CNTN2_RAT
ID CNTN2_RAT Reviewed; 1040 AA.
AC P22063;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 162.
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=Tax1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 31-41.
RC TISSUE=Spinal cord;
RX PubMed=2317872; DOI=10.1016/0092-8674(90)90223-2;
RA Furley A.J., Morton S.B., Manalo D., Karagogeos D., Dodd J., Jessell T.M.;
RT "The axonal glycoprotein TAG-1 is an immunoglobulin superfamily member with
RT neurite outgrowth-promoting activity.";
RL Cell 61:157-170(1990).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78; ASN-463 AND ASN-500, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: May play a role in the initial growth and guidance of axons.
CC May be involved in cell adhesion. In conjunction with another
CC transmembrane protein, CNTNAP2, contributes to the organization of
CC axonal domains at nodes of Ranvier by maintaining voltage-gated
CC potassium channels at the juxtaparanodal region (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC Note=Attached to the neuronal membrane by a GPI-anchor and is also
CC released from neurons.
CC -!- TISSUE SPECIFICITY: In neural tissues in embryos, and in adult brain,
CC spinal cord and cerebellum.
CC -!- DEVELOPMENTAL STAGE: Transiently expressed on a subset of axons in the
CC developing rat nervous system.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; M31725; AAA42201.1; -; mRNA.
DR PIR; A34695; A34695.
DR RefSeq; NP_037016.1; NM_012884.1.
DR AlphaFoldDB; P22063; -.
DR SMR; P22063; -.
DR STRING; 10116.ENSRNOP00000012190; -.
DR GlyGen; P22063; 11 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; P22063; -.
DR PhosphoSitePlus; P22063; -.
DR PaxDb; P22063; -.
DR PRIDE; P22063; -.
DR GeneID; 25356; -.
DR KEGG; rno:25356; -.
DR UCSC; RGD:3821; rat.
DR CTD; 6900; -.
DR RGD; 3821; Cntn2.
DR eggNOG; KOG3513; Eukaryota.
DR InParanoid; P22063; -.
DR PhylomeDB; P22063; -.
DR PRO; PR:P22063; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0099025; C:anchored component of postsynaptic membrane; ISO:RGD.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043194; C:axon initial segment; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0044224; C:juxtaparanode region of axon; ISO:RGD.
DR GO; GO:0043209; C:myelin sheath; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0033268; C:node of Ranvier; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; IDA:BHF-UCL.
DR GO; GO:0030246; F:carbohydrate binding; ISO:RGD.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; ISO:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007413; P:axonal fasciculation; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0022010; P:central nervous system myelination; ISO:RGD.
DR GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; ISO:RGD.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; ISO:RGD.
DR GO; GO:0071206; P:establishment of protein localization to juxtaparanode region of axon; ISO:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; ISO:RGD.
DR GO; GO:0010954; P:positive regulation of protein processing; ISO:RGD.
DR GO; GO:0097090; P:presynaptic membrane organization; ISS:UniProtKB.
DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISO:RGD.
DR GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR GO; GO:0002023; P:reduction of food intake in response to dietary excess; ISO:RGD.
DR GO; GO:0048710; P:regulation of astrocyte differentiation; ISO:RGD.
DR GO; GO:0031133; P:regulation of axon diameter; ISO:RGD.
DR GO; GO:0010769; P:regulation of cell morphogenesis involved in differentiation; ISO:RGD.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0002021; P:response to dietary excess; ISO:RGD.
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; 3.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:2317872"
FT CHAIN 31..1015
FT /note="Contactin-2"
FT /id="PRO_0000014699"
FT PROPEP 1016..1040
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014700"
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 895..921
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 1015
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
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:0007744|PubMed:24090084"
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:0007744|PubMed:24090084"
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"
SQ SEQUENCE 1040 AA; 113043 MW; 6E707EF6614CB4FB CRC64;
MGTHARKKAS LLLLVLATVA LVSSPGWSFA QGTPATFGPI FEEQPIGLLF PEESAEDQVT
LACRARASPP ATYRWKMNGT DMNLEPGSRH QLMGGNLVIM SPTKTQDAGV YQCLASNPVG
TVVSKEAVLR FGFLQEFSKE ERDPVKTHEG WGVMLPCNPP AHYPGLSYRW LLNEFPNFIP
TDGRHFVSQT TGNLYIARTN ASDLGNYSCL ATSHMDFSTK SVFSKFAQLN LAAEDPRLFA
PSIKARFPPE TYALVGQQVT LECFAFGNPV PRIKWRKVDG SLSPQWATAE PTLQIPSVSF
EDEGTYECEA ENSKGRDTVQ GRIIVQAQPE WLKVISDTEA DIGSNLRWGC AAAGKPRPMV
RWLRNGEPLA SQNRVEVLAG DLRFSKLSLE DSGMYQCVAE NKHGTIYASA ELAVQALAPD
FRQNPVRRLI PAARGGEISI LCQPRAAPKA TILWSKGTEI LGNSTRVTVT SDGTLIIRNI
SRSDEGKYTC FAENFMGKAN STGILSVRDA TKITLAPSSA DINVGDNLTL QCHASHDPTM
DLTFTWTLDD FPIDFDKPGG HYRRASAKET IGDLTILNAH VRHGGKYTCM AQTVVDGTSK
EATVLVRGPP GPPGGVVVRD IGDTTVQLSW SRGFDNHSPI AKYTLQARTP PSGKWKQVRT
NPVNIEGNAE TAQVLGLMPW MDYEFRVSAS NILGTGEPSG PSSKIRTKEA VPSVAPSGLS
GGGGAPGELI INWTPVSREY QNGDGFGYLL SFRRQGSSSW QTARVPGADA QYFVYGNDSI
QPYTPFEVKI RSYNRRGDGP ESLTALVYSA EEEPRVAPAK VWAKGSSSSE MNVSWEPVLQ
DMNGILLGYE IRYWKAGDNE AAADRVRTAG LDTSARVTGL NPNTKYHVTV RAYNRAGTGP
ASPSADAMTV KPPPRRPPGN ISWTFSSSSL SLKWDPVVPL RNESTVTGYK MLYQNDLHPT
PTLHLTSKNW IEIPVPEDIG HALVQIRTTG PGGDGIPAEV HIVRNGGTSM MVESAAARPA
HPGPAFSCMV ILMLAGYQKL
