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   08-NOV-2023, entry version 186.
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; 4.
DR   STRING; 10116.ENSRNOP00000006219; -.
DR   GlyCosmos; Q63198; 9 sites, 33 glycans.
DR   GlyGen; Q63198; 9 sites, 33 N-linked glycans (5 sites).
DR   iPTMnet; Q63198; -.
DR   PhosphoSitePlus; Q63198; -.
DR   SwissPalm; Q63198; -.
DR   PaxDb; 10116-ENSRNOP00000006219; -.
DR   ABCD; Q63198; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000006219; ENSRNOP00000006219; ENSRNOG00000004438.
DR   GeneID; 117258; -.
DR   KEGG; rno:117258; -.
DR   AGR; RGD:621300; -.
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   OrthoDB; 3073820at2759; -.
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:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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; ISO:RGD.
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   CDD; cd05727; Ig2_Contactin-2-like; 1.
DR   CDD; cd05852; Ig5_Contactin-1; 1.
DR   CDD; cd04970; Ig6_Contactin; 1.
DR   CDD; cd05849; IgI_1_Contactin-1; 1.
DR   CDD; cd05851; IgI_3_Contactin-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR   InterPro; IPR047102; Contactin-1_2_Ig1.
DR   InterPro; IPR036992; Contactin-1_Ig1.
DR   InterPro; IPR047100; Contactin-1_Ig3.
DR   InterPro; IPR047101; Contactin-1_Ig6.
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; CONTACTIN-1; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13927; Ig_3; 2.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 6.
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
//