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   27-MAR-2024, entry version 172.
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   GlyCosmos; O94779; 9 sites, No reported glycans.
DR   GlyGen; O94779; 9 sites.
DR   iPTMnet; O94779; -.
DR   PhosphoSitePlus; O94779; -.
DR   BioMuta; CNTN5; -.
DR   MassIVE; O94779; -.
DR   PaxDb; 9606-ENSP00000435637; -.
DR   PeptideAtlas; O94779; -.
DR   ProteomicsDB; 21441; -.
DR   ProteomicsDB; 50439; -. [O94779-1]
DR   ProteomicsDB; 50440; -. [O94779-2]
DR   Antibodypedia; 31696; 185 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   AGR; HGNC:2175; -.
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; CLTWTVL; -.
DR   OrthoDB; 3073820at2759; -.
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 1144 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 94 other cell types or tissues.
DR   ExpressionAtlas; O94779; baseline and differential.
DR   Genevisible; O94779; HS.
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:0042734; C:presynaptic membrane; IEA:Ensembl.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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   CDD; cd04969; Ig5_Contactin; 1.
DR   CDD; cd05848; IgI_1_Contactin-5; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR44170:SF17; CONTACTIN-5; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07679; I-set; 4.
DR   Pfam; PF13927; Ig_3; 2.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 6.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 6.
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
//