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UniProtKB/Swiss-Prot entry Q02246


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CNTN2_HUMAN
Primary accession number Q02246
Secondary accession numbers P78432 Q5T054
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 92)
Name and origin of the protein
Protein name Contactin-2 [Precursor]
Synonyms Axonin-1
Axonal glycoprotein TAG-1
Transient axonal glycoprotein 1
TAX-1
Gene name
Name: CNTN2
Synonyms: AXT, TAG1, TAX1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8425542 [NCBI, ExPASy, EBI, Israel, Japan]
Hasler T.H., Rader C., Stoeckli E.T., Zuellig R.A., Sonderegger P.;
"cDNA cloning, structural features, and eucaryotic expression of human TAG-1/axonin-1.";
Eur. J. Biochem. 211:329-339(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1016/S0888-7543(05)80357-X; PubMed=8307567 [NCBI, ExPASy, EBI, Israel, Japan]
Tsiotra C.P., Karagogeos D., Theodorakis K., Michaelidis M.T., Modi W.S., Furley J.A., Jessel M.T., Papamatheakis J.;
"Isolation of the cDNA and chromosomal localization of the gene (TAX1) encoding the human axonal glycoprotein TAG-1.";
Genomics 18:562-567(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
DOI=10.1006/geno.1995.9892; PubMed=8586412 [NCBI, ExPASy, EBI, Israel, Japan]
Kozlov S.V., Giger R.J., Hasler T., Korvatska E., Schorderet D.F., Sonderegger P.;
"The human TAX1 gene encoding the axon-associated cell adhesion molecule TAG-1/axonin-1: genomic structure and basic promoter.";
Genomics 30:141-148(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
TISSUE=Placenta;
Tsiotra C.P., Theodorakis C., Michaelidis M.T., Mamalaki C., Karagogeus D., Papamatheakis J.;
"Molecular structure and functional studies of the TAX-1 promoter.";
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 31-45.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-904, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[8]
X-RAY CRYSTALLOGRAPHY (3.07 ANGSTROMS) OF 34-414, AND DISULFIDE BONDS.
DOI=10.1110/ps.072802707; PubMed=17766378 [NCBI, ExPASy, EBI, Israel, Japan]
Mortl M., Sonderegger P., Diederichs K., Welte W.;
"The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction.";
Protein Sci. 16:2174-2183(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X68274; CAA48335.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X67734; CAA47963.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84420; CAA59137.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL583832; CAI15288.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X92681; CAA63365.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S35508; A49356.
RefSeq NP_005067.1; -.
UniGene Hs.519220
3D structure databases
PDB
2OM5; X-ray; 3.07 A; A=34-414.[ExPASy / RCSB / EBI]
PDBsum 2OM5; -.
ModBase Q02246.
Organism-specific databases
H-InvDB HIX0001506; -.
HGNC HGNC:2172; CNTN2.
GenAtlas CNTN2.
HPA HPA001397; -.
HPA012497; -.
MIM 190197; gene. [NCBI / EBI]
PharmGKB PA26686; -.
GeneCards Q02246.
Gene expression databases
ArrayExpress Q02246; -.
CleanEx HS_CNTN2; -.
GermOnline ENSG00000184144; Homo sapiens.
Ontologies
GO
GO:0031225; Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007155; Biological process: cell adhesion (non-traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR008957; Fibronectin_typ-III-like_fold.
IPR003961; FN_III.
IPR003962; FnIII_subd.
IPR013151; Ig.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR013098; Ig_I-set.
IPR003599; Ig_sub.
IPR003598; Ig_sub2.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.30; FN_III-like; 2.
G3DSA:2.60.40.10; Ig-like_fold; 5.
Pfam PF00041; fn3; 3.
PF07679; I-set; 2.
PF00047; ig; 3.
Pfam graphical view of domain structure.
PRINTS PR00014; FNTYPEIII.
SMART SM00060; FN3; 4.
SM00409; IG; 1.
SM00408; IGc2; 5.
SMART graphical view of domain structure.
PROSITE PS50853; FN3; 4.
PS50835; IG_LIKE; 6.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q02246.
ProtoNet Q02246.
Genome annotation databases
Ensembl ENSG00000184144; Homo sapiens. [Contig view]
GeneID 6900; -.
KEGG hsa:6900; -.
Phylogenomic databases
HOGENOM Q02246; -.
HOVERGEN Q02246; -.
Other
NextBio 26975; -.
SOURCE CNTN2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell adhesion; Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane; Polymorphism; Repeat; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     30  30      
CHAIN   31   1012  982     Contactin-2. PRO_0000014695
PROPEP   1013   1040  28     Removed in mature form (Potential). PRO_0000014696
DOMAIN   43    128  86     Ig-like C2-type 1. 
DOMAIN   133    222  90     Ig-like C2-type 2. 
DOMAIN   239    322  84     Ig-like C2-type 3. 
DOMAIN   327    411  85     Ig-like C2-type 4. 
DOMAIN   417    504  88     Ig-like C2-type 5. 
DOMAIN   509    603  95     Ig-like C2-type 6. 
DOMAIN   607    703  97     Fibronectin type-III 1. 
DOMAIN   710    807  98     Fibronectin type-III 2. 
DOMAIN   812    908  97     Fibronectin type-III 3. 
DOMAIN   912   1002  91     Fibronectin type-III 4. 
MOTIF   794    796  3     Cell attachment site (By similarity). 
COMPBIAS   606    612  7     Gly/Pro-rich. 
LIPID   1012   1012        GPI-anchor amidated asparagine (Potential). 
CARBOHYD   76     76        N-linked (GlcNAc...) (Potential). 
CARBOHYD   198    198        N-linked (GlcNAc...) (Potential). 
CARBOHYD   204    204        N-linked (GlcNAc...) (Potential). 
CARBOHYD   461    461        N-linked (GlcNAc...) (Potential). 
CARBOHYD   477    477        N-linked (GlcNAc...) (Potential). 
CARBOHYD   498    498        N-linked (GlcNAc...) (Potential). 
CARBOHYD   525    525        N-linked (GlcNAc...) (Potential). 
CARBOHYD   830    830        N-linked (GlcNAc...) (Potential). 
CARBOHYD   904    904        N-linked (GlcNAc...). 
CARBOHYD   918    918        N-linked (GlcNAc...) (Potential). 
CARBOHYD   940    940        N-linked (GlcNAc...) (Potential). 
DISULFID   61    111         
DISULFID   155    207         
DISULFID   261    306         
DISULFID   348    395         
VARIANT   145    145  1     A -> T (in dbSNP:rs2275697 [NCBI]). VAR_021918 [3D]
VARIANT   366    366  1     P -> L (in dbSNP:rs2229866 [NCBI]). VAR_029129 [3D]
VARIANT   657    657  1     R -> W (in dbSNP:rs2305276 [NCBI]). VAR_021919 
STRAND   35     41  7      
STRAND   46     51  6      
STRAND   55     59  5      
STRAND   62     67  6      
STRAND   70     75  6      
STRAND   87     91  5      
STRAND   94     99  6      
HELIX   102    105  4      
STRAND   107    115  9      
STRAND   118    121  4      
STRAND   125    132  8      
STRAND   151    153  3      
STRAND   160    162  3      
STRAND   165    172  8      
STRAND   180    185  6      
STRAND   187    189  3      
STRAND   192    196  5      
STRAND   203    213  11      
STRAND   216    221  6      
STRAND   225    227  3      
STRAND   229    231  3      
STRAND   237    243  7      
STRAND   247    252  6      
STRAND   257    260  4      
STRAND   262    267  6      
STRAND   270    275  6      
STRAND   289    295  7      
HELIX   298    300  3      
STRAND   302    310  9      
STRAND   313    324  12      
STRAND   329    331  3      
STRAND   336    339  4      
STRAND   344    347  4      
STRAND   352    354  3      
STRAND   357    366  10      
STRAND   373    376  4      
STRAND   379    384  6      
HELIX   387    389  3      
STRAND   391    398  8      
STRAND   403    413  11      
Sequence information
Length: 1040 AA [This is the length of the unprocessed precursor] Molecular weight: 113393 Da [This is the MW of the unprocessed precursor] CRC64: 254E78DD3C28EFB6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGTATRRKPH LLLVAAVALV SSSAWSSALG SQTTFGPVFE DQPLSVLFPE ESTEEQVLLA 

        70         80         90        100        110        120 
CRARASPPAT YRWKMNGTEM KLEPGSRHQL VGGNLVIMNP TKAQDAGVYQ CLASNPVGTV 

       130        140        150        160        170        180 
VSREAILRFG FLQEFSKEER DPVKAHEGWG VMLPCNPPAH YPGLSYRWLL NEFPNFIPTD 

       190        200        210        220        230        240 
GRHFVSQTTG NLYIARTNAS DLGNYSCLAT SHMDFSTKSV FSKFAQLNLA AEDTRLFAPS 

       250        260        270        280        290        300 
IKARFPAETY ALVGQQVTLE CFAFGNPVPR IKWRKVDGSL SPQWTTAEPT LQIPSVSFED 

       310        320        330        340        350        360 
EGTYECEAEN SKGRDTVQGR IIVQAQPEWL KVISDTEADI GSNLRWGCAA AGKPRPTVRW 

       370        380        390        400        410        420 
LRNGEPLASQ NRVEVLAGDL RFSKLSLEDS GMYQCVAENK HGTIYASAEL AVQALAPDFR 

       430        440        450        460        470        480 
LNPVRRLIPA ARGGEILIPC QPRAAPKAVV LWSKGTEILV NSSRVTVTPD GTLIIRNISR 

       490        500        510        520        530        540 
SDEGKYTCFA ENFMGKANST GILSVRDATK ITLAPSSADI NLGDNLTLQC HASHDPTMDL 

       550        560        570        580        590        600 
TFTWTLDDFP IDFDKPGGHY RRTNVKETIG DLTILNAQLR HGGKYTCMAQ TVVDSASKEA 

       610        620        630        640        650        660 
TVLVRGPPGP PGGVVVRDIG DTTIQLSWSR GFDNHSPIAK YTLQARTPPA GKWKQVRTNP 

       670        680        690        700        710        720 
ANIEGNAETA QVLGLTPWMD YEFRVIASNI LGTGEPSGPS SKIRTREAAP SVAPSGLSGG 

       730        740        750        760        770        780 
GGAPGELIVN WTPMSREYQN GDGFGYLLSF RRQGSTHWQT ARVPGADAQY FVYSNESVRP 

       790        800        810        820        830        840 
YTPFEVKIRS YNRRGDGPES LTALVYSAEE EPRVAPTKVW AKGVSSSEMN VTWEPVQQDM 

       850        860        870        880        890        900 
NGILLGYEIR YWKAGDKEAA ADRVRTAGLD TSARVSGLHP NTKYHVTVRA YNRAGTGPAS 

       910        920        930        940        950        960 
PSANATTMKP PPRRPPGNIS WTFSSSSLSI KWDPVVPFRN ESAVTGYKML YQNDLHLTPT 

       970        980        990       1000       1010       1020 
LHLTGKNWIE IPVPEDIGHA LVQIRTTGPG GDGIPAEVHI VRNGGTSMMV ENMAVRPAPH 

      1030       1040 
PGTVISHSVA MLILIGSLEL 

Q02246 in FASTA format

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View entry in raw text format (no links)
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