CNTN5_MOUSE
ID CNTN5_MOUSE Reviewed; 1098 AA.
AC P68500; E0CYC2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Contactin-5;
DE AltName: Full=Neural recognition molecule NB-2;
DE Flags: Precursor;
GN Name=Cntn5;
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 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 [2]
RP PROTEIN SEQUENCE OF 39-48 AND 638-646, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12653969; DOI=10.1046/j.1460-9568.2003.02514.x;
RA Li H., Takeda Y., Niki H., Ogawa J., Kobayashi S., Kai N., Akasaka K.,
RA Asano M., Sudo K., Iwakura Y., Watanabe K.;
RT "Aberrant responses to acoustic stimuli in mice deficient for neural
RT recognition molecule NB-2.";
RL Eur. J. Neurosci. 17:929-936(2003).
RN [4]
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 in
CC the cerebral cortical neurons but not in hippocampal neurons (By
CC similarity). Involved in neuronal activity in the auditory system.
CC {ECO:0000250, ECO:0000269|PubMed:12653969}.
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: Expressed in the nervous system. Preferentially
CC expressed in the central auditory pathways.
CC {ECO:0000269|PubMed:12653969}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in the postnatal nervous
CC system, reaching a maximum level at 3 weeks postnatal.
CC {ECO:0000269|PubMed:12653969}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; AC100491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC102350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT033779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52722.1; -.
DR RefSeq; NP_001164258.1; NM_001170787.1.
DR RefSeq; XP_006509935.1; XM_006509872.3.
DR PDB; 5E4I; X-ray; 2.60 A; A=96-477.
DR PDB; 7MRN; X-ray; 3.50 A; A/B=669-970.
DR PDBsum; 5E4I; -.
DR PDBsum; 7MRN; -.
DR AlphaFoldDB; P68500; -.
DR SMR; P68500; -.
DR STRING; 10090.ENSMUSP00000124327; -.
DR GlyConnect; 2228; 1 N-Linked glycan (1 site).
DR GlyGen; P68500; 9 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P68500; -.
DR PhosphoSitePlus; P68500; -.
DR MaxQB; P68500; -.
DR PaxDb; P68500; -.
DR PRIDE; P68500; -.
DR ProteomicsDB; 283664; -.
DR Antibodypedia; 31696; 172 antibodies from 23 providers.
DR Ensembl; ENSMUST00000074133; ENSMUSP00000073769; ENSMUSG00000039488.
DR Ensembl; ENSMUST00000160216; ENSMUSP00000124327; ENSMUSG00000039488.
DR GeneID; 244682; -.
DR KEGG; mmu:244682; -.
DR UCSC; uc012goa.1; mouse.
DR CTD; 53942; -.
DR MGI; MGI:3042287; Cntn5.
DR VEuPathDB; HostDB:ENSMUSG00000039488; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000158183; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; P68500; -.
DR OMA; ELSLGWE; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; P68500; -.
DR TreeFam; TF351103; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 244682; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Cntn5; mouse.
DR PRO; PR:P68500; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P68500; protein.
DR Bgee; ENSMUSG00000039488; Expressed in midbrain and 32 other tissues.
DR ExpressionAtlas; P68500; baseline and differential.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR032989; Contactin-5.
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 PANTHER; PTHR44170:SF17; PTHR44170:SF17; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 4.
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; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1071
FT /note="Contactin-5"
FT /id="PRO_0000014719"
FT PROPEP 1072..1098
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014720"
FT DOMAIN 98..189
FT /note="Ig-like C2-type 1"
FT DOMAIN 195..281
FT /note="Ig-like C2-type 2"
FT DOMAIN 299..384
FT /note="Ig-like C2-type 3"
FT DOMAIN 389..473
FT /note="Ig-like C2-type 4"
FT DOMAIN 479..568
FT /note="Ig-like C2-type 5"
FT DOMAIN 570..659
FT /note="Ig-like C2-type 6"
FT DOMAIN 672..770
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 775..872
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 877..971
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 976..1066
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 956..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1071
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 815
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 930
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1001
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 122..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 216..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 321..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 410..457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 502..550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 592..649
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:5E4I"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:5E4I"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:5E4I"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:5E4I"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:5E4I"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:5E4I"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:5E4I"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 364..372
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 375..393
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:5E4I"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 464..475
FT /evidence="ECO:0007829|PDB:5E4I"
FT STRAND 675..681
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 686..690
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 702..707
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 720..726
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 731..734
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 745..750
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 788..792
FT /evidence="ECO:0007829|PDB:7MRN"
FT HELIX 798..800
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 803..805
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 807..814
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 818..825
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 832..836
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 845..854
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 857..861
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 865..868
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 882..885
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 887..889
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 891..894
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 906..914
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 923..926
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 928..930
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 932..936
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 944..952
FT /evidence="ECO:0007829|PDB:7MRN"
FT STRAND 964..967
FT /evidence="ECO:0007829|PDB:7MRN"
SQ SEQUENCE 1098 AA; 120746 MW; 201929C9C7C5C3C8 CRC64;
MASCWRLILF LSVTRWLSDY SEALSGLSTS YAALLRIKKS STSPFGSKSR PRFSSPSLGT
ISVSPPSWRG AAQQYHSPGN LYHSSDAFRQ DESVDYGPVF VQEPDDVIFP TDSDEKKVAL
NCEVRGNPSP SYRWLRNGTE IALESDYRYS LIDGTFIISN PSELRDSGLY QCLATNSFGS
ILSREATLQF AYLGNFSGRT RSAVSVREGQ GVVLMCSPPP HSPEIIYSWV FNEFPSFVAE
DSRRFISQET GNLYISKVQT SDVGSYICLV KNAVTNARVL SPPTPLTLRN DGVMGEYEPK
IEVHFPFTVT AAKGTTVKME CFALGNPVPT ITWMKVNGYI PSKSRLRKSQ AVLEIPNLQL
DDAGIYECTA ENSRGKNSFR GQLQIFTYPH WVQKLNDTQL DSGSPLQWEC KATGKPRPTY
RWLKNGAPLL PQSRVDTVNG ILAIQSVNQS DAGMYQCLAE NKYGAIYASA ELKILASPPS
FELNQVKKSI IVTKDRGVLI ECEPQGSPKP AISWRKGDKA VRANKRIAIL PDGSLRILNA
SKADEGKYIC QGVNIFGSAE IIASLSVKEP TRIELTPKRT ELTVGESIVL NCKAIHDASL
DVTFYWTLKG QPIDFEKEGG HFENIRAQAS SADLMIRNIL LMHAGRYGCR VQTTADSVSD
EAELLVRGPP GPPGVVIVEE ITESTATLSW SPATDNHSPI SSYNLQARSP FSLGWQTVKT
VPEVITGDME SAMAVDLNPW VEYEFRVVAT NPIGTGDPSI PSRMIRTNEA VPKTAPSNVS
GRSGRRHELV IAWEPVSEEF QNGEGFGYIV AFRPNGTRGW KEKMVTSSEA SKFIYRDESV
PPLTPFEVKV GVYNNKGDGP FSQIVVICSA EGEPTAAPTD VTATSVSVSE IFVVWKHVKE
SLGRPQGFEI SYWKDTEPED SVETVRTRGN ESFVMLTGLE GNTLYHLTVR AYNGAGYGPP
SREASTTTKR HPPREPPGNL RWEQQGSQVS LGWEPVRPLA NESEVMGYKV FYRQEGHSEG
QVIETQKPQA VVPLPEAGVY IIEVRAYSEG GDGTASSQIR VPSYSGGKIT SAQSTLHSLS
KWSSVTLLLA LMLPSSSW
