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   13-FEB-2019, entry version 142.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Watanabe K.;
RT   "Human NB-2 of the contactin subgroup molecules: chromosomal
RT   localization of the gene (CNTN5) and distinct expression pattern from
RT   other subgroup 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.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   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
RP   VARIANTS 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
RT   project: 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
RT   members 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
CC       nervous system development. Has some neurite outgrowth-promoting
CC       activity in the cerebral cortical neurons but not in hippocampal
CC       neurons. Probably involved in neuronal activity in the auditory
CC       system (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
CC       GPI-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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in brain and kidney and at very low
CC       level in placenta. Not expressed in other tissues. In brain, it is
CC       highly expressed in the occipital lobe, amygdala, cerebral cortex,
CC       frontal lobe, thalamus and temporal lobe. Expressed at moderate
CC       level in the cerebellum, substantia nigra, putamen, medulla and
CC       hippocampus. Weakly expressed in the spinal cord and caudate
CC       nucleus. Weakly or not expressed in the corpus callosum.
CC       {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; Positions=223; Note=Translated as Ser.; 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   UniGene; Hs.656783; -.
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   ProteinModelPortal; O94779; -.
DR   SMR; O94779; -.
DR   BioGrid; 119823; 1.
DR   IntAct; O94779; 2.
DR   STRING; 9606.ENSP00000279463; -.
DR   iPTMnet; O94779; -.
DR   PhosphoSitePlus; O94779; -.
DR   BioMuta; CNTN5; -.
DR   EPD; O94779; -.
DR   jPOST; O94779; -.
DR   PaxDb; O94779; -.
DR   PeptideAtlas; O94779; -.
DR   PRIDE; O94779; -.
DR   ProteomicsDB; 50439; -.
DR   ProteomicsDB; 50440; -. [O94779-2]
DR   Ensembl; ENST00000418526; ENSP00000393229; ENSG00000149972. [O94779-2]
DR   Ensembl; ENST00000524871; ENSP00000435637; ENSG00000149972. [O94779-1]
DR   Ensembl; ENST00000527185; ENSP00000433575; ENSG00000149972. [O94779-4]
DR   Ensembl; ENST00000528682; ENSP00000436185; ENSG00000149972. [O94779-1]
DR   GeneID; 53942; -.
DR   KEGG; hsa:53942; -.
DR   UCSC; uc001pfz.4; human. [O94779-1]
DR   CTD; 53942; -.
DR   DisGeNET; 53942; -.
DR   EuPathDB; HostDB:ENSG00000149972.10; -.
DR   GeneCards; CNTN5; -.
DR   HGNC; HGNC:2175; CNTN5.
DR   HPA; HPA039492; -.
DR   HPA; HPA041223; -.
DR   MIM; 607219; gene.
DR   neXtProt; NX_O94779; -.
DR   OpenTargets; ENSG00000149972; -.
DR   PharmGKB; PA26689; -.
DR   eggNOG; KOG3513; Eukaryota.
DR   eggNOG; ENOG410XSVG; LUCA.
DR   GeneTree; ENSGT00940000158183; -.
DR   HOGENOM; HOG000059617; -.
DR   HOVERGEN; HBG051047; -.
DR   InParanoid; O94779; -.
DR   KO; K06763; -.
DR   OMA; VPSYRWL; -.
DR   OrthoDB; 655902at2759; -.
DR   PhylomeDB; O94779; -.
DR   TreeFam; TF351103; -.
DR   Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   ChiTaRS; CNTN5; human.
DR   GenomeRNAi; 53942; -.
DR   PRO; PR:O94779; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000149972; Expressed in 84 organ(s), highest expression level in adrenal tissue.
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:0005829; C:cytosol; IDA:HPA.
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; TAS:Reactome.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; PTHR43905:SF3; PTHR43905:SF3; 1.
DR   Pfam; PF00041; fn3; 2.
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; Alternative splicing; Cell adhesion; Cell membrane;
KW   Complete proteome; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Polymorphism;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   1072       Contactin-5.
FT                                /FTId=PRO_0000014717.
FT   PROPEP     1073   1100       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000014718.
FT   DOMAIN       99    190       Ig-like C2-type 1.
FT   DOMAIN      196    282       Ig-like C2-type 2.
FT   DOMAIN      300    385       Ig-like C2-type 3.
FT   DOMAIN      390    474       Ig-like C2-type 4.
FT   DOMAIN      480    567       Ig-like C2-type 5.
FT   DOMAIN      571    660       Ig-like C2-type 6.
FT   DOMAIN      673    771       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      776    873       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      878    972       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      977   1067       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   LIPID      1072   1072       GPI-anchor amidated serine.
FT                                {ECO:0000255}.
FT   CARBOHYD    138    138       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    196    196       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    397    397       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    449    449       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    540    540       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    779    779       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    816    816       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    931    931       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1002   1002       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    123    173       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    217    269       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    322    369       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    411    458       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    503    551       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    593    650       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   VAR_SEQ      19     92       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11013081}.
FT                                /FTId=VSP_011967.
FT   VAR_SEQ     912   1100       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_045995.
FT   VARIANT      23     23       S -> A (in dbSNP:rs10790978).
FT                                /FTId=VAR_019907.
FT   VARIANT      70     70       L -> R (in dbSNP:rs7125822).
FT                                /FTId=VAR_019908.
FT   VARIANT      81     81       N -> S (in dbSNP:rs10893933).
FT                                /FTId=VAR_019909.
FT   VARIANT     530    530       I -> V (in dbSNP:rs11223168).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_019910.
FT   VARIANT    1065   1065       Y -> F (in dbSNP:rs1944169).
FT                                /FTId=VAR_019911.
FT   VARIANT    1079   1079       S -> T (in dbSNP:rs1216183).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_019912.
FT   VARIANT    1094   1094       M -> V (in dbSNP:rs35208161).
FT                                /FTId=VAR_033610.
FT   STRAND      677    682       {ECO:0000244|PDB:5E52}.
FT   STRAND      684    691       {ECO:0000244|PDB:5E52}.
FT   STRAND      703    709       {ECO:0000244|PDB:5E52}.
FT   STRAND      721    727       {ECO:0000244|PDB:5E52}.
FT   STRAND      732    737       {ECO:0000244|PDB:5E52}.
FT   STRAND      743    751       {ECO:0000244|PDB:5E52}.
FT   STRAND      778    782       {ECO:0000244|PDB:5E52}.
FT   STRAND      789    795       {ECO:0000244|PDB:5E52}.
FT   HELIX       799    801       {ECO:0000244|PDB:5E52}.
FT   STRAND      804    806       {ECO:0000244|PDB:5E52}.
FT   STRAND      808    815       {ECO:0000244|PDB:5E52}.
FT   STRAND      822    826       {ECO:0000244|PDB:5E52}.
FT   STRAND      833    837       {ECO:0000244|PDB:5E52}.
FT   STRAND      839    841       {ECO:0000244|PDB:5E52}.
FT   STRAND      846    855       {ECO:0000244|PDB:5E52}.
FT   STRAND      858    862       {ECO:0000244|PDB:5E52}.
FT   STRAND      866    871       {ECO:0000244|PDB:5E52}.
FT   STRAND      880    886       {ECO:0000244|PDB:4N68}.
FT   STRAND      888    890       {ECO:0000244|PDB:4N68}.
FT   STRAND      892    897       {ECO:0000244|PDB:4N68}.
FT   HELIX       901    903       {ECO:0000244|PDB:4N68}.
FT   STRAND      907    915       {ECO:0000244|PDB:4N68}.
FT   HELIX       920    922       {ECO:0000244|PDB:4N68}.
FT   STRAND      924    927       {ECO:0000244|PDB:4N68}.
FT   STRAND      929    931       {ECO:0000244|PDB:5E52}.
FT   STRAND      934    937       {ECO:0000244|PDB:4N68}.
FT   STRAND      945    954       {ECO:0000244|PDB:4N68}.
FT   STRAND      965    968       {ECO:0000244|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
//