Reviewed, UniProtKB/Swiss-Prot Q02246 (CNTN2_HUMAN)

Names and origin

Protein names

Recommended name:
    Contactin-2
Alternative name(s):
    Axonin-1
    Axonal glycoprotein TAG-1
    Transient axonal glycoprotein 1
      Short name=TAX-1

Gene names

Name:	CNTN2
Synonyms:	AXT, TAG1, TAX1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1040 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May play a role in the initial growth and guidance of axons. May be involved in cell adhesion.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor. Note: Attached to the neuronal membrane by a GPI-anchor and is also released from neurons.
Sequence similarities	Belongs to the immunoglobulin superfamily. Contactin family. Contains 4 fibronectin type-III domains. Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Immunoglobulin domain Repeat Signal
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular protein localization Inferred from sequence or structural similarity. Source: UniProtKB clustering of voltage-gated potassium channels Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc juxtaparanode region of axon Inferred from sequence or structural similarity. Source: UniProtKB myelin sheath Inferred from sequence or structural similarity. Source: UniProtKB node of Ranvier Inferred from sequence or structural similarity. Source: UniProtKB synapse part Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	identical protein binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Ref.6

Chain

31 – 1012

982

Contactin-2

PRO_0000014695

Propeptide

1013 – 1040

28

Removed in mature form Potential

PRO_0000014696

Regions

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

Compositional bias

606 – 612

7

Gly/Pro-rich

Amino acid modifications

Lipidation

1012

1

GPI-anchor amidated asparagine Potential

Glycosylation

76

1

N-linked (GlcNAc...) Potential

Glycosylation

198

1

N-linked (GlcNAc...) Potential

Glycosylation

204

1

N-linked (GlcNAc...) Potential

Glycosylation

461

1

N-linked (GlcNAc...) Potential

Glycosylation

477

1

N-linked (GlcNAc...) Potential

Glycosylation

498

1

N-linked (GlcNAc...) Potential

Glycosylation

525

1

N-linked (GlcNAc...) Potential

Glycosylation

830

1

N-linked (GlcNAc...) Potential

Glycosylation

904

1

N-linked (GlcNAc...) Ref.7

Glycosylation

918

1

N-linked (GlcNAc...) Potential

Glycosylation

940

1

N-linked (GlcNAc...) Potential

Disulfide bond

61 ↔ 111

Ref.8

Disulfide bond

155 ↔ 207

Ref.8

Disulfide bond

261 ↔ 306

Ref.8

Disulfide bond

348 ↔ 395

Ref.8

Natural variations

Natural variant

145

1

A → T: dbSNP rs2275697.

VAR_021918

Natural variant

366

1

P → L: dbSNP rs2229866.

VAR_029129

Natural variant

657

1

R → W: dbSNP rs2305276.

VAR_021919

Natural variant

1024

1

V → I: dbSNP rs17416074.

VAR_049867

Secondary structure

1

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1040

Helix Strand Turn

Details...

Beta strand

35 – 41

7

Beta strand

46 – 51

6

Beta strand

55 – 59

5

Beta strand

62 – 67

6

Beta strand

70 – 75

6

Beta strand

87 – 91

5

Beta strand

94 – 99

6

Helix

102 – 105

4

Beta strand

107 – 115

9

Beta strand

118 – 121

4

Beta strand

125 – 132

8

Beta strand

151 – 153

3

Beta strand

160 – 162

3

Beta strand

165 – 172

8

Beta strand

180 – 185

6

Beta strand

187 – 189

3

Beta strand

192 – 196

5

Beta strand

203 – 213

11

Beta strand

216 – 221

6

Beta strand

225 – 227

3

Beta strand

229 – 231

3

Beta strand

237 – 243

7

Beta strand

247 – 252

6

Beta strand

257 – 260

4

Beta strand

262 – 267

6

Beta strand

270 – 275

6

Beta strand

289 – 295

7

Helix

298 – 300

3

Beta strand

302 – 310

9

Beta strand

313 – 324

12

Beta strand

329 – 331

3

Beta strand

336 – 339

4

Beta strand

344 – 347

4

Beta strand

352 – 354

3

Beta strand

357 – 366

10

Beta strand

373 – 376

4

Beta strand

379 – 384

6

Helix

387 – 389

3

Beta strand

391 – 398

8

Beta strand

403 – 413

11

Sequences

	Sequence		Length	Mass (Da)
	Q02246-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 254E78DD3C28EFB6	FASTA	1,040	113,393
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, structural features, and eucaryotic expression of human TAG-1/axonin-1." Hasler T.H., Rader C., Stoeckli E.T., Zuellig R.A., Sonderegger P. Eur. J. Biochem. 211:329-339(1993) [PubMed: 8425542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Isolation of the cDNA and chromosomal localization of the gene (TAX1) encoding the human axonal glycoprotein TAG-1." Tsiotra C.P., Karagogeos D., Theodorakis K., Michaelidis M.T., Modi W.S., Furley J.A., Jessel M.T., Papamatheakis J. Genomics 18:562-567(1993) [PubMed: 8307567] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	"The human TAX1 gene encoding the axon-associated cell adhesion molecule TAG-1/axonin-1: genomic structure and basic promoter." Kozlov S.V., Giger R.J., Hasler T., Korvatska E., Schorderet D.F., Sonderegger P. Genomics 30:141-148(1995) [PubMed: 8586412] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[4]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Molecular structure and functional studies of the TAX-1 promoter." Tsiotra C.P., Theodorakis C., Michaelidis M.T., Mamalaki C., Karagogeus D., Papamatheakis J. Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136. Tissue: Placenta.
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-45.
[7]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-904, MASS SPECTROMETRY. Tissue: Plasma.
[8]	"The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction." Mortl M., Sonderegger P., Diederichs K., Welte W. Protein Sci. 16:2174-2183(2007) [PubMed: 17766378] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.07 ANGSTROMS) OF 34-414, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X68274 mRNA. Translation: CAA48335.1.
X67734 mRNA. Translation: CAA47963.1.
X84420 Genomic DNA. Translation: CAA59137.1.
AL583832 Genomic DNA. Translation: CAI15288.1.
X92681 Genomic DNA. Translation: CAA63365.1.

IPI

IPI00024966.

PIR

A49356. S35508.

RefSeq

NP_005067.1.

UniGene

Hs.519220

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OM5	X-ray	3.07	A	34-414	[»]

SMR

Q02246. Positions 54-498, 144-598, 603-811, 607-954.

ModBase

Search...

Protein-protein interaction databases

STRING

Q02246.

Proteomic databases

PRIDE

Q02246.

Genome annotation databases

Ensembl

ENST00000331830; ENSP00000330633; ENSG00000184144; Homo sapiens. [Genome view]

GeneID

6900.

KEGG

hsa:6900.

UCSC

uc001hbr.1. human.

Organism-specific databases

CTD

6900.

GeneCards

GC01P203278.

H-InvDB

HIX0001506.

HGNC

HGNC:2172. CNTN2.

HPA

HPA001397.
HPA012497.

MIM

190197. gene.

PharmGKB

PA26686.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG444805.

HOVERGEN

Q02246.

InParanoid

Q02246.

OMA

ECFAFGN.

OrthoDB

EOG9CNTB4.

PhylomeDB

Q02246.

Enzyme and pathway databases

Reactome

REACT_18266. Axon guidance.

Gene expression databases

ArrayExpress

Q02246.

Bgee

Q02246.

CleanEx

HS_CNTN2.

Genevestigator

Q02246.

GermOnline

ENSG00000184144. Homo sapiens.

Family and domain databases

InterPro

IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]

Gene3D

G3DSA:2.60.40.30. FN_III-like. 2 hits.
G3DSA:2.60.40.10. Ig-like_fold. 5 hits.

Pfam

PF00041. fn3. 3 hits.
PF07679. I-set. 5 hits.
[Graphical view]

SMART

SM00060. FN3. 4 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 5 hits.
[Graphical view]

PROSITE

PS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

26975.

SOURCE

Search...

Entry information

Entry name

CNTN2_HUMAN

Accession

Primary (citable) accession number: Q02246
Secondary accession number(s): P78432, Q5T054

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	January 19, 2010
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.