CNTN5_HUMAN
ID CNTN5_HUMAN Reviewed; 1100 AA.
AC O94779; A1L4P0; B7ZM07; E9PKE8; O94780; Q49AF3;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Contactin-5;
DE AltName: Full=Neural recognition molecule NB-2;
DE Short=hNB-2;
DE Flags: Precursor;
GN Name=CNTN5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Cerebellum;
RX PubMed=11013081; DOI=10.1006/geno.2000.6310;
RA Kamei Y., Takeda Y., Teramoto K., Tsutsumi O., Taketani Y., Watanabe K.;
RT "Human NB-2 of the contactin subgroup molecules: chromosomal localization
RT of the gene (CNTN5) and distinct expression pattern from other subgroup
RT members.";
RL Genomics 69:113-119(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP VAL-530 AND THR-1079.
RC 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 [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. Probably
CC involved in neuronal activity in the auditory system (By similarity).
CC {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=O94779-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, HNB-2s;
CC IsoId=O94779-2; Sequence=VSP_011967;
CC Name=3;
CC IsoId=O94779-4; Sequence=VSP_045995;
CC -!- TISSUE SPECIFICITY: Expressed in brain and kidney and at very low level
CC in placenta. Not expressed in other tissues. In brain, it is highly
CC expressed in the occipital lobe, amygdala, cerebral cortex, frontal
CC lobe, thalamus and temporal lobe. Expressed at moderate level in the
CC cerebellum, substantia nigra, putamen, medulla and hippocampus. Weakly
CC expressed in the spinal cord and caudate nucleus. Weakly or not
CC expressed in the corpus callosum. {ECO:0000269|PubMed:11013081}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH39255.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB013802; BAA36579.2; -; mRNA.
DR EMBL; AB013803; BAA36580.2; -; mRNA.
DR EMBL; AP000760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP004249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039255; AAH39255.1; ALT_SEQ; mRNA.
DR EMBL; BC130619; AAI30620.1; -; mRNA.
DR EMBL; BC144185; AAI44186.1; -; mRNA.
DR CCDS; CCDS53696.1; -. [O94779-1]
DR CCDS; CCDS53697.1; -. [O94779-2]
DR CCDS; CCDS58168.1; -. [O94779-4]
DR RefSeq; NP_001230199.1; NM_001243270.1. [O94779-1]
DR RefSeq; NP_001230200.1; NM_001243271.1. [O94779-4]
DR RefSeq; NP_055176.1; NM_014361.3. [O94779-1]
DR RefSeq; NP_780775.1; NM_175566.2. [O94779-2]
DR RefSeq; XP_011541173.1; XM_011542871.1. [O94779-2]
DR RefSeq; XP_016873415.1; XM_017017926.1. [O94779-1]
DR PDB; 4N68; X-ray; 1.80 A; A=871-971.
DR PDB; 5E52; X-ray; 2.69 A; A=671-969.
DR PDBsum; 4N68; -.
DR PDBsum; 5E52; -.
DR AlphaFoldDB; O94779; -.
DR SMR; O94779; -.
DR BioGRID; 119823; 1.
DR IntAct; O94779; 3.
DR STRING; 9606.ENSP00000435637; -.
DR GlyGen; O94779; 9 sites.
DR iPTMnet; O94779; -.
DR PhosphoSitePlus; O94779; -.
DR BioMuta; CNTN5; -.
DR MassIVE; O94779; -.
DR PaxDb; O94779; -.
DR PeptideAtlas; O94779; -.
DR PRIDE; O94779; -.
DR ProteomicsDB; 21441; -.
DR ProteomicsDB; 50439; -. [O94779-1]
DR ProteomicsDB; 50440; -. [O94779-2]
DR Antibodypedia; 31696; 172 antibodies from 23 providers.
DR DNASU; 53942; -.
DR Ensembl; ENST00000418526.6; ENSP00000393229.2; ENSG00000149972.12. [O94779-2]
DR Ensembl; ENST00000524871.6; ENSP00000435637.1; ENSG00000149972.12. [O94779-1]
DR Ensembl; ENST00000527185.5; ENSP00000433575.1; ENSG00000149972.12. [O94779-4]
DR Ensembl; ENST00000528682.5; ENSP00000436185.1; ENSG00000149972.12. [O94779-1]
DR GeneID; 53942; -.
DR KEGG; hsa:53942; -.
DR MANE-Select; ENST00000524871.6; ENSP00000435637.1; NM_014361.4; NP_055176.1.
DR UCSC; uc001pfz.4; human. [O94779-1]
DR CTD; 53942; -.
DR DisGeNET; 53942; -.
DR GeneCards; CNTN5; -.
DR HGNC; HGNC:2175; CNTN5.
DR HPA; ENSG00000149972; Tissue enhanced (brain, placenta, salivary gland, thyroid gland).
DR MIM; 607219; gene.
DR neXtProt; NX_O94779; -.
DR OpenTargets; ENSG00000149972; -.
DR PharmGKB; PA26689; -.
DR VEuPathDB; HostDB:ENSG00000149972; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000158183; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; O94779; -.
DR OMA; ELSLGWE; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; O94779; -.
DR TreeFam; TF351103; -.
DR PathwayCommons; O94779; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; O94779; -.
DR BioGRID-ORCS; 53942; 12 hits in 1066 CRISPR screens.
DR ChiTaRS; CNTN5; human.
DR GenomeRNAi; 53942; -.
DR Pharos; O94779; Tbio.
DR PRO; PR:O94779; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O94779; protein.
DR Bgee; ENSG00000149972; Expressed in adrenal tissue and 93 other tissues.
DR ExpressionAtlas; O94779; baseline and differential.
DR Genevisible; O94779; HS.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
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:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0099054; P:presynapse assembly; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
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; 2.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13895; Ig_2; 1.
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; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1072
FT /note="Contactin-5"
FT /id="PRO_0000014717"
FT PROPEP 1073..1100
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014718"
FT DOMAIN 99..190
FT /note="Ig-like C2-type 1"
FT DOMAIN 196..282
FT /note="Ig-like C2-type 2"
FT DOMAIN 300..385
FT /note="Ig-like C2-type 3"
FT DOMAIN 390..474
FT /note="Ig-like C2-type 4"
FT DOMAIN 480..567
FT /note="Ig-like C2-type 5"
FT DOMAIN 571..660
FT /note="Ig-like C2-type 6"
FT DOMAIN 673..771
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 776..873
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 878..972
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 977..1067
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 959..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1072
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 816
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 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 217..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 322..369
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 411..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 503..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 593..650
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 19..92
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11013081"
FT /id="VSP_011967"
FT VAR_SEQ 912..1100
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045995"
FT VARIANT 23
FT /note="S -> A (in dbSNP:rs10790978)"
FT /id="VAR_019907"
FT VARIANT 70
FT /note="L -> R (in dbSNP:rs7125822)"
FT /id="VAR_019908"
FT VARIANT 81
FT /note="N -> S (in dbSNP:rs10893933)"
FT /id="VAR_019909"
FT VARIANT 530
FT /note="I -> V (in dbSNP:rs11223168)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_019910"
FT VARIANT 1065
FT /note="Y -> F (in dbSNP:rs1944169)"
FT /id="VAR_019911"
FT VARIANT 1079
FT /note="S -> T (in dbSNP:rs1216183)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_019912"
FT VARIANT 1094
FT /note="M -> V (in dbSNP:rs35208161)"
FT /id="VAR_033610"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 684..691
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 703..709
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 721..727
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 732..737
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 743..751
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 778..782
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 789..795
FT /evidence="ECO:0007829|PDB:5E52"
FT HELIX 799..801
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 808..815
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 822..826
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 833..837
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 839..841
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 846..855
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 858..862
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 866..871
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 880..886
FT /evidence="ECO:0007829|PDB:4N68"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:4N68"
FT STRAND 892..897
FT /evidence="ECO:0007829|PDB:4N68"
FT HELIX 901..903
FT /evidence="ECO:0007829|PDB:4N68"
FT STRAND 907..915
FT /evidence="ECO:0007829|PDB:4N68"
FT HELIX 920..922
FT /evidence="ECO:0007829|PDB:4N68"
FT STRAND 924..927
FT /evidence="ECO:0007829|PDB:4N68"
FT STRAND 929..931
FT /evidence="ECO:0007829|PDB:5E52"
FT STRAND 934..937
FT /evidence="ECO:0007829|PDB:4N68"
FT STRAND 945..954
FT /evidence="ECO:0007829|PDB:4N68"
FT STRAND 965..968
FT /evidence="ECO:0007829|PDB:4N68"
SQ SEQUENCE 1100 AA; 120686 MW; 5883575D84AD030E CRC64;
MASSWKLMLF LSVTMCLSEY SKSLPGLSTS YAALLRIKKS SSSSLFGSKT RPRYSSPSLG
TLSASSPSWL GAAQNYYSPI NLYHSSDAFK QDESVDYGPV FVQEPDDIIF PTDSDEKKVA
LNCEVRGNPV PSYRWLRNGT EIDLESDYRY SLIDGTFIIS NPSEAKDSGH YQCLATNTVG
SILSREATLQ FAYLGNFSGR TRSAVSVREG QGVVLMCSPP PHSPEIIYSW VFNEFPSFVA
EDSRRFISQE TGNLYISKVQ TSDVGSYICL VKNTVTNARV LSPPTPLTLR NDGVMGEYEP
KIEVHFPFTV TAAKGTTVKM ECFALGNPVP TITWMKVNGY IPSKARLRKS QAVLEIPNVQ
LDDAGIYECR AENSRGKNSF RGQLQVYTYP HWVEKLNDTQ LDSGSPLRWE CKATGKPRPT
YRWLKNGVPL SPQSRVEMVN GVLMIHNVNQ SDAGMYQCLA ENKYGAIYAS AELKILASAP
TFALNQLKKT IIVTKDQEVV IECKPQGSPK PTISWKKGDR AVRENKRIAI LPDGSLRILN
ASKSDEGKYV CRGENVFGSA EIIASLSVKE PTRIELTPKR TELTVGESIV LNCKAIHDAS
LDVTFYWTLK GQPIDFEEEG GHFESIRAQA SSADLMIRNI LLMHAGRYGC RVQTTADSVS
DEAELLVRGP PGPPGIVIVE EITESTATLS WSPAADNHSP ISSYNLQARS PFSLGWQTVK
TVPEIITGDM ESAMAVDLNP WVEYEFRVVA TNPIGTGDPS TPSRMIRTNE AVPKTAPTNV
SGRSGRRHEL VIAWEPVSEE FQNGEGFGYI VAFRPNGTRG WKEKMVTSSE ASKFIYRDES
VPPLTPFEVK VGVYNNKGDG PFSQIVVICS AEGEPSAAPT DVKATSVSVS EILVAWKHIK
ESLGRPQGFE VGYWKDMEQE DTAETVKTRG NESFVILTGL EGNTLYHFTV RAYNGAGYGP
PSSEVSATTK KSPPSQAPSN LRWEQQGSQV SLGWEPVIPL ANESEVVGYK VFYRQEGHSN
SQVIETQKLQ AVVPLPDAGV YIIEVRAYSE GGDGTASSQI RVPSYSGGKI TSAQSTLHSL
STSSSSVTLL LALMIPSTSW
