314 AND VAL-954.
RX PubMed=21220648; DOI=10.1001/archneurol.2010.351;
RA Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D.,
RA Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A.,
RA Rouleau G.A.;
RT "Resequencing of 29 candidate genes in patients with familial and sporadic
RT amyotrophic lateral sclerosis.";
RL Arch. Neurol. 68:587-593(2011).
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. Involved in motor
CC coordination (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in nervous system. Highly expressed in
CC cerebellum. Expressed at intermediate level in thalamus, subthalamic
CC nucleus. Weakly expressed in corpus callosum, caudate nucleus and
CC spinal cord.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; AB003592; BAA82612.1; -; mRNA.
DR EMBL; BC113118; AAI13119.1; -; mRNA.
DR CCDS; CCDS2557.1; -.
DR RefSeq; NP_001276009.1; NM_001289080.1.
DR RefSeq; NP_001276010.1; NM_001289081.1.
DR RefSeq; NP_055276.1; NM_014461.3.
DR RefSeq; XP_005265115.1; XM_005265058.3.
DR RefSeq; XP_011531892.1; XM_011533590.2.
DR RefSeq; XP_016861660.1; XM_017006171.1.
DR RefSeq; XP_016861661.1; XM_017006172.1.
DR AlphaFoldDB; Q9UQ52; -.
DR SMR; Q9UQ52; -.
DR BioGRID; 118103; 3.
DR STRING; 9606.ENSP00000407822; -.
DR GlyGen; Q9UQ52; 13 sites.
DR iPTMnet; Q9UQ52; -.
DR PhosphoSitePlus; Q9UQ52; -.
DR BioMuta; CNTN6; -.
DR DMDM; 55976622; -.
DR MassIVE; Q9UQ52; -.
DR MaxQB; Q9UQ52; -.
DR PaxDb; Q9UQ52; -.
DR PeptideAtlas; Q9UQ52; -.
DR PRIDE; Q9UQ52; -.
DR ProteomicsDB; 85508; -.
DR Antibodypedia; 9868; 141 antibodies from 28 providers.
DR DNASU; 27255; -.
DR Ensembl; ENST00000350110.2; ENSP00000341882.2; ENSG00000134115.13.
DR Ensembl; ENST00000446702.7; ENSP00000407822.2; ENSG00000134115.13.
DR GeneID; 27255; -.
DR KEGG; hsa:27255; -.
DR MANE-Select; ENST00000446702.7; ENSP00000407822.2; NM_001289080.2; NP_001276009.1.
DR UCSC; uc003boz.5; human.
DR CTD; 27255; -.
DR DisGeNET; 27255; -.
DR GeneCards; CNTN6; -.
DR HGNC; HGNC:2176; CNTN6.
DR HPA; ENSG00000134115; Tissue enhanced (brain, thyroid gland).
DR MIM; 607220; gene.
DR neXtProt; NX_Q9UQ52; -.
DR OpenTargets; ENSG00000134115; -.
DR PharmGKB; PA26690; -.
DR VEuPathDB; HostDB:ENSG00000134115; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000160606; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; Q9UQ52; -.
DR OMA; LINTCAG; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q9UQ52; -.
DR TreeFam; TF351103; -.
DR PathwayCommons; Q9UQ52; -.
DR Reactome; R-HSA-447041; CHL1 interactions.
DR SignaLink; Q9UQ52; -.
DR SIGNOR; Q9UQ52; -.
DR BioGRID-ORCS; 27255; 7 hits in 1068 CRISPR screens.
DR ChiTaRS; CNTN6; human.
DR GeneWiki; CNTN6; -.
DR GenomeRNAi; 27255; -.
DR Pharos; Q9UQ52; Tbio.
DR PRO; PR:Q9UQ52; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UQ52; protein.
DR Bgee; ENSG00000134115; Expressed in cerebellar hemisphere and 121 other tissues.
DR ExpressionAtlas; Q9UQ52; baseline and differential.
DR Genevisible; Q9UQ52; HS.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
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; 2.
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_0000014727"
FT PROPEP 1000..1028
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014728"
FT DOMAIN 26..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:0007744|PubMed:19690332"
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"
FT VARIANT 108
FT /note="T -> A (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035509"
FT VARIANT 150
FT /note="F -> S (in dbSNP:rs6808056)"
FT /id="VAR_033611"
FT VARIANT 303
FT /note="R -> Q (in dbSNP:rs41293401)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065744"
FT VARIANT 314
FT /note="F -> V (in dbSNP:rs774763830)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065745"
FT VARIANT 440
FT /note="A -> S (in dbSNP:rs265771)"
FT /id="VAR_019913"
FT VARIANT 585
FT /note="S -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035510"
FT VARIANT 954
FT /note="E -> V (in a patient with amyotrophic lateral
FT sclerosis; dbSNP:rs1447631177)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065746"
SQ SEQUENCE 1028 AA; 113956 MW; 8B5A2ED2F29936A6 CRC64;
MRLLWKLVIL LPLINSSAGD GLLSRPIFTQ EPHDVIFPLD LSKSEVILNC AANGYPSPHY
RWKQNGTDID FTMSYHYRLD GGSLAINSPH TDQDIGMYQC LATNLLGTIL SRKAKLQFAY
IEDFETKTRS TVSVREGQGV VLLCGPPPHF GDLSYAWTFN DNPLYVQEDN RRFVSQETGN
LYIAKVEPSD VGNYTCFITN KEAQRSVQGP PTPLVQRTDG VMGEYEPKIE VRFPETIQAA
KDSSVKLECF ALGNPVPDIS WRRLDGSPLP GKVKYSKSQA ILEIPNFQQE DEGFYECIAS
NLRGRNLAKG QLIFYAPPEW EQKIQNTHLS IYDNLLWECK ASGKPNPWYT WLKNGERLNP
EERIQIENGT LIITMLNVSD SGVYQCAAEN KYQIIYANAE LRVLASAPDF SKSPVKKKSF
VQVGGDIVIG CKPNAFPRAA ISWKRGTETL RQSKRIFLLE DGSLKIYNIT RSDAGSYTCI
ATNQFGTAKN TGSLIVKERT VITVPPSKMD VTVGESIVLP CQVSHDPSIE VVFVWFFNGD
VIDLKKGVAH FERIGGESVG DLMIRNIQLH HSGKYLCTVQ TTLESLSAVA DIIVRGPPGP
PEDVQVEDIS STTSQLSWRA GPDNNSPIQI FTIQTRTPFS VGWQAVATVP EILNGKTYNA
TVVGLSPWVE YEFRVVAGNS IGIGEPSEPS ELLRTKASVP VVAPVNIHGG GGSRSELVIT
WESIPEELQN GEGFGYIIMF RPVGSTTWSK EKVSSVESSR FVYRNESIIP LSPFEVKVGV
YNNEGEGSLS TVTIVYSGED EPQLAPRGTS LQSFSASEME VSWNAIAWNR NTGRVLGYEV
LYWTDDSKES MIGKIRVSGN VTTKNITGLK ANTIYFASVR AYNTAGTGPS SPPVNVTTKK
SPPSQPPANI AWKLTNSKLC LNWEHVKTME NESEVLGYKI LYRQNRQSKT HILETNNTSA
ELLVPFEEDY LIEIRTVSDG GDGSSSEEIR IPKMSSLSSR GIQFLEPSTH FLSIVIVIFH
CFAIQPLI
