CNTN1_RAT
ID CNTN1_RAT Reviewed; 1021 AA.
AC Q63198;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Contactin-1;
DE AltName: Full=Neural cell surface protein F3;
DE Flags: Precursor;
GN Name=Cntn1;
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].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7777204; DOI=10.1016/0304-3940(95)11287-7;
RA Hosoya H., Shimazaki K., Kobayashi S., Takahashi H., Shirasawa T.,
RA Takenawa T., Watanabe K.;
RT "Developmental expression of the neural adhesion molecule F3 in the rat
RT brain.";
RL Neurosci. Lett. 186:83-86(1995).
RN [2]
RP INTERACTION WITH PTPRZ1.
RX PubMed=7628014; DOI=10.1016/0092-8674(95)90312-7;
RA Peles E., Nativ M., Campbell P.L., Sakurai T., Martinez R., Lev S.,
RA Clary D.O., Schilling J., Barnea G., Plowman G.D., Grumet M.,
RA Schlessinger J.;
RT "The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a
RT functional ligand for the axonal cell recognition molecule contactin.";
RL Cell 82:251-260(1995).
RN [3]
RP INTERACTION WITH TNR, AND FUNCTION.
RX PubMed=9081628; DOI=10.1111/j.1460-9568.1996.tb01262.x;
RA Xiao Z.-C., Taylor J., Montag D., Rougon G., Schachner M.;
RT "Distinct effects of recombinant tenascin-R domains in neuronal cell
RT functions and identification of the domain interacting with the neuronal
RT recognition molecule F3/11.";
RL Eur. J. Neurosci. 8:766-782(1996).
RN [4]
RP INTERACTION WITH CNTNAP1.
RX PubMed=9118959; DOI=10.1093/emboj/16.5.978;
RA Peles E., Nativ M., Lustig M., Grumet M., Schilling J., Martinez R.,
RA Plowman G.D., Schlessinger J.;
RT "Identification of a novel contactin-associated transmembrane receptor with
RT multiple domains implicated in protein-protein interactions.";
RL EMBO J. 16:978-988(1997).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=9396755; DOI=10.1083/jcb.139.6.1495;
RA Einheber S., Zanazzi G., Ching W., Scherer S., Milner T.A., Peles E.,
RA Salzer J.L.;
RT "The axonal membrane protein Caspr, a homologue of neurexin IV, is a
RT component of the septate-like paranodal junctions that assemble during
RT myelination.";
RL J. Cell Biol. 139:1495-1506(1997).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-338; ASN-457; ASN-494 AND
RP ASN-935, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Involved in the formation of paranodal axo-glial
CC junctions in myelinated peripheral nerves and in the signaling between
CC axons and myelinating glial cells via its association with CNTNAP1.
CC Participates in oligodendrocytes generation by acting as a ligand of
CC NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through
CC the released notch intracellular domain (NICD) and subsequent
CC translocation to the nucleus. Interaction with TNR induces a repulsion
CC of neurons and an inhibition of neurite outgrowth.
CC {ECO:0000269|PubMed:9081628}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with NOTCH1 (By
CC similarity). Interacts with CNTNAP1 in cis form and TNR
CC (PubMed:9118959, PubMed:9081628). Binds to the carbonic-anhydrase like
CC domain of PTPRZ1 (PubMed:7628014). Detected in a complex with NRCAM and
CC PTPRB (By similarity). Interacts with TASOR (By similarity).
CC {ECO:0000250|UniProtKB:P12960, ECO:0000250|UniProtKB:Q12860,
CC ECO:0000269|PubMed:7628014, ECO:0000269|PubMed:9081628,
CC ECO:0000269|PubMed:9118959}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Expressed by neurons, oligodendrocytes and their
CC progenitors (at protein level). Myelination regulates the expression
CC being down-regulated when neurons are in contact with Schwann cells.
CC {ECO:0000269|PubMed:9396755}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; D38492; BAA07504.1; -; mRNA.
DR PIR; A57112; A57112.
DR RefSeq; NP_476459.1; NM_057118.2.
DR RefSeq; XP_006242239.1; XM_006242177.3.
DR RefSeq; XP_017450105.1; XM_017594616.1.
DR AlphaFoldDB; Q63198; -.
DR SMR; Q63198; -.
DR BioGRID; 250705; 3.
DR CORUM; Q63198; -.
DR DIP; DIP-53082N; -.
DR IntAct; Q63198; 3.
DR MINT; Q63198; -.
DR STRING; 10116.ENSRNOP00000006219; -.
DR GlyGen; Q63198; 9 sites, 33 N-linked glycans (4 sites).
DR iPTMnet; Q63198; -.
DR PhosphoSitePlus; Q63198; -.
DR SwissPalm; Q63198; -.
DR PaxDb; Q63198; -.
DR PRIDE; Q63198; -.
DR ABCD; Q63198; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000006219; ENSRNOP00000006219; ENSRNOG00000004438.
DR GeneID; 117258; -.
DR KEGG; rno:117258; -.
DR CTD; 1272; -.
DR RGD; 621300; Cntn1.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000155915; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; Q63198; -.
DR OMA; PNHEVRM; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q63198; -.
DR TreeFam; TF351103; -.
DR PRO; PR:Q63198; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004438; Expressed in cerebellum and 17 other tissues.
DR Genevisible; Q63198; RN.
DR GO; GO:0099025; C:anchored component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; ISO:RGD.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; ISO:RGD.
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:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0032289; P:central nervous system myelin formation; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:RGD.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR036992; Contactin-1.
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 InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR44170:SF10; PTHR44170:SF10; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
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 Reference proteome; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1001
FT /note="Contactin-1"
FT /id="PRO_0000014689"
FT PROPEP 1002..1021
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014690"
FT DOMAIN 41..131
FT /note="Ig-like C2-type 1"
FT DOMAIN 137..223
FT /note="Ig-like C2-type 2"
FT DOMAIN 241..326
FT /note="Ig-like C2-type 3"
FT DOMAIN 331..407
FT /note="Ig-like C2-type 4"
FT DOMAIN 413..500
FT /note="Ig-like C2-type 5"
FT DOMAIN 504..603
FT /note="Ig-like C2-type 6"
FT DOMAIN 608..706
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 711..808
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 813..908
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 909..1002
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 695..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1001
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 935
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT DISULFID 65..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 263..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 436..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 526..585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1021 AA; 113495 MW; FC8DC13055EE5C68 CRC64;
MKTPLLVSHL LLISLTSCLG EFTWHRRYGH GVSEEDKGFG PIFEEQPINT IYPEESLEGK
VSLNCRARAS PFPVYKWRMN NGDVDLTNDR YSMVGGNLVI NNPDKQKDAG IYYCLASNNY
GMVRSTEATL SFGYLDPFPP EDRPEVKVKE GKGMVLLCDP PYHFPDDLSY RWLLNEFPVF
ITMDKRRFVS QTNGNLYIAN VESSDRGNYS CFVSSPSITK SVFSKFIPLI PIPERTTKPY
PADIVVQFKD IYTMMGQNVT LECFALGNPV PDIRWRKVLE PMPTTAEIST SGAVLKIFNI
QLEDEGLYEC EAENIRGKDK HQARIYVQAF PEWVEHINDT EVDIGSDLYW PCVATGKPIP
TIRWLKNGYA YHKGELRLYD VTFENAGMYQ CIAENAYGTI YANAELKILA LAPTFEMNPM
KKKILAAKGG RVIIECKPKA APKPKFSWSK GTEWLVNSSR ILIWEDGSLE INNITRNDGG
IYTCFAENNR GKANSTGTLV ITNPTRIILA PINADITVGE NATMQCAASF DPSLDLTFVW
SFNGYVIDFN KEITNIHYQR NFMLDANGEL LIRNAQLKHA GRYTCTAQTI VDNSSASADL
VVRGPPGPPG GLRIEDIRAT SVALTWSRGS DNHSPISKYT IQTKTILSDD WKDAKTDPPI
IEGNMESAKA VDLIPWMEYE FRVVATNTLG TGEPSIPSNR IKTDGAAPNV APSDVGGGGG
TNRELTITWA PLSREYHYGN NFGYIVAFKP FDGEEWKKVT VTNPDTGRYV HKDETMTPST
AFQVKVKAFN NKGDGPYSLI AVINSAQDAP SEAPTEVGVK VLSSSEISVH WKHVLEKIVE
SYQIRYWAGH DKEAAAHRVQ VTSQEYSARL ENLLPDTQYF IEVGACNSAG CGPSSDVIET
FTRKAPPSQP PRIISSVRSG SRYIITWDHV VALSNESTVT GYKILYRPDG QHDGKLFSTH
KHSIEVPIPR DGEYVVEVRA HSDGGDGVVS QVKISGVSTL SSGLLSLLLP SLGFLVFYSE
F
