CNTN1_MOUSE
ID CNTN1_MOUSE Reviewed; 1020 AA.
AC P12960; Q6NXV7; Q8BR42; Q8C6A0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Contactin-1;
DE AltName: Full=Neural cell surface protein F3;
DE Flags: Precursor;
GN Name=Cntn1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=2474555; DOI=10.1083/jcb.109.2.775;
RA Gennarini G., Cibelli G., Rougon G., Mattei M.-G., Goridis C.;
RT "The mouse neuronal cell surface protein F3: a phosphatidylinositol-
RT anchored member of the immunoglobulin superfamily related to chicken
RT contactin.";
RL J. Cell Biol. 109:775-788(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Neural stem cell;
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 PROTEIN SEQUENCE OF 79-90; 226-249; 604-613; 619-628; 759-768 AND 859-869,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-1020.
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP INTERACTION WITH TNR, AND FUNCTION.
RX PubMed=7678967; DOI=10.1016/0896-6273(93)90243-k;
RA Pesheva P., Gennarini G., Goridis C., Schachner M.;
RT "The F3/11 cell adhesion molecule mediates the repulsion of neurons by the
RT extracellular matrix glycoprotein J1-160/180.";
RL Neuron 10:69-82(1993).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH NRCAM AND PTPRB.
RX PubMed=11564762; DOI=10.1083/jcb.200104122;
RA Sakurai T., Lustig M., Babiarz J., Furley A.J., Tait S., Brophy P.J.,
RA Brown S.A., Brown L.Y., Mason C.A., Grumet M.;
RT "Overlapping functions of the cell adhesion molecules Nr-CAM and L1 in
RT cerebellar granule cell development.";
RL J. Cell Biol. 154:1259-1273(2001).
RN [7]
RP FUNCTION.
RX PubMed=11395001; DOI=10.1016/s0896-6273(01)00296-3;
RA Boyle M.E., Berglund E.O., Murai K.K., Weber L., Peles E., Ranscht B.;
RT "Contactin orchestrates assembly of the septate-like junctions at the
RT paranode in myelinated peripheral nerve.";
RL Neuron 30:385-397(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH NOTCH1.
RX PubMed=14567914; DOI=10.1016/s0092-8674(03)00810-9;
RA Hu Q.-D., Ang B.-T., Karsak M., Hu W.-P., Cui X.-Y., Duka T., Takeda Y.,
RA Chia W., Sankar N., Ng Y.-K., Ling E.-A., Maciag T., Small D.,
RA Trifonova R., Kopan R., Okano H., Nakafuku M., Chiba S., Hirai H.,
RA Aster J.C., Schachner M., Pallen C.J., Watanabe K., Xiao Z.-C.;
RT "F3/contactin acts as a functional ligand for Notch during oligodendrocyte
RT maturation.";
RL Cell 115:163-175(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH PTPRZ1.
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 [11]
RP INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
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:11395001, ECO:0000269|PubMed:14567914,
CC ECO:0000269|PubMed:7678967}.
CC -!- SUBUNIT: Monomer. Interacts with CNTNAP1 in cis form (By similarity).
CC Binds to the carbonic-anhydrase like domain of PTPRZ1
CC (PubMed:20133774). Interacts with NOTCH1 and TNR (PubMed:7678967,
CC PubMed:14567914). Detected in a complex with NRCAM and PTPRB
CC (PubMed:11564762). Interacts with TASOR (PubMed:31112734).
CC {ECO:0000250|UniProtKB:Q12860, ECO:0000250|UniProtKB:Q63198,
CC ECO:0000269|PubMed:14567914, ECO:0000269|PubMed:20133774,
CC ECO:0000269|PubMed:31112734, ECO:0000269|PubMed:7678967}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Expressed in the ovary and in Sertoli cells of the
CC testis. {ECO:0000269|PubMed:31112734}.
CC -!- MISCELLANEOUS: F3 shares with L1, N-CAM, MAG, and other cell adhesion
CC molecules from nervous tissue the L2/HNK-1 carbohydrate epitope.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; X14943; CAA33075.1; -; mRNA.
DR EMBL; BC066864; AAH66864.1; -; mRNA.
DR EMBL; AK045710; BAC32466.1; -; mRNA.
DR EMBL; AK076273; BAC36282.1; -; mRNA.
DR CCDS; CCDS27763.1; -.
DR PIR; S05944; S05944.
DR RefSeq; NP_001153119.1; NM_001159647.1.
DR RefSeq; NP_001153120.1; NM_001159648.1.
DR RefSeq; NP_031753.1; NM_007727.2.
DR RefSeq; XP_017171911.1; XM_017316422.1.
DR AlphaFoldDB; P12960; -.
DR SMR; P12960; -.
DR BioGRID; 198797; 25.
DR IntAct; P12960; 10.
DR MINT; P12960; -.
DR STRING; 10090.ENSMUSP00000000109; -.
DR GlyConnect; 2224; 19 N-Linked glycans (8 sites).
DR GlyGen; P12960; 9 sites, 19 N-linked glycans (8 sites).
DR iPTMnet; P12960; -.
DR PhosphoSitePlus; P12960; -.
DR SwissPalm; P12960; -.
DR CPTAC; non-CPTAC-3642; -.
DR MaxQB; P12960; -.
DR PaxDb; P12960; -.
DR PeptideAtlas; P12960; -.
DR PRIDE; P12960; -.
DR ProteomicsDB; 285524; -.
DR ABCD; P12960; 1 sequenced antibody.
DR Antibodypedia; 25021; 344 antibodies from 40 providers.
DR DNASU; 12805; -.
DR Ensembl; ENSMUST00000000109; ENSMUSP00000000109; ENSMUSG00000055022.
DR Ensembl; ENSMUST00000068378; ENSMUSP00000067842; ENSMUSG00000055022.
DR Ensembl; ENSMUST00000169825; ENSMUSP00000133063; ENSMUSG00000055022.
DR GeneID; 12805; -.
DR KEGG; mmu:12805; -.
DR UCSC; uc007xik.2; mouse.
DR CTD; 1272; -.
DR MGI; MGI:105980; Cntn1.
DR VEuPathDB; HostDB:ENSMUSG00000055022; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000155915; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; P12960; -.
DR OMA; PNHEVRM; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; P12960; -.
DR TreeFam; TF351103; -.
DR BioGRID-ORCS; 12805; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Cntn1; mouse.
DR PRO; PR:P12960; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P12960; protein.
DR Bgee; ENSMUSG00000055022; Expressed in lateral geniculate body and 209 other tissues.
DR Genevisible; P12960; MM.
DR GO; GO:0099025; C:anchored component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IDA:MGI.
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; IGI:MGI.
DR GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IGI:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:MGI.
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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Notch signaling pathway; Reference proteome; Repeat; Signal.
FT SIGNAL 1..20
FT CHAIN 21..1001
FT /note="Contactin-1"
FT /id="PRO_0000014687"
FT PROPEP 1002..1020
FT /note="Removed in mature form"
FT /id="PRO_0000014688"
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:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000255"
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:0000255"
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"
FT CONFLICT 433
FT /note="I -> V (in Ref. 2; AAH66864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1020 AA; 113388 MW; 9DCDAA40EAA4CBC7 CRC64;
MKMPLLVSHL LLISLTSCLG DFTWHRRYGH GVSEEDKGFG PIFEEQPINT IYPEESLEGK
VSLNCRARAS PFPVYKWRMN NGDVDLTNDR YSMVGGNLVI NNPDKQKDAG VYYCLASNNY
GMVRSTEATL SFGYLDPFPP EERPEVKVKE GKGMVLLCDP PYHFPDDLSY RWLLNEFPVF
ITMDKRRFVS QTNGNLYIAN VESSDRGNYS CFVSSPSITK SVFSKFIPLI PIPERTTKPY
PADIVVQFKD IYTMMGQNVT LECFALGNPV PDIRWRKVLE PMPSTAEIST SGAVLKIFNI
QLEDEGLYEC EAENIRGKDK HQARIYVQAF PEWVEHINDT EVDIGSDLYW PCIATGKPIP
TIRWLKNGYS YHKGELRLYD VTFENAGMYQ CIAENAYGSI YANAELKILA LAPTFEMNPM
KKKILAAKGG RVIIECKPKA APKPKFSWSK GTEWLVNSSR ILIWEDGSLE INNITRNDGG
IYTCFAENNR GKANSTGTLV ITNPTRIILA PINADITVGE NATMQCAASF DPALDLTFVW
SFNGYVIDFN KEITHIHYQR NFMLDANGEL LIRNAQLKHA GRYTCTAQTI VDNSSASADL
VVRGPPGPPG GLRIEDIRAT SVALTWSRGS DNHSPISKYT IQTKTILSDD WKDAKTDPPI
IEGNMESAKA VDLIPWMEYE FRVVATNTLG TGEPSIPSNR IKTDGAAPNV APSDVGGGGG
TNRELTITWA PLSREYHYGN NFGYIVAFKP FDGEEWKKVT VTNPDTGRYV HKDETMTPST
AFQVKVKAFN NKGDGPYSLV AVINSAQDAP SEAPTEVGVK VLSSSEISVH WKHVLEKIVE
SYQIRYWAGH DKEAAAHRVQ VTSQEYSARL ENLLPDTQYF IEVGACNSAG CGPSSDVIET
FTRKAPPSQP PRIISSVRSG SRYIITWDHV VALSNESTVT GYKILYRPDG QHDGKLFSTH
KHSIEVPIPR DGEYVVEVRA HSDGGDGVVS QVKISGVSTL SSSLLSLLLP SLGFLVYSEF
