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Q12860 (CNTN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Contactin-1
Alternative name(s):
Glycoprotein gp135
Neural cell surface protein F3
Gene names
Name:CNTN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1018 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 By similarity.

Subunit structure

Monomer. Interacts with CNTNAP1 in cis form. Interacts with NOTCH1 and TNR By similarity. Binds to the carbonic-anhydrase like domain of PTPRZ1. Ref.5 Ref.8

Subcellular location

Isoform 1: Cell membrane; Lipid-anchorGPI-anchor; Extracellular side.

Isoform 2: Cell membrane; Lipid-anchorGPI-anchor; Extracellular side.

Tissue specificity

Strongly expressed in brain and in neuroblastoma and retinoblastoma cell lines. Lower levels of expression in lung, pancreas, kidney and skeletal muscle. Ref.1 Ref.5

Involvement in disease

Compton-North congenital myopathy (CNCM) [MIM:612540]: Familial lethal form of congenital onset muscle weakness, inherited in an autosomal-recessive fashion and characterized by a secondary loss of beta2-syntrophin and alpha-dystrobrevin from the muscle sarcolemma, central nervous system involvement, and fetal akinesia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Belongs to the immunoglobulin superfamily. Contactin family.

Contains 4 fibronectin type-III domains.

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12860-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q12860-2)

The sequence of this isoform differs from the canonical sequence as follows:
     21-31: Missing.
Isoform 3 (identifier: Q12860-3)

The sequence of this isoform differs from the canonical sequence as follows:
     603-627: PPGPPGGLRIEDIRATSVALTWSRG → KNRKGGEKNMVDSFLPVCASLPPTW
     628-1018: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.5
Chain21 – ?993973Contactin-1
PRO_0000014685
Propeptide?994 – 101825Removed in mature form
PRO_0000014686

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 – 60198Ig-like C2-type 6
Domain606 – 70499Fibronectin type-III 1
Domain709 – 80698Fibronectin type-III 2
Domain811 – 90696Fibronectin type-III 3
Domain907 – 100094Fibronectin type-III 4
Compositional bias602 – 6098Gly/Pro-rich

Amino acid modifications

Lipidation9931GPI-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...) (complex) Ref.6 Ref.7
Glycosylation5211N-linked (GlcNAc...) Potential
Glycosylation5911N-linked (GlcNAc...) Potential
Glycosylation9331N-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 ↔ 583 By similarity

Natural variations

Alternative sequence21 – 3111Missing in isoform 2.
VSP_002500
Alternative sequence603 – 62725PPGPP…TWSRG → KNRKGGEKNMVDSFLPVCAS LPPTW in isoform 3.
VSP_011959
Alternative sequence628 – 1018391Missing in isoform 3.
VSP_011960
Natural variant7941P → H in a colorectal cancer sample; somatic mutation. Ref.10
VAR_035506
Natural variant7981V → L.
Corresponds to variant rs1056020 [ dbSNP | Ensembl ].
VAR_011722
Natural variant8241E → G.
Corresponds to variant rs11553341 [ dbSNP | Ensembl ].
VAR_049866

Experimental info

Sequence conflict6821V → I AA sequence Ref.5
Sequence conflict6871L → P AA sequence Ref.5
Sequence conflict6891R → I AA sequence Ref.5
Sequence conflict6921P → F AA sequence Ref.5
Isoform 3:
Sequence conflict6101K → I in BAF82233. Ref.3

Secondary structure

............................................................ 1018
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4B8FDC5BFD434ED5

FASTA1,018113,320
        10         20         30         40         50         60 
MKMWLLVSHL VIISITTCLA EFTWYRRYGH GVSEEDKGFG PIFEEQPINT IYPEESLEGK 

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

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

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

       250        260        270        280        290        300 
PADIVVQFKD VYALMGQNVT LECFALGNPV PDIRWRKVLE PMPSTAEIST SGAVLKIFNI 

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

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

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

       490        500        510        520        530        540 
IYTCFAENNR GKANSTGTLV ITDPTRIILA PINADITVGE NATMQCAASF DPALDLTFVW 

       550        560        570        580        590        600 
SFNGYVIDFN KENIHYQRNF MLDSNGELLI RNAQLKHAGR YTCTAQTIVD NSSASADLVV 

       610        620        630        640        650        660 
RGPPGPPGGL RIEDIRATSV ALTWSRGSDN HSPISKYTIQ TKTILSDDWK DAKTDPPIIE 

       670        680        690        700        710        720 
GNMEAARAVD LIPWMEYEFR VVATNTLGRG EPSIPSNRIK TDGAAPNVAP SDVGGGGGRN 

       730        740        750        760        770        780 
RELTITWAPL SREYHYGNNF GYIVAFKPFD GEEWKKVTVT NPDTGRYVHK DETMSPSTAF 

       790        800        810        820        830        840 
QVKVKAFNNK GDGPYSLVAV INSAQDAPSE APTEVGVKVL SSSEISVHWE HVLEKIVESY 

       850        860        870        880        890        900 
QIRYWAAHDK EEAANRVQVT SQEYSARLEN LLPDTQYFIE VGACNSAGCG PPSDMIEAFT 

       910        920        930        940        950        960 
KKAPPSQPPR IISSVRSGSR YIITWDHVVA LSNESTVTGY KVLYRPDGQH DGKLYSTHKH 

       970        980        990       1000       1010 
SIEVPIPRDG EYVVEVRAHS DGGDGVVSQV KISGAPTLSP SLLGLLLPAF GILVYLEF 

« Hide

Isoform 2 [UniParc].

Checksum: 0078E9F82F498EE0
Show »

FASTA1,007111,867
Isoform 3 [UniParc].

Checksum: 86825008EAAA085A
Show »

FASTA62770,604

References

« Hide 'large scale' references
[1]"Identification and characterization of the human cell adhesion molecule contactin."
Reid R.A., Bronson D.D., Young K.M., Hemperly J.J.
Brain Res. Mol. Brain Res. 21:1-8(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Neuroblastoma.
[2]"Molecular cloning and in situ localization of the human contactin gene (CNTN1) on chromosome 12q11-q12."
Berglund E.O., Ranscht B.
Genomics 21:571-582(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Amygdala and Cerebellum.
[4]"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] (ISOFORM 3).
Tissue: Brain.
[5]"Isolation and characterization of a membrane glycoprotein from human brain with sequence similarities to cell adhesion proteins from chicken and mouse."
Berglund E., Stigbrand T., Carlsson S.R.
Eur. J. Biochem. 197:549-554(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-40 AND 679-693 (ISOFORM 1), SUBUNIT, TISSUE SPECIFICITY.
Tissue: Brain cortex.
[6]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-494.
Tissue: Plasma.
[7]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-494.
[8]"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.
[9]"Solution structures of the FN3 domain of human contactin 1."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 791-903.
[10]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-794.
[11]"Mutations in contactin-1, a neural adhesion and neuromuscular junction protein, cause a familial form of lethal congenital myopathy."
Compton A.G., Albrecht D.E., Seto J.T., Cooper S.T., Ilkovski B., Jones K.J., Challis D., Mowat D., Ranscht B., Bahlo M., Froehner S.C., North K.N.
Am. J. Hum. Genet. 83:714-724(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CNCM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21488 mRNA. Translation: CAA79696.1.
U07819 mRNA. Translation: AAA67920.1.
U07820 mRNA. Translation: AAA67921.1.
AK289544 mRNA. Translation: BAF82233.1.
AK289698 mRNA. Translation: BAF82387.1.
BC036569 mRNA. Translation: AAH36569.1.
PIRA54744.
S15394.
RefSeqNP_001242992.1. NM_001256063.1.
NP_001242993.1. NM_001256064.1.
NP_001834.2. NM_001843.3.
NP_778203.1. NM_175038.2.
XP_005268708.1. XM_005268651.1.
UniGeneHs.143434.
Hs.739161.
Hs.741112.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EE2NMR-A798-903[»]
3S97X-ray2.30C/D133-329[»]
ProteinModelPortalQ12860.
SMRQ12860. Positions 37-1001.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107672. 10 interactions.
DIPDIP-59714N.
IntActQ12860. 4 interactions.
MINTMINT-2806030.
STRING9606.ENSP00000325660.

PTM databases

PhosphoSiteQ12860.

Polymorphism databases

DMDM2497301.

Proteomic databases

PaxDbQ12860.
PRIDEQ12860.

Protocols and materials databases

DNASU1272.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347616; ENSP00000325660; ENSG00000018236. [Q12860-1]
ENST00000348761; ENSP00000261160; ENSG00000018236. [Q12860-2]
ENST00000360099; ENSP00000353213; ENSG00000018236. [Q12860-3]
ENST00000547702; ENSP00000448004; ENSG00000018236. [Q12860-3]
ENST00000547849; ENSP00000448653; ENSG00000018236. [Q12860-3]
ENST00000551295; ENSP00000447006; ENSG00000018236. [Q12860-1]
GeneID1272.
KEGGhsa:1272.
UCSCuc001rmm.2. human. [Q12860-1]
uc001rmo.4. human. [Q12860-3]
uc031qgz.1. human. [Q12860-2]

Organism-specific databases

CTD1272.
GeneCardsGC12P041086.
HGNCHGNC:2171. CNTN1.
HPACAB025200.
HPA041060.
MIM600016. gene.
612540. phenotype.
neXtProtNX_Q12860.
Orphanet210163. Congenital lethal myopathy, Compton-North type.
PharmGKBPA26685.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG293951.
HOVERGENHBG051047.
InParanoidQ12860.
KOK06759.
OMAFTWYRRY.
OrthoDBEOG7J17Z5.
PhylomeDBQ12860.
TreeFamTF351103.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkQ12860.

Gene expression databases

ArrayExpressQ12860.
BgeeQ12860.
CleanExHS_CNTN1.
GenevestigatorQ12860.

Family and domain databases

Gene3D2.60.40.10. 10 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamPF00041. fn3. 3 hits.
PF07679. I-set. 3 hits.
[Graphical view]
SMARTSM00060. FN3. 4 hits.
SM00409. IG. 2 hits.
SM00408. IGc2. 4 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ12860.
GeneWikiCNTN1.
GenomeRNAi1272.
NextBio5153.
PROQ12860.
SOURCESearch...

Entry information

Entry nameCNTN1_HUMAN
AccessionPrimary (citable) accession number: Q12860
Secondary accession number(s): A8K0H9 expand/collapse secondary AC list , A8K0Y3, Q12861, Q14030, Q7M4P0, Q8N466
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM