CNTN3_MOUSE
ID CNTN3_MOUSE Reviewed; 1028 AA.
AC Q07409; G5E878;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Contactin-3;
DE AltName: Full=Brain-derived immunoglobulin superfamily protein 1;
DE Short=BIG-1;
DE AltName: Full=Plasmacytoma-associated neuronal glycoprotein;
DE Flags: Precursor;
GN Name=Cntn3; Synonyms=Pang, Pcs;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Plasmacytoma;
RX PubMed=8108413; DOI=10.1073/pnas.91.4.1337;
RA Connelly M.A., Grady R.C., Mushinski J.F., Marcu K.B.;
RT "PANG, a gene encoding a neuronal glycoprotein, is ectopically activated by
RT intracisternal A-type particle long terminal repeats in murine
RT plasmacytomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1337-1341(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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).
RN [5]
RP INTERACTION WITH PTPRG.
RX PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA Bouyain S., Watkins D.J.;
RT "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members
RT of the contactin family of neural recognition molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Has some neurite outgrowth-promoting activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain. Ectopically
CC expressed in tumors expressing endogenous intracisternal A-type
CC particles (IAPs). {ECO:0000269|PubMed:8108413}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; L01991; AAA17403.1; -; mRNA.
DR EMBL; AC114423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466523; EDK99385.1; -; Genomic_DNA.
DR CCDS; CCDS39581.1; -.
DR PIR; A53449; A53449.
DR RefSeq; NP_032805.2; NM_008779.2.
DR RefSeq; XP_006505788.1; XM_006505725.3.
DR RefSeq; XP_006505790.1; XM_006505727.3.
DR RefSeq; XP_006505791.1; XM_006505728.3.
DR RefSeq; XP_017176937.1; XM_017321448.1.
DR PDB; 5E4Q; X-ray; 2.82 A; A=604-900.
DR PDB; 5E5R; X-ray; 2.60 A; B/D=124-316.
DR PDB; 5I99; X-ray; 2.40 A; A=406-801.
DR PDBsum; 5E4Q; -.
DR PDBsum; 5E5R; -.
DR PDBsum; 5I99; -.
DR AlphaFoldDB; Q07409; -.
DR SMR; Q07409; -.
DR BioGRID; 202024; 1.
DR STRING; 10090.ENSMUSP00000032159; -.
DR GlyConnect; 2226; 4 N-Linked glycans (3 sites).
DR GlyGen; Q07409; 11 sites, 4 N-linked glycans (3 sites).
DR PhosphoSitePlus; Q07409; -.
DR PaxDb; Q07409; -.
DR PeptideAtlas; Q07409; -.
DR PRIDE; Q07409; -.
DR ProteomicsDB; 283660; -.
DR Antibodypedia; 1216; 165 antibodies from 24 providers.
DR DNASU; 18488; -.
DR Ensembl; ENSMUST00000032159; ENSMUSP00000032159; ENSMUSG00000030075.
DR Ensembl; ENSMUST00000203619; ENSMUSP00000145176; ENSMUSG00000030075.
DR GeneID; 18488; -.
DR KEGG; mmu:18488; -.
DR UCSC; uc009dch.1; mouse.
DR CTD; 5067; -.
DR MGI; MGI:99534; Cntn3.
DR VEuPathDB; HostDB:ENSMUSG00000030075; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000160282; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; Q07409; -.
DR OMA; HKLMGAR; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q07409; -.
DR TreeFam; TF351103; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 18488; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Cntn3; mouse.
DR PRO; PR:Q07409; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q07409; protein.
DR Bgee; ENSMUSG00000030075; Expressed in epithelium of cochlear duct and 127 other tissues.
DR Genevisible; Q07409; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
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 3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1002
FT /note="Contactin-3"
FT /id="PRO_0000014707"
FT PROPEP 1003..1028
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014708"
FT DOMAIN 32..117
FT /note="Ig-like C2-type 1"
FT DOMAIN 122..209
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 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"
FT CONFLICT 173
FT /note="F -> L (in Ref. 1; AAA17403)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="C -> G (in Ref. 1; AAA17403)"
FT /evidence="ECO:0000305"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5E5R"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:5E5R"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 245..255
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:5E5R"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:5E5R"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 304..315
FT /evidence="ECO:0007829|PDB:5E5R"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:5I99"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 475..483
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 486..497
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 532..537
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:5I99"
FT HELIX 545..547
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:5I99"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 573..581
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 584..595
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 602..608
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 614..619
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 628..636
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 638..642
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 647..654
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 659..664
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 670..679
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 716..720
FT /evidence="ECO:0007829|PDB:5I99"
FT HELIX 726..728
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 735..742
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 749..753
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 760..765
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 773..782
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 785..789
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 793..796
FT /evidence="ECO:0007829|PDB:5I99"
FT STRAND 810..813
FT /evidence="ECO:0007829|PDB:5E4Q"
FT STRAND 815..817
FT /evidence="ECO:0007829|PDB:5E4Q"
FT STRAND 819..822
FT /evidence="ECO:0007829|PDB:5E4Q"
FT HELIX 830..832
FT /evidence="ECO:0007829|PDB:5E4Q"
FT STRAND 837..843
FT /evidence="ECO:0007829|PDB:5E4Q"
FT STRAND 853..857
FT /evidence="ECO:0007829|PDB:5E4Q"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:5E4Q"
FT STRAND 874..883
FT /evidence="ECO:0007829|PDB:5E4Q"
FT STRAND 894..897
FT /evidence="ECO:0007829|PDB:5E4Q"
SQ SEQUENCE 1028 AA; 113232 MW; 73EBC0C7EB661078 CRC64;
MMLSWKQLIL LSFIGCLAGE LLLQGPVFIK EPSNSIFPVD SEDKKITLNC EARGNPSPHY
RWQLNGSDID TSLDHRYKLN GGNLIVINPN RNWDTGSYQC FATNSLGTIV SREAKLQFAY
LENFKTRMRS TVSVREGQGV VLLCGPPPHS GELSYAWVFN EYPSFVEEDS RRFVSQETGH
LYIAKVEPSD VGNYTCVVTS TVTNTRVLGS PTPLVLRSDG VMGEYEPKIE VQFPETLPAA
KGSTVRLECF ALGNPVPQIN WRRSDGMPFP NKIKLRKFNG MLEIQNFQQE DTGSYECIAE
NSRGKNVARG RLTYYAKPYW LQLLRDVEIA VEDSLYWECR ASGKPKPSYR WLKNGDALVL
EERIQIENGA LTITNLNVTD SGMFQCIAEN KHGLIYSSAE LKVVASAPDF SRNPMKKMVQ
VQVGSLVILD CKPRASPRAL SFWKKGDMMV REQARVSFLN DGGLKIMNVT KADAGTYTCT
AENQFGKANG TTHLVVTEPT RIILAPSNMD VAVGESVILP CQVQHDPLLD IMFAWYFNGA
LTDFKKDGSH FEKVGGSSSG DLMIRNIQLK HSGKYVCMVQ TGVDSVSSAA ELIVRGSPGP
PENVKVDEIT DTTAQLSWTE GTDSHSPVIS YAVQARTPFS VGWQSVRTVP EVIDGKTHTA
TVVELNPWVE YEFRIVASNK IGGGEPSLPS EKVRTEEAAP EIAPSEVSGG GGSRSELVIT
WDPVPEELQN GGGFGYVVAF RPLGVTTWIQ TVVTSPDNPR YVFRNESIVP FSPYEVKVGV
YNNKGEGPFS PVTTVFSAEE EPTVAPSHIS AHSLSSSEIE VSWNTIPWKL SNGHLLGYEV
RYWNNGGEEE SSRKVKVAGN QTSAVLRGLK SNLAYYTAVR AYNSAGAGPF SATVNATTKK
TPPSQPPGNV VWNATDTKVL LNWEQVKAME NESEVTGYKV FYRTSSQNNV HVLNTNKTSA
ELLLPIKEDY IIEVKATTDG GDGTSSEQIR IPRITSMDAR GSTSAISNIH PLSGYMSVLL
FFIVNALW
