CNTN3_RAT
ID CNTN3_RAT Reviewed; 1028 AA.
AC Q62682;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Contactin-3;
DE AltName: Full=Brain-derived immunoglobulin superfamily protein 1;
DE Short=BIG-1;
DE Flags: Precursor;
GN Name=Cntn3;
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], FUNCTION, GPI-ANCHOR, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8060619; DOI=10.1016/0896-6273(94)90357-3;
RA Yoshihara Y., Kawasaki M., Tani A., Tamada A., Nagata S., Kagamiyama H.,
RA Mori K.;
RT "BIG-1: a new TAG-1/F3-related member of the immunoglobulin superfamily
RT with neurite outgrowth-promoting activity.";
RL Neuron 13:415-426(1994).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Has some neurite outgrowth-promoting activity.
CC {ECO:0000269|PubMed:8060619}.
CC -!- SUBUNIT: Interacts with PTPRG. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain. Not expressed in
CC peripheral tissues such as heart, lung, liver, spleen, kidney and
CC skeletal muscle. In brain, it is restricted to subsets of neurons such
CC as Purkinje cells of the cerebellum, granule cells of the dentate
CC gyrus, and neurons in the superficial layers of the cerebral cortex.
CC {ECO:0000269|PubMed:8060619}.
CC -!- DEVELOPMENTAL STAGE: Weakly or not expressed from E12 to E20. Expressed
CC at much higher level from postnatal day 2, reaching a maximum level in
CC adult brain. {ECO:0000269|PubMed:8060619}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; U11031; AAA63607.1; -; mRNA.
DR PIR; I58164; I58164.
DR RefSeq; NP_062202.1; NM_019329.2.
DR RefSeq; XP_006237030.1; XM_006236968.3.
DR AlphaFoldDB; Q62682; -.
DR SMR; Q62682; -.
DR STRING; 10116.ENSRNOP00000008221; -.
DR GlyGen; Q62682; 12 sites.
DR PaxDb; Q62682; -.
DR Ensembl; ENSRNOT00000008221; ENSRNOP00000008221; ENSRNOG00000006144.
DR GeneID; 54279; -.
DR KEGG; rno:54279; -.
DR UCSC; RGD:3253; rat.
DR CTD; 5067; -.
DR RGD; 3253; Cntn3.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000160282; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; Q62682; -.
DR OMA; HKLMGAR; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q62682; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q62682; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000006144; Expressed in frontal cortex and 4 other tissues.
DR Genevisible; Q62682; RN.
DR GO; GO:0046658; C:anchored component of plasma membrane; NAS:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; TAS:RGD.
DR GO; GO:0007399; P:nervous system development; IDA:RGD.
DR CDD; cd00063; FN3; 4.
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; 6.
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 Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1002
FT /note="Contactin-3"
FT /id="PRO_0000014709"
FT PROPEP 1003..1028
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014710"
FT DOMAIN 26..117
FT /note="Ig-like C2-type 1"
FT DOMAIN 122..208
FT /note="Ig-like C2-type 2"
FT DOMAIN 227..313
FT /note="Ig-like C2-type 3"
FT DOMAIN 318..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 408..497
FT /note="Ig-like C2-type 5"
FT DOMAIN 499..593
FT /note="Ig-like C2-type 6"
FT DOMAIN 600..698
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 703..800
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 805..901
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 902..998
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 684..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1002
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 913
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 249..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 339..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 431..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 521..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1028 AA; 112789 MW; 49A2367D3D3BC10B CRC64;
MMLSWKQLIL LSFIGCLAGE LLLQGPVFVK EPSNSIFPVG SEDKKITLNC EARGNPSPHY
RWQLNGSDID TSLDHRYKLN GGNLIVINPN RNWDTGSYQC FATNSLGTIV SREAKLQFAY
LENFKSRMRS RVSVREGQGV VLLCGPPPHS GELSYAWVFN EYPSFVEEDS RRFVSQETGH
LYIAKVEPSD VGNYTCVVTS TVTNARVLGS PTPLVLRSDG VMGEYEPKIE LQFPETLPAA
KGSTVKLECF ALGNPVPQIN WRRSDGMPFP TKIKLRKFNG VLEIPNFQQE DTGSYECIAE
NSRGKNVARG RLTYYAKPYW VQLLKDVETA VEDSLYWECR ASGKPKPSYR WLKNGDALVL
EERIQIENGA LTIANLNVSD SGMFQCIAEN KHGLIYSSAE LKVLASAPDF SRNPMKKMIQ
VQVGSLVILD CKPSASPRAL SFWKKGDTVV REQARISLLN DGGLKIMNVT KADAGIYTCI
AENQFGKANG TTQLVVTEPT RIILAPSNMD VAVGESIILP CQVQHDPLLD IMFAWYFNGT
LTDFKKDGSH FEKVGGSSSG DLMIRNIQLK HSGKYVCMVQ TGVDSVSSAA ELIVRGSPGP
PENVKVDEIT DTTAQLSWTE GTDSHSPVIS YAVQARTPFS VGWQNVRTVP EAIDGKTRTA
TVVELNPWVE YEFRVVASNK IGGGEPSLPS EKVRTEEAAP EVAPSEVSGG GGSRSELVIT
WDPVPEELQN GGGFGYVVAF RPLGVTTWIQ TVVTSPDNPR YVFRNESIVP FSPYEVKVGV
YNNKGEGPFS PVTTVFSAEE EPTVAPSHIS AHSLSSSEIE VSWNTIPWKS SNGRLLGYEV
RYWNNGGEEE SSSKVKVAGN QTSAVLRGLK SNLAYYTAVR AYNTAGAGPF SATVNATTKK
TPPSQPPGNV VWNATDTKVL LNWEQVKALE NESEVTGYKV FYRTSSQNNV QVLNTNKTSA
ELLLPIKEDY IIEVKATTDG GDGTSSEQIR IPRITSMDAR GSTSAISDIH PVSGYISVLL
FFIVNALW
