ID NFASC_HUMAN Reviewed; 1347 AA. AC O94856; B2RNN8; B3KQZ1; B5MDP6; B5MDR6; B7ZMD8; Q149P5; Q5T2F0; AC Q5T2F1; Q5T2F2; Q5T2F3; Q5T2F4; Q5T2F5; Q5T2F6; Q5T2F7; Q5T2F9; AC Q5T2G0; Q5W9F8; Q68DH3; Q6ZQV6; Q7Z3K1; Q96HT1; Q96K50; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 4. DT 13-FEB-2019, entry version 174. DE RecName: Full=Neurofascin; DE Flags: Precursor; GN Name=NFASC; Synonyms=KIAA0756; 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 [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [2] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 804-1347 (ISOFORMS 3/4), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 931-1347 (ISOFORM 6), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 972-1347 (ISOFORM 1). RC TISSUE=Teratocarcinoma, and Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE RP SPLICING. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 9), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-1347 (ISOFORM 2). 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 193-1347 (ISOFORM 5). RX PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028; RA Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.; RT "Alternative splice variants encoding unstable protein domains exist RT in the human brain."; RL J. Mol. Biol. 343:1207-1220(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1040-1347 (ISOFORM 7), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1204-1347 (ISOFORMS RP 1/3/4/6/7). RC TISSUE=Amygdala, and Esophageal carcinoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-481 AND SER-485, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP INTERACTION WITH MYOC. RX PubMed=23897819; DOI=10.1074/jbc.M112.446138; RA Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C., RA Tomarev S.I.; RT "Myocilin mediates myelination in the peripheral nervous system RT through ErbB2/3 signaling."; RL J. Biol. Chem. 288:26357-26371(2013). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-428, GLYCOSYLATION AT RP ASN-409, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=21047790; DOI=10.1074/jbc.M110.180281; RA Liu H., Focia P.J., He X.; RT "Homophilic adhesion mechanism of neurofascin, a member of the L1 RT family of neural cell adhesion molecules."; RL J. Biol. Chem. 286:797-805(2011). CC -!- FUNCTION: Cell adhesion, ankyrin-binding protein which may be CC involved in neurite extension, axonal guidance, synaptogenesis, CC myelination and neuron-glial cell interactions. {ECO:0000250}. CC -!- SUBUNIT: Horseshoe-shaped homodimer. Probable constituent of a CC NFASC/NRCAM/ankyrin-G complex. Associates with the sodium channel CC beta-1 (SCN1B) and beta-3 (SCN3B) subunits. Interacts with CC GLDN/gliomedin (By similarity). Interacts with MYOC. {ECO:0000250, CC ECO:0000269|PubMed:21047790, ECO:0000269|PubMed:23897819}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=13; CC Name=1; CC IsoId=O94856-1; Sequence=Displayed; CC Note=No experimental confirmation available.; CC Name=2; CC IsoId=O94856-2; Sequence=VSP_016426, VSP_008938; CC Note=May be due to intron retention.; CC Name=3; CC IsoId=O94856-3; Sequence=VSP_016424, VSP_016425, VSP_008937, CC VSP_008940; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=O94856-4; Sequence=VSP_016427, VSP_016428, VSP_008940; CC Note=No experimental confirmation available.; CC Name=5; CC IsoId=O94856-5; Sequence=VSP_008937, VSP_016429; CC Note=May be due to intron retention.; CC Name=6; CC IsoId=O94856-6; Sequence=VSP_016430, VSP_016434; CC Note=No experimental confirmation available.; CC Name=7; CC IsoId=O94856-7; Sequence=VSP_016433; CC Note=No experimental confirmation available.; CC Name=8; CC IsoId=O94856-8; Sequence=VSP_016424, VSP_016425, VSP_008937, CC VSP_016432; CC Note=No experimental confirmation available.; CC Name=9; CC IsoId=O94856-9; Sequence=VSP_016427, VSP_016428; CC Note=No experimental confirmation available.; CC Name=10; CC IsoId=O94856-10; Sequence=VSP_016424, VSP_008937, VSP_016432; CC Note=No experimental confirmation available.; CC Name=11; CC IsoId=O94856-11; Sequence=VSP_016424, VSP_016425, VSP_016432; CC Note=No experimental confirmation available.; CC Name=12; CC IsoId=O94856-12; Sequence=VSP_016427, VSP_016428, VSP_016432; CC Note=No experimental confirmation available.; CC Name=13; CC IsoId=O94856-13; Sequence=VSP_016431; CC Note=No experimental confirmation available.; CC -!- DOMAIN: Homophilic adhesion is primarily mediated by the CC interaction of the second Ig-like domains. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CC L1/neurofascin/NgCAM family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA34476.3; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAB55195.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC87577.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AB018299; BAA34476.3; ALT_INIT; mRNA. DR EMBL; AK027553; BAB55195.1; ALT_INIT; mRNA. DR EMBL; AK090639; BAG52203.1; -; mRNA. DR EMBL; AK127424; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK128699; BAC87577.1; ALT_INIT; mRNA. DR EMBL; AC096675; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391822; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008124; AAH08124.2; -; mRNA. DR EMBL; BC117674; AAI17675.2; -; mRNA. DR EMBL; BC137013; AAI37014.1; -; mRNA. DR EMBL; BC144454; AAI44455.1; -; mRNA. DR EMBL; AB177861; BAD66839.1; -; mRNA. DR EMBL; BX537841; CAD97852.1; -; mRNA. DR EMBL; CR749402; CAH18247.1; -; mRNA. DR CCDS; CCDS30982.1; -. [O94856-3] DR CCDS; CCDS53460.1; -. [O94856-9] DR CCDS; CCDS53461.1; -. [O94856-2] DR CCDS; CCDS53462.1; -. [O94856-8] DR RefSeq; NP_001005388.2; NM_001005388.2. [O94856-9] DR RefSeq; NP_001005389.2; NM_001005389.1. [O94856-2] DR RefSeq; NP_001153803.1; NM_001160331.1. [O94856-11] DR RefSeq; NP_001153804.1; NM_001160332.1. [O94856-8] DR RefSeq; NP_001153805.1; NM_001160333.1. DR RefSeq; NP_055905.2; NM_015090.3. [O94856-3] DR RefSeq; XP_011507621.1; XM_011509319.1. [O94856-1] DR RefSeq; XP_011507630.1; XM_011509328.1. DR UniGene; Hs.13349; -. DR PDB; 3P3Y; X-ray; 2.60 A; A=25-428. DR PDB; 3P40; X-ray; 3.20 A; A=25-428. DR PDBsum; 3P3Y; -. DR PDBsum; 3P40; -. DR ProteinModelPortal; O94856; -. DR SMR; O94856; -. DR BioGrid; 116737; 2. DR IntAct; O94856; 7. DR STRING; 9606.ENSP00000344786; -. DR CarbonylDB; O94856; -. DR GlyConnect; 1552; -. DR iPTMnet; O94856; -. DR PhosphoSitePlus; O94856; -. DR SwissPalm; O94856; -. DR BioMuta; NFASC; -. DR EPD; O94856; -. DR jPOST; O94856; -. DR MaxQB; O94856; -. DR PaxDb; O94856; -. DR PeptideAtlas; O94856; -. DR PRIDE; O94856; -. DR ProteomicsDB; 50490; -. DR ProteomicsDB; 50491; -. [O94856-10] DR ProteomicsDB; 50492; -. [O94856-11] DR ProteomicsDB; 50493; -. [O94856-12] DR ProteomicsDB; 50494; -. [O94856-13] DR ProteomicsDB; 50495; -. [O94856-2] DR ProteomicsDB; 50496; -. [O94856-3] DR ProteomicsDB; 50497; -. [O94856-4] DR ProteomicsDB; 50498; -. [O94856-5] DR ProteomicsDB; 50499; -. [O94856-6] DR ProteomicsDB; 50500; -. [O94856-7] DR ProteomicsDB; 50501; -. [O94856-8] DR ProteomicsDB; 50502; -. [O94856-9] DR TopDownProteomics; O94856-2; -. [O94856-2] DR Ensembl; ENST00000339876; ENSP00000344786; ENSG00000163531. [O94856-9] DR Ensembl; ENST00000360049; ENSP00000353154; ENSG00000163531. [O94856-3] DR Ensembl; ENST00000401399; ENSP00000385637; ENSG00000163531. [O94856-9] DR Ensembl; ENST00000403080; ENSP00000384875; ENSG00000163531. [O94856-2] DR Ensembl; ENST00000404076; ENSP00000385676; ENSG00000163531. [O94856-10] DR Ensembl; ENST00000404907; ENSP00000384061; ENSG00000163531. [O94856-8] DR Ensembl; ENST00000513543; ENSP00000425908; ENSG00000163531. [O94856-3] DR Ensembl; ENST00000539706; ENSP00000438614; ENSG00000163531. [O94856-8] DR GeneID; 23114; -. DR KEGG; hsa:23114; -. DR UCSC; uc001hbh.4; human. [O94856-1] DR CTD; 23114; -. DR DisGeNET; 23114; -. DR EuPathDB; HostDB:ENSG00000163531.15; -. DR GeneCards; NFASC; -. DR HGNC; HGNC:29866; NFASC. DR HPA; HPA008832; -. DR MIM; 609145; gene. DR neXtProt; NX_O94856; -. DR OpenTargets; ENSG00000163531; -. DR PharmGKB; PA128395771; -. DR eggNOG; KOG3513; Eukaryota. DR eggNOG; ENOG410XSVG; LUCA. DR GeneTree; ENSGT00940000157024; -. DR HOVERGEN; HBG000144; -. DR InParanoid; O94856; -. DR KO; K06757; -. DR OMA; WEPQGDN; -. DR OrthoDB; 434404at2759; -. DR PhylomeDB; O94856; -. DR TreeFam; TF351098; -. DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins. DR Reactome; R-HSA-447043; Neurofascin interactions. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR ChiTaRS; NFASC; human. DR EvolutionaryTrace; O94856; -. DR GeneWiki; NFASC; -. DR GenomeRNAi; 23114; -. DR PRO; PR:O94856; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000163531; Expressed in 203 organ(s), highest expression level in brain. DR ExpressionAtlas; O94856; baseline and differential. DR Genevisible; O94856; HS. DR GO; GO:0043194; C:axon initial segment; ISS:ARUK-UCL. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl. DR GO; GO:0033268; C:node of Ranvier; ISS:BHF-UCL. DR GO; GO:0033010; C:paranodal junction; IEA:Ensembl. DR GO; GO:0033270; C:paranode region of axon; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0097454; C:Schwann cell microvillus; IEA:Ensembl. DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl. DR GO; GO:0007411; P:axon guidance; IEA:Ensembl. DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; IEA:Ensembl. DR GO; GO:0042552; P:myelination; ISS:BHF-UCL. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0030913; P:paranodal junction assembly; IEA:Ensembl. DR GO; GO:0007422; P:peripheral nervous system development; ISS:BHF-UCL. DR GO; GO:0071205; P:protein localization to juxtaparanode region of axon; IEA:Ensembl. DR GO; GO:0002175; P:protein localization to paranode region of axon; IEA:Ensembl. DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:0050808; P:synapse organization; IEA:Ensembl. DR GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl. DR CDD; cd00063; FN3; 5. DR Gene3D; 2.60.40.10; -; 11. 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 InterPro; IPR013151; Immunoglobulin. DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C. DR InterPro; IPR026965; NFASC. DR PANTHER; PTHR43951:SF4; PTHR43951:SF4; 1. DR Pfam; PF13882; Bravo_FIGEY; 1. DR Pfam; PF00041; fn3; 5. DR Pfam; PF07679; I-set; 2. DR Pfam; PF00047; ig; 1. DR SMART; SM00060; FN3; 5. DR SMART; SM00409; IG; 6. DR SMART; SM00408; IGc2; 6. DR SUPFAM; SSF48726; SSF48726; 6. DR SUPFAM; SSF49265; SSF49265; 3. DR PROSITE; PS50853; FN3; 5. 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; KW Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 1347 Neurofascin. FT /FTId=PRO_0000015049. FT TOPO_DOM 25 1217 Extracellular. {ECO:0000255}. FT TRANSMEM 1218 1238 Helical. {ECO:0000255}. FT TOPO_DOM 1239 1347 Cytoplasmic. {ECO:0000255}. FT DOMAIN 41 137 Ig-like C2-type 1. FT DOMAIN 143 230 Ig-like C2-type 2. FT DOMAIN 244 332 Ig-like C2-type 3. FT DOMAIN 337 424 Ig-like C2-type 4. FT DOMAIN 429 517 Ig-like C2-type 5. FT DOMAIN 521 603 Ig-like C2-type 6. FT DOMAIN 630 725 Fibronectin type-III 1. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 730 823 Fibronectin type-III 2. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 828 930 Fibronectin type-III 3. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 934 1030 Fibronectin type-III 4. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT DOMAIN 1114 1206 Fibronectin type-III 5. FT {ECO:0000255|PROSITE-ProRule:PRU00316}. FT COMPBIAS 1031 1108 Thr-rich. FT MOD_RES 481 481 Phosphotyrosine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 485 485 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1267 1267 Phosphoserine. FT {ECO:0000250|UniProtKB:Q810U3}. FT MOD_RES 1281 1281 Phosphoserine. FT {ECO:0000250|UniProtKB:P97685}. FT MOD_RES 1294 1294 Phosphoserine. FT {ECO:0000250|UniProtKB:P97685}. FT MOD_RES 1297 1297 Phosphoserine. FT {ECO:0000250|UniProtKB:P97685}. FT MOD_RES 1333 1333 Phosphoserine. FT {ECO:0000250|UniProtKB:Q810U3}. FT MOD_RES 1334 1334 Phosphoserine. FT {ECO:0000250|UniProtKB:Q810U3}. FT MOD_RES 1338 1338 Phosphoserine. FT {ECO:0000250|UniProtKB:Q810U3}. FT CARBOHYD 305 305 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 409 409 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:21047790}. FT CARBOHYD 446 446 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 483 483 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 752 752 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 778 778 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 973 973 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 988 988 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 63 118 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:21047790}. FT DISULFID 162 213 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:21047790}. FT DISULFID 268 316 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:21047790}. FT DISULFID 358 408 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:21047790}. FT DISULFID 452 501 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 543 592 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VAR_SEQ 31 36 Missing (in isoform 3, isoform 8, isoform FT 10 and isoform 11). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9872452}. FT /FTId=VSP_016424. FT VAR_SEQ 236 236 T -> NHPYNDSSLRNHPDMYSA (in isoform 3, FT isoform 8 and isoform 11). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9872452}. FT /FTId=VSP_016425. FT VAR_SEQ 611 625 Missing (in isoform 3, isoform 5, isoform FT 8 and isoform 10). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15491607, FT ECO:0000303|PubMed:9872452}. FT /FTId=VSP_008937. FT VAR_SEQ 611 619 ADQATPTNR -> GNCPCSPWH (in isoform 2). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_016426. FT VAR_SEQ 620 1347 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_008938. FT VAR_SEQ 824 930 Missing (in isoform 4, isoform 9 and FT isoform 12). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_016427. FT VAR_SEQ 931 931 V -> L (in isoform 4, isoform 9 and FT isoform 12). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_016428. FT VAR_SEQ 1030 1203 Missing (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9872452}. FT /FTId=VSP_008940. FT VAR_SEQ 1030 1152 Missing (in isoform 6). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_016430. FT VAR_SEQ 1030 1043 ATPTAAPPTLPPTT -> GRCMAAAPGVKGPS (in FT isoform 5). FT {ECO:0000303|PubMed:15491607}. FT /FTId=VSP_016429. FT VAR_SEQ 1035 1203 Missing (in isoform 8, isoform 10, FT isoform 11 and isoform 12). FT {ECO:0000305}. FT /FTId=VSP_016432. FT VAR_SEQ 1035 1113 Missing (in isoform 13). {ECO:0000305}. FT /FTId=VSP_016431. FT VAR_SEQ 1114 1203 Missing (in isoform 7). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_016433. FT VAR_SEQ 1153 1153 S -> G (in isoform 6). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_016434. FT VARIANT 159 159 T -> M (in dbSNP:rs3795564). FT /FTId=VAR_017251. FT CONFLICT 807 807 F -> L (in Ref. 3; BAB55195). FT {ECO:0000305}. FT CONFLICT 972 972 F -> V (in Ref. 3; AK127424). FT {ECO:0000305}. FT STRAND 43 46 {ECO:0000244|PDB:3P3Y}. FT STRAND 49 53 {ECO:0000244|PDB:3P40}. FT STRAND 55 57 {ECO:0000244|PDB:3P3Y}. FT STRAND 63 65 {ECO:0000244|PDB:3P3Y}. FT STRAND 72 77 {ECO:0000244|PDB:3P3Y}. FT HELIX 84 86 {ECO:0000244|PDB:3P3Y}. FT STRAND 94 96 {ECO:0000244|PDB:3P3Y}. FT TURN 104 106 {ECO:0000244|PDB:3P3Y}. FT HELIX 109 112 {ECO:0000244|PDB:3P40}. FT STRAND 114 121 {ECO:0000244|PDB:3P3Y}. FT STRAND 126 136 {ECO:0000244|PDB:3P3Y}. FT STRAND 150 153 {ECO:0000244|PDB:3P3Y}. FT STRAND 158 160 {ECO:0000244|PDB:3P3Y}. FT STRAND 172 176 {ECO:0000244|PDB:3P3Y}. FT STRAND 187 191 {ECO:0000244|PDB:3P3Y}. FT STRAND 197 201 {ECO:0000244|PDB:3P3Y}. FT HELIX 205 207 {ECO:0000244|PDB:3P3Y}. FT STRAND 211 216 {ECO:0000244|PDB:3P3Y}. FT TURN 218 220 {ECO:0000244|PDB:3P3Y}. FT STRAND 223 225 {ECO:0000244|PDB:3P3Y}. FT STRAND 231 234 {ECO:0000244|PDB:3P3Y}. FT STRAND 236 238 {ECO:0000244|PDB:3P40}. FT STRAND 246 249 {ECO:0000244|PDB:3P3Y}. FT STRAND 251 259 {ECO:0000244|PDB:3P3Y}. FT STRAND 264 267 {ECO:0000244|PDB:3P3Y}. FT STRAND 277 282 {ECO:0000244|PDB:3P3Y}. FT TURN 289 291 {ECO:0000244|PDB:3P3Y}. FT STRAND 292 295 {ECO:0000244|PDB:3P3Y}. FT HELIX 296 298 {ECO:0000244|PDB:3P3Y}. FT STRAND 300 305 {ECO:0000244|PDB:3P3Y}. FT HELIX 308 310 {ECO:0000244|PDB:3P3Y}. FT STRAND 312 319 {ECO:0000244|PDB:3P3Y}. FT STRAND 324 341 {ECO:0000244|PDB:3P3Y}. FT STRAND 346 348 {ECO:0000244|PDB:3P3Y}. FT STRAND 354 357 {ECO:0000244|PDB:3P3Y}. FT STRAND 359 364 {ECO:0000244|PDB:3P3Y}. FT STRAND 367 372 {ECO:0000244|PDB:3P3Y}. FT HELIX 377 379 {ECO:0000244|PDB:3P3Y}. FT STRAND 386 389 {ECO:0000244|PDB:3P3Y}. FT STRAND 392 397 {ECO:0000244|PDB:3P3Y}. FT STRAND 405 412 {ECO:0000244|PDB:3P3Y}. FT STRAND 415 425 {ECO:0000244|PDB:3P3Y}. SQ SEQUENCE 1347 AA; 150027 MW; 4DC555E5AA06C223 CRC64; MARQPPPPWV HAAFLLCLLS LGGAIEIPMD PSIQNELTQP PTITKQSAKD HIVDPRDNIL IECEAKGNPA PSFHWTRNSR FFNIAKDPRV SMRRRSGTLV IDFRSGGRPE EYEGEYQCFA RNKFGTALSN RIRLQVSKSP LWPKENLDPV VVQEGAPLTL QCNPPPGLPS PVIFWMSSSM EPITQDKRVS QGHNGDLYFS NVMLQDMQTD YSCNARFHFT HTIQQKNPFT LKVLTTRGVA ERTPSFMYPQ GTASSQMVLR GMDLLLECIA SGVPTPDIAW YKKGGDLPSD KAKFENFNKA LRITNVSEED SGEYFCLASN KMGSIRHTIS VRVKAAPYWL DEPKNLILAP GEDGRLVCRA NGNPKPTVQW MVNGEPLQSA PPNPNREVAG DTIIFRDTQI SSRAVYQCNT SNEHGYLLAN AFVSVLDVPP RMLSPRNQLI RVILYNRTRL DCPFFGSPIP TLRWFKNGQG SNLDGGNYHV YENGSLEIKM IRKEDQGIYT CVATNILGKA ENQVRLEVKD PTRIYRMPED QVARRGTTVQ LECRVKHDPS LKLTVSWLKD DEPLYIGNRM KKEDDSLTIF GVAERDQGSY TCVASTELDQ DLAKAYLTVL ADQATPTNRL AALPKGRPDR PRDLELTDLA ERSVRLTWIP GDANNSPITD YVVQFEEDQF QPGVWHDHSK YPGSVNSAVL RLSPYVNYQF RVIAINEVGS SHPSLPSERY RTSGAPPESN PGDVKGEGTR KNNMEITWTP MNATSAFGPN LRYIVKWRRR ETREAWNNVT VWGSRYVVGQ TPVYVPYEIR VQAENDFGKG PEPESVIGYS GEDYPRAAPT EVKVRVMNST AISLQWNRVY SDTVQGQLRE YRAYYWRESS LLKNLWVSQK RQQASFPGDR LRGVVSRLFP YSNYKLEMVV VNGRGDGPRS ETKEFTTPEG VPSAPRRFRV RQPNLETINL EWDHPEHPNG IMIGYTLKYV AFNGTKVGKQ IVENFSPNQT KFTVQRTDPV SRYRFTLSAR TQVGSGEAVT EESPAPPNEA TPTAAPPTLP PTTVGATGAV SSTDATAIAA TTEATTVPII PTVAPTTIAT TTTVATTTTT TAAATTTTES PPTTTSGTKI HESAPDEQSI WNVTVLPNSK WANITWKHNF GPGTDFVVEY IDSNHTKKTV PVKAQAQPIQ LTDLYPGMTY TLRVYSRDNE GISSTVITFM TSTAYTNNQA DIATQGWFIG LMCAIALLVL ILLIVCFIKR SRGGKYPVRE KKDVPLGPED PKEEDGSFDY SDEDNKPLQG SQTSLDGTIK QQESDDSLVD YGEGGEGQFN EDGSFIGQYT VKKDKEETEG NESSEATSPV NAIYSLA //