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Protein

Contactin-1

Gene

Cntn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth.3 Publications

GO - Molecular functioni

  • carbohydrate binding Source: MGI
  • glycoprotein binding Source: MGI

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • cerebellum development Source: MGI
  • neuron projection development Source: MGI
  • Notch signaling pathway Source: UniProtKB-KW
  • positive regulation of gene expression Source: MGI
  • positive regulation of neuron projection development Source: MGI
  • positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
  • positive regulation of sodium ion transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Notch signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Contactin-1
Alternative name(s):
Neural cell surface protein F3
Gene namesi
Name:Cntn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:105980. Cntn1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 1001981Contactin-1PRO_0000014687Add
BLAST
Propeptidei1002 – 102019Removed in mature formPRO_0000014688Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi65 ↔ 114PROSITE-ProRule annotation
Disulfide bondi158 ↔ 211PROSITE-ProRule annotation
Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence analysis
Disulfide bondi263 ↔ 310PROSITE-ProRule annotation
Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi352 ↔ 391PROSITE-ProRule annotation
Disulfide bondi436 ↔ 484PROSITE-ProRule annotation
Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence analysis
Glycosylationi473 – 4731N-linked (GlcNAc...)Sequence analysis
Glycosylationi494 – 4941N-linked (GlcNAc...)Sequence analysis
Glycosylationi521 – 5211N-linked (GlcNAc...)Sequence analysis
Disulfide bondi526 ↔ 585PROSITE-ProRule annotation
Glycosylationi593 – 5931N-linked (GlcNAc...)Sequence analysis
Glycosylationi935 – 9351N-linked (GlcNAc...)Sequence analysis
Lipidationi1001 – 10011GPI-anchor amidated serineSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP12960.
PaxDbiP12960.
PRIDEiP12960.

PTM databases

iPTMnetiP12960.
PhosphoSiteiP12960.
SwissPalmiP12960.

Expressioni

Gene expression databases

BgeeiP12960.
CleanExiMM_CNTN1.
GenevisibleiP12960. MM.

Interactioni

Subunit structurei

Monomer. Interacts with CNTNAP1 in cis form (By similarity). Binds to the carbonic-anhydrase like domain of PTPRZ1 (PubMed:20133774). Interacts with NOTCH1 and TNR (PubMed:7678967, PubMed:14567914). Detected in a complex with NRCAM and PTPRB (PubMed:11564762).By similarity3 Publications

GO - Molecular functioni

  • glycoprotein binding Source: MGI

Protein-protein interaction databases

BioGridi198797. 2 interactions.
IntActiP12960. 7 interactions.
MINTiMINT-1177246.
STRINGi10090.ENSMUSP00000000109.

Structurei

3D structure databases

ProteinModelPortaliP12960.
SMRiP12960. Positions 133-329, 793-905.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 13191Ig-like C2-type 1Add
BLAST
Domaini137 – 22387Ig-like C2-type 2Add
BLAST
Domaini241 – 32686Ig-like C2-type 3Add
BLAST
Domaini331 – 40777Ig-like C2-type 4Add
BLAST
Domaini413 – 50088Ig-like C2-type 5Add
BLAST
Domaini504 – 603100Ig-like C2-type 6Add
BLAST
Domaini608 – 70699Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini711 – 80898Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini813 – 90896Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini909 – 100294Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi604 – 6118Gly/Pro-rich

Sequence similaritiesi

Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3513. Eukaryota.
ENOG410XSVG. LUCA.
GeneTreeiENSGT00760000118840.
HOGENOMiHOG000059617.
HOVERGENiHBG051047.
InParanoidiP12960.
KOiK06759.
OMAiFTWYRRY.
OrthoDBiEOG7J17Z5.
PhylomeDBiP12960.
TreeFamiTF351103.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR032991. Contactin-1.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
[Graphical view]
PANTHERiPTHR10489:SF531. PTHR10489:SF531. 1 hit.
PfamiPF00041. fn3. 3 hits.
PF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 4 hits.
SM00409. IG. 6 hits.
SM00408. IGc2. 5 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 6 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12960-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMPLLVSHL LLISLTSCLG DFTWHRRYGH GVSEEDKGFG PIFEEQPINT
60 70 80 90 100
IYPEESLEGK VSLNCRARAS PFPVYKWRMN NGDVDLTNDR YSMVGGNLVI
110 120 130 140 150
NNPDKQKDAG VYYCLASNNY GMVRSTEATL SFGYLDPFPP EERPEVKVKE
160 170 180 190 200
GKGMVLLCDP PYHFPDDLSY RWLLNEFPVF ITMDKRRFVS QTNGNLYIAN
210 220 230 240 250
VESSDRGNYS CFVSSPSITK SVFSKFIPLI PIPERTTKPY PADIVVQFKD
260 270 280 290 300
IYTMMGQNVT LECFALGNPV PDIRWRKVLE PMPSTAEIST SGAVLKIFNI
310 320 330 340 350
QLEDEGLYEC EAENIRGKDK HQARIYVQAF PEWVEHINDT EVDIGSDLYW
360 370 380 390 400
PCIATGKPIP TIRWLKNGYS YHKGELRLYD VTFENAGMYQ CIAENAYGSI
410 420 430 440 450
YANAELKILA LAPTFEMNPM KKKILAAKGG RVIIECKPKA APKPKFSWSK
460 470 480 490 500
GTEWLVNSSR ILIWEDGSLE INNITRNDGG IYTCFAENNR GKANSTGTLV
510 520 530 540 550
ITNPTRIILA PINADITVGE NATMQCAASF DPALDLTFVW SFNGYVIDFN
560 570 580 590 600
KEITHIHYQR NFMLDANGEL LIRNAQLKHA GRYTCTAQTI VDNSSASADL
610 620 630 640 650
VVRGPPGPPG GLRIEDIRAT SVALTWSRGS DNHSPISKYT IQTKTILSDD
660 670 680 690 700
WKDAKTDPPI IEGNMESAKA VDLIPWMEYE FRVVATNTLG TGEPSIPSNR
710 720 730 740 750
IKTDGAAPNV APSDVGGGGG TNRELTITWA PLSREYHYGN NFGYIVAFKP
760 770 780 790 800
FDGEEWKKVT VTNPDTGRYV HKDETMTPST AFQVKVKAFN NKGDGPYSLV
810 820 830 840 850
AVINSAQDAP SEAPTEVGVK VLSSSEISVH WKHVLEKIVE SYQIRYWAGH
860 870 880 890 900
DKEAAAHRVQ VTSQEYSARL ENLLPDTQYF IEVGACNSAG CGPSSDVIET
910 920 930 940 950
FTRKAPPSQP PRIISSVRSG SRYIITWDHV VALSNESTVT GYKILYRPDG
960 970 980 990 1000
QHDGKLFSTH KHSIEVPIPR DGEYVVEVRA HSDGGDGVVS QVKISGVSTL
1010 1020
SSSLLSLLLP SLGFLVYSEF
Length:1,020
Mass (Da):113,388
Last modified:January 1, 1990 - v1
Checksum:i9DCDAA40EAA4CBC7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti433 – 4331I → V in AAH66864 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14943 mRNA. Translation: CAA33075.1.
BC066864 mRNA. Translation: AAH66864.1.
AK045710 mRNA. Translation: BAC32466.1.
AK076273 mRNA. Translation: BAC36282.1.
CCDSiCCDS27763.1.
PIRiS05944.
RefSeqiNP_001153119.1. NM_001159647.1.
NP_001153120.1. NM_001159648.1.
NP_031753.1. NM_007727.2.
UniGeneiMm.470343.
Mm.4911.

Genome annotation databases

EnsembliENSMUST00000000109; ENSMUSP00000000109; ENSMUSG00000055022.
ENSMUST00000068378; ENSMUSP00000067842; ENSMUSG00000055022.
ENSMUST00000169825; ENSMUSP00000133063; ENSMUSG00000055022.
GeneIDi12805.
KEGGimmu:12805.
UCSCiuc007xik.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14943 mRNA. Translation: CAA33075.1.
BC066864 mRNA. Translation: AAH66864.1.
AK045710 mRNA. Translation: BAC32466.1.
AK076273 mRNA. Translation: BAC36282.1.
CCDSiCCDS27763.1.
PIRiS05944.
RefSeqiNP_001153119.1. NM_001159647.1.
NP_001153120.1. NM_001159648.1.
NP_031753.1. NM_007727.2.
UniGeneiMm.470343.
Mm.4911.

3D structure databases

ProteinModelPortaliP12960.
SMRiP12960. Positions 133-329, 793-905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198797. 2 interactions.
IntActiP12960. 7 interactions.
MINTiMINT-1177246.
STRINGi10090.ENSMUSP00000000109.

PTM databases

iPTMnetiP12960.
PhosphoSiteiP12960.
SwissPalmiP12960.

Proteomic databases

MaxQBiP12960.
PaxDbiP12960.
PRIDEiP12960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000109; ENSMUSP00000000109; ENSMUSG00000055022.
ENSMUST00000068378; ENSMUSP00000067842; ENSMUSG00000055022.
ENSMUST00000169825; ENSMUSP00000133063; ENSMUSG00000055022.
GeneIDi12805.
KEGGimmu:12805.
UCSCiuc007xik.2. mouse.

Organism-specific databases

CTDi1272.
MGIiMGI:105980. Cntn1.

Phylogenomic databases

eggNOGiKOG3513. Eukaryota.
ENOG410XSVG. LUCA.
GeneTreeiENSGT00760000118840.
HOGENOMiHOG000059617.
HOVERGENiHBG051047.
InParanoidiP12960.
KOiK06759.
OMAiFTWYRRY.
OrthoDBiEOG7J17Z5.
PhylomeDBiP12960.
TreeFamiTF351103.

Miscellaneous databases

NextBioi282242.
PROiP12960.
SOURCEiSearch...

Gene expression databases

BgeeiP12960.
CleanExiMM_CNTN1.
GenevisibleiP12960. MM.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
InterProiIPR032991. Contactin-1.
IPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
[Graphical view]
PANTHERiPTHR10489:SF531. PTHR10489:SF531. 1 hit.
PfamiPF00041. fn3. 3 hits.
PF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 4 hits.
SM00409. IG. 6 hits.
SM00408. IGc2. 5 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 6 hits.
SSF49265. SSF49265. 2 hits.
PROSITEiPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse neuronal cell surface protein F3: a phosphatidylinositol-anchored member of the immunoglobulin superfamily related to chicken contactin."
    Gennarini G., Cibelli G., Rougon G., Mattei M.-G., Goridis C.
    J. Cell Biol. 109:775-788(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: CD-1.
    Tissue: Neural stem cell.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 79-90; 226-249; 604-613; 619-628; 759-768 AND 859-869, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-1020.
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina and Skin.
  5. "The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180."
    Pesheva P., Gennarini G., Goridis C., Schachner M.
    Neuron 10:69-82(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNR, FUNCTION.
  6. "Overlapping functions of the cell adhesion molecules Nr-CAM and L1 in cerebellar granule cell development."
    Sakurai T., Lustig M., Babiarz J., Furley A.J., Tait S., Brophy P.J., Brown S.A., Brown L.Y., Mason C.A., Grumet M.
    J. Cell Biol. 154:1259-1273(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. "Contactin orchestrates assembly of the septate-like junctions at the paranode in myelinated peripheral nerve."
    Boyle M.E., Berglund E.O., Murai K.K., Weber L., Peles E., Ranscht B.
    Neuron 30:385-397(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: FUNCTION, INTERACTION WITH NOTCH1.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members of the contactin family of neural recognition molecules."
    Bouyain S., Watkins D.J.
    Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPRZ1.

Entry informationi

Entry nameiCNTN1_MOUSE
AccessioniPrimary (citable) accession number: P12960
Secondary accession number(s): Q6NXV7, Q8BR42, Q8C6A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 11, 2016
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

F3 shares with L1, N-CAM, MAG, and other cell adhesion molecules from nervous tissue the L2/HNK-1 carbohydrate epitope.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.