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Q63198 (CNTN1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Contactin-1
Alternative name(s):
Neural cell surface protein F3
Gene names
Name:Cntn1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1021 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Subunit structure

Monomer. Interacts with NOTCH1 By similarity. Interacts with CNTNAP1 in cis form and TNR. Binds to the carbonic-anhydrase like domain of protein-tyrosine phosphatase zeta. Ref.2 Ref.3 Ref.4

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor.

Sequence similarities

Belongs to the immunoglobulin superfamily. Contactin family.

Contains 4 fibronectin type-III domains.

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 1001981Contactin-1
PRO_0000014689
Propeptide1002 – 102120Removed in mature form Potential
PRO_0000014690

Regions

Domain41 – 13191Ig-like C2-type 1
Domain137 – 22387Ig-like C2-type 2
Domain241 – 32686Ig-like C2-type 3
Domain331 – 40777Ig-like C2-type 4
Domain413 – 50088Ig-like C2-type 5
Domain504 – 603100Ig-like C2-type 6
Domain605 – 70197Fibronectin type-III 1
Domain708 – 80598Fibronectin type-III 2
Domain810 – 90192Fibronectin type-III 3
Domain906 – 99893Fibronectin type-III 4
Compositional bias604 – 6118Gly/Pro-rich

Amino acid modifications

Lipidation10011GPI-anchor amidated serine Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation3381N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation4731N-linked (GlcNAc...) Potential
Glycosylation4941N-linked (GlcNAc...) Potential
Glycosylation5211N-linked (GlcNAc...) Potential
Glycosylation5931N-linked (GlcNAc...) Potential
Glycosylation9351N-linked (GlcNAc...) Potential
Disulfide bond65 ↔ 114 By similarity
Disulfide bond158 ↔ 211 By similarity
Disulfide bond263 ↔ 310 By similarity
Disulfide bond352 ↔ 391 By similarity
Disulfide bond436 ↔ 484 By similarity
Disulfide bond526 ↔ 585 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q63198 [UniParc].

Last modified August 1, 1998. Version 2.
Checksum: FC8DC13055EE5C68

FASTA1,021113,495
        10         20         30         40         50         60 
MKTPLLVSHL LLISLTSCLG EFTWHRRYGH GVSEEDKGFG PIFEEQPINT IYPEESLEGK 

        70         80         90        100        110        120 
VSLNCRARAS PFPVYKWRMN NGDVDLTNDR YSMVGGNLVI NNPDKQKDAG IYYCLASNNY 

       130        140        150        160        170        180 
GMVRSTEATL SFGYLDPFPP EDRPEVKVKE GKGMVLLCDP PYHFPDDLSY RWLLNEFPVF 

       190        200        210        220        230        240 
ITMDKRRFVS QTNGNLYIAN VESSDRGNYS CFVSSPSITK SVFSKFIPLI PIPERTTKPY 

       250        260        270        280        290        300 
PADIVVQFKD IYTMMGQNVT LECFALGNPV PDIRWRKVLE PMPTTAEIST SGAVLKIFNI 

       310        320        330        340        350        360 
QLEDEGLYEC EAENIRGKDK HQARIYVQAF PEWVEHINDT EVDIGSDLYW PCVATGKPIP 

       370        380        390        400        410        420 
TIRWLKNGYA YHKGELRLYD VTFENAGMYQ CIAENAYGTI YANAELKILA LAPTFEMNPM 

       430        440        450        460        470        480 
KKKILAAKGG RVIIECKPKA APKPKFSWSK GTEWLVNSSR ILIWEDGSLE INNITRNDGG 

       490        500        510        520        530        540 
IYTCFAENNR GKANSTGTLV ITNPTRIILA PINADITVGE NATMQCAASF DPSLDLTFVW 

       550        560        570        580        590        600 
SFNGYVIDFN KEITNIHYQR NFMLDANGEL LIRNAQLKHA GRYTCTAQTI VDNSSASADL 

       610        620        630        640        650        660 
VVRGPPGPPG GLRIEDIRAT SVALTWSRGS DNHSPISKYT IQTKTILSDD WKDAKTDPPI 

       670        680        690        700        710        720 
IEGNMESAKA VDLIPWMEYE FRVVATNTLG TGEPSIPSNR IKTDGAAPNV APSDVGGGGG 

       730        740        750        760        770        780 
TNRELTITWA PLSREYHYGN NFGYIVAFKP FDGEEWKKVT VTNPDTGRYV HKDETMTPST 

       790        800        810        820        830        840 
AFQVKVKAFN NKGDGPYSLI AVINSAQDAP SEAPTEVGVK VLSSSEISVH WKHVLEKIVE 

       850        860        870        880        890        900 
SYQIRYWAGH DKEAAAHRVQ VTSQEYSARL ENLLPDTQYF IEVGACNSAG CGPSSDVIET 

       910        920        930        940        950        960 
FTRKAPPSQP PRIISSVRSG SRYIITWDHV VALSNESTVT GYKILYRPDG QHDGKLFSTH 

       970        980        990       1000       1010       1020 
KHSIEVPIPR DGEYVVEVRA HSDGGDGVVS QVKISGVSTL SSGLLSLLLP SLGFLVFYSE 


F 

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References

[1]"Developmental expression of the neural adhesion molecule F3 in the rat brain."
Hosoya H., Shimazaki K., Kobayashi S., Takahashi H., Shirasawa T., Takenawa T., Watanabe K.
Neurosci. Lett. 186:83-86(1995) [PubMed: 7777204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain.
[2]"The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin."
Peles E., Nativ M., Campbell P.L., Sakurai T., Martinez R., Lev S., Clary D.O., Schilling J., Barnea G., Plowman G.D., Grumet M., Schlessinger J.
Cell 82:251-260(1995) [PubMed: 7628014] [Abstract]
Cited for: INTERACTION WITH PTPRZ1.
[3]"Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11."
Xiao Z.-C., Taylor J., Montag D., Rougon G., Schachner M.
Eur. J. Neurosci. 8:766-782(1996) [PubMed: 9081628] [Abstract]
Cited for: INTERACTION WITH TNR, FUNCTION.
[4]"Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions."
Peles E., Nativ M., Lustig M., Grumet M., Schilling J., Martinez R., Plowman G.D., Schlessinger J.
EMBO J. 16:978-988(1997) [PubMed: 9118959] [Abstract]
Cited for: INTERACTION WITH CNTNAP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38492 mRNA. Translation: BAA07504.1.
IPIIPI00206054.
PIRA57112.
RefSeqNP_476459.1. NM_057118.1.
UniGeneRn.21397.

3D structure databases

ProteinModelPortalQ63198.
SMRQ63198. Positions 37-410, 793-905.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ63198.

Proteomic databases

PRIDEQ63198.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000006219; ENSRNOP00000006219; ENSRNOG00000004438.
GeneID117258.
KEGGrno:117258.
UCSCNM_057118. rat.

Organism-specific databases

CTD1272.
RGD621300. Cntn1.

Phylogenomic databases

GeneTreeENSGT00550000074380.
HOVERGENHBG051047.
InParanoidQ63198.
OMAEFTWYRR.
OrthoDBEOG4DZ1TH.
PhylomeDBQ63198.

Gene expression databases

ArrayExpressQ63198.
GenevestigatorQ63198.
GermOnlineENSRNOG00000004438. Rattus norvegicus.

Family and domain databases

InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 10 hits.
KOK06759.
PfamPF00041. fn3. 3 hits.
PF07679. I-set. 4 hits.
[Graphical view]
SMARTSM00060. FN3. 4 hits.
SM00409. IG. 2 hits.
SM00408. IGc2. 4 hits.
[Graphical view]
SUPFAMSSF49265. FN_III-like. 4 hits.
PROSITEPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio620126.

Entry information

Entry nameCNTN1_RAT
AccessionPrimary (citable) accession number: Q63198
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: August 1, 1998
Last modified: November 16, 2011
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families