CNTN2_MOUSE
ID CNTN2_MOUSE Reviewed; 1040 AA.
AC Q61330; Q6NZJ4; Q7TSJ5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Contactin-2;
DE AltName: Full=Axonal glycoprotein TAG-1;
DE AltName: Full=Axonin-1;
DE AltName: Full=Transient axonal glycoprotein 1;
DE Short=TAX-1;
DE Flags: Precursor;
GN Name=Cntn2; Synonyms=Tax;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 664-881.
RC STRAIN=ICR; TISSUE=Embryo;
RA Wolfer D., Giger R.J.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: In conjunction with another transmembrane protein, CNTNAP2,
CC contributes to the organization of axonal domains at nodes of Ranvier
CC by maintaining voltage-gated potassium channels at the juxtaparanodal
CC region. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Note=Attached to the neuronal membrane by a GPI-
CC anchor and is also released from neurons. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; BC066106; AAH66106.1; -; mRNA.
DR EMBL; BC053033; AAH53033.1; -; mRNA.
DR EMBL; X81365; CAA57130.1; -; mRNA.
DR CCDS; CCDS15288.1; -.
DR RefSeq; NP_796103.2; NM_177129.5.
DR RefSeq; XP_006529425.1; XM_006529362.2.
DR PDB; 5E7L; X-ray; 2.00 A; A=609-911.
DR PDBsum; 5E7L; -.
DR AlphaFoldDB; Q61330; -.
DR SMR; Q61330; -.
DR BioGRID; 203974; 11.
DR IntAct; Q61330; 2.
DR MINT; Q61330; -.
DR STRING; 10090.ENSMUSP00000083707; -.
DR GlyConnect; 2225; 6 N-Linked glycans (4 sites).
DR GlyGen; Q61330; 11 sites, 5 N-linked glycans (4 sites).
DR iPTMnet; Q61330; -.
DR PhosphoSitePlus; Q61330; -.
DR MaxQB; Q61330; -.
DR PaxDb; Q61330; -.
DR PeptideAtlas; Q61330; -.
DR PRIDE; Q61330; -.
DR ProteomicsDB; 283585; -.
DR Antibodypedia; 670; 273 antibodies from 32 providers.
DR Ensembl; ENSMUST00000086521; ENSMUSP00000083707; ENSMUSG00000053024.
DR GeneID; 21367; -.
DR KEGG; mmu:21367; -.
DR UCSC; uc007cpa.1; mouse.
DR CTD; 6900; -.
DR MGI; MGI:104518; Cntn2.
DR VEuPathDB; HostDB:ENSMUSG00000053024; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000159193; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; Q61330; -.
DR OMA; RIIIQAQ; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q61330; -.
DR TreeFam; TF351103; -.
DR BioGRID-ORCS; 21367; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Cntn2; mouse.
DR PRO; PR:Q61330; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61330; protein.
DR Bgee; ENSMUSG00000053024; Expressed in cortical plate and 109 other tissues.
DR ExpressionAtlas; Q61330; baseline and differential.
DR Genevisible; Q61330; MM.
DR GO; GO:0099025; C:anchored component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043194; C:axon initial segment; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0044224; C:juxtaparanode region of axon; IDA:BHF-UCL.
DR GO; GO:0043209; C:myelin sheath; IDA:BHF-UCL.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IDA:MGI.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; IPI:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0007413; P:axonal fasciculation; IMP:MGI.
DR GO; GO:0007409; P:axonogenesis; ISO:MGI.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
DR GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; IMP:MGI.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; IMP:BHF-UCL.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR GO; GO:0071206; P:establishment of protein localization to juxtaparanode region of axon; IDA:BHF-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IMP:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI.
DR GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; IMP:MGI.
DR GO; GO:0010954; P:positive regulation of protein processing; IDA:MGI.
DR GO; GO:0097090; P:presynaptic membrane organization; ISS:UniProtKB.
DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; IMP:BHF-UCL.
DR GO; GO:0016485; P:protein processing; IDA:MGI.
DR GO; GO:0031623; P:receptor internalization; IDA:MGI.
DR GO; GO:0002023; P:reduction of food intake in response to dietary excess; IMP:MGI.
DR GO; GO:0048710; P:regulation of astrocyte differentiation; IMP:MGI.
DR GO; GO:0031133; P:regulation of axon diameter; IMP:MGI.
DR GO; GO:0010769; P:regulation of cell morphogenesis involved in differentiation; IMP:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..1014
FT /note="Contactin-2"
FT /id="PRO_0000014697"
FT PROPEP 1015..1040
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014698"
FT DOMAIN 39..130
FT /note="Ig-like C2-type 1"
FT DOMAIN 135..224
FT /note="Ig-like C2-type 2"
FT DOMAIN 241..324
FT /note="Ig-like C2-type 3"
FT DOMAIN 329..413
FT /note="Ig-like C2-type 4"
FT DOMAIN 419..506
FT /note="Ig-like C2-type 5"
FT DOMAIN 511..605
FT /note="Ig-like C2-type 6"
FT DOMAIN 612..710
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 715..812
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 817..913
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 917..1008
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 897..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 796..798
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT LIPID 1014
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 832
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 263..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 350..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 665
FT /note="I -> M (in Ref. 2; CAA57130)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="A -> R (in Ref. 2; CAA57130)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="Y -> N (in Ref. 2; CAA57130)"
FT /evidence="ECO:0000305"
FT STRAND 614..620
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 626..631
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 642..648
FT /evidence="ECO:0007829|PDB:5E7L"
FT TURN 650..652
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 659..666
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 671..675
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 682..691
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 717..721
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 728..734
FT /evidence="ECO:0007829|PDB:5E7L"
FT HELIX 738..741
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 743..745
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 747..754
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 761..766
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 772..776
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 785..794
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 797..801
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 805..808
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 821..825
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 831..835
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 848..855
FT /evidence="ECO:0007829|PDB:5E7L"
FT HELIX 860..862
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 864..867
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 874..877
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 885..894
FT /evidence="ECO:0007829|PDB:5E7L"
FT STRAND 905..908
FT /evidence="ECO:0007829|PDB:5E7L"
SQ SEQUENCE 1040 AA; 113217 MW; 012C05DDF7F97462 CRC64;
MGAPARKRAS LLLLLLATMA LVSSPGWSFS QGTPATFGPV FEEQPVGLLF PEESAEDQVT
LACRARASPP ATYRWKMNGT EMNLEPGSRH QLMGGNLVIM SPTKAQDAGV YQCLASNPVG
TVVSKEAVLR FGFLQEFSKE ERDPVKTHEG WGVMLPCNPP AHYPGLSYRW LLNEFPNFIP
TDGRHFVSQT TGNLYIARTN ASDLGNYSCL ATSHLDFSTK SVFSKFAQLN LAAEDPRLFA
PSIKARFPPE TYALVGQQVT LECFAFGNPV PRIKWRKVDG SLSPQWGTAE PTLQIPSVSF
EDEGTYECEA ENSKGRDTVQ GRIIVQAQPE WLKVISDTEA DIGSNLRWGC AAAGKPRPMV
RWLRNGEPLA SQNRVEVLAG DLRFSKLNLE DSGMYQCVAE NKHGTIYASA ELAVQALAPD
FRQNPVRRLI PAARGGEISI PCQPRAAPKA TILWSKGTEI LGNSTRVTVT LDGTLIIRNI
SRSDEGKYTC FAENFMGKAN STGILSVRDA TKITLAPSSA DINVGDNLTL QCHASHDPTM
DLTFTWTLDD FPVDFDKPGG HYRRASVKET IGDLTILNAQ LRHGGTYTCM AQTVVDGASK
EATVLVRGPP GPPGGVVVRD IGDTTVQLSW SRGFDNHSPI AKYTLQARTP PSGKWKQVRT
NPVNIEGNAE TAQVLGLMPW MDYEFRVSAS NILGTGEPSG PSSRIRTKEA VPSVAPSGLS
GGGGAPGELT INWTPMSREY QNGDGFGYLL SFRRQGSSSW QTARVPGADT QYFVYSNDSI
HPYTPFEVKI RSYNRRGDGP ESLTAIVYSA EEEPKVAPAK VWAKGSSSSE MNVSWEPVLQ
DMNGILLGYE IRYWKAGDKE AAADRVRTAG LDSSARVTGL YPNTKYHVTV RAYNRAGTGP
ASPSADAMTM KPPPRRPPGN ISWTFSSSSL SLKWDPVVPL RNESTVTGYK MLYQNDLQPT
PMLHLTSKNW IEIPVPEDIG HALVQIRTTG PGGDGIPAEV HIVRNGGTSM MVESSAVRPA
HPGPVFSCMV ILMLAGCQRL
