NFASC_HUMAN
ID NFASC_HUMAN Reviewed; 1347 AA.
AC O94856; B2RNN8; B3KQZ1; B5MDP6; B5MDR6; B7ZMD8; Q149P5; Q5T2F0; Q5T2F1;
AC Q5T2F2; Q5T2F3; Q5T2F4; Q5T2F5; Q5T2F6; Q5T2F7; Q5T2F9; Q5T2G0; Q5W9F8;
AC Q68DH3; Q6ZQV6; Q7Z3K1; Q96HT1; Q96K50;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 4.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Neurofascin;
DE Flags: Precursor;
GN Name=NFASC; Synonyms=KIAA0756;
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 [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. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT 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 SEQUENCE
RP [LARGE SCALE MRNA] OF 804-1347 (ISOFORMS 3/4), NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 931-1347 (ISOFORM 6), AND NUCLEOTIDE SEQUENCE [LARGE SCALE
RP 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 SPLICING.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 NUCLEOTIDE
RP 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 project:
RT 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 in the
RT 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 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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 through
RT 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 ASN-409,
RP 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 family of
RT neural cell adhesion molecules.";
RL J. Biol. Chem. 286:797-805(2011).
RN [11]
RP INVOLVEMENT IN NEDCPMD, AND VARIANT NEDCPMD PRO-359.
RX PubMed=28940097; DOI=10.1007/s00439-017-1843-2;
RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A.,
RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M.,
RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A.,
RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S.,
RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T.,
RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C.,
RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M.,
RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.;
RT "Expanding the genetic heterogeneity of intellectual disability.";
RL Hum. Genet. 136:1419-1429(2017).
RN [12]
RP ERRATUM OF PUBMED:28940097.
RX PubMed=29288388; DOI=10.1007/s00439-017-1859-7;
RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A.,
RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M.,
RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A.,
RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S.,
RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T.,
RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C.,
RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M.,
RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.;
RT "Correction to: Expanding the genetic heterogeneity of intellectual
RT disability.";
RL Hum. Genet. 137:105-109(2018).
RN [13]
RP VARIANT NEDCPMD 835-VAL--ALA-1347 DEL, CHARACTERIZATION OF VARIANT NEDCPMD
RP 835-ARG--ALA-1347 DEL, AND SUBCELLULAR LOCATION (ISOFORM 8).
RX PubMed=30124836; DOI=10.1093/hmg/ddy277;
RA Smigiel R., Sherman D.L., Rydzanicz M., Walczak A., Mikolajkow D.,
RA Krolak-Olejnik B., Kosinska J., Gasperowicz P., Biernacka A., Stawinski P.,
RA Marciniak M., Andrzejewski W., Boczar M., Krajewski P., Sasiadek M.M.,
RA Brophy P.J., Ploski R.;
RT "Homozygous mutation in the Neurofascin gene affecting the glial isoform of
RT Neurofascin causes severe neurodevelopment disorder with hypotonia, amimia
RT and areflexia.";
RL Hum. Mol. Genet. 27:3669-3674(2018).
RN [14]
RP INVOLVEMENT IN NEDCPMD, VARIANT NEDCPMD GLU-1229, CHARACTERIZATION OF
RP VARIANT NEDCPMD GLU-1229, AND SUBCELLULAR LOCATION.
RX PubMed=30850329; DOI=10.1016/j.parkreldis.2019.02.045;
RA Monfrini E., Straniero L., Bonato S., Monzio Compagnoni G., Bordoni A.,
RA Dilena R., Rinchetti P., Silipigni R., Ronchi D., Corti S., Comi G.P.,
RA Bresolin N., Duga S., Di Fonzo A.;
RT "Neurofascin (NFASC) gene mutation causes autosomal recessive ataxia with
RT demyelinating neuropathy.";
RL Parkinsonism Relat. Disord. 63:66-72(2019).
CC -!- FUNCTION: Cell adhesion, ankyrin-binding protein which may be involved
CC in neurite extension, axonal guidance, synaptogenesis, myelination and
CC 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 beta-
CC 1 (SCN1B) and beta-3 (SCN3B) subunits. Interacts with GLDN/gliomedin
CC (By similarity). Interacts with MYOC. {ECO:0000250,
CC ECO:0000269|PubMed:21047790, ECO:0000269|PubMed:23897819}.
CC -!- INTERACTION:
CC O94856-3; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-12035911, EBI-11743294;
CC O94856-3; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12035911, EBI-11096309;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30850329};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Cell junction, paranodal septate
CC junction {ECO:0000269|PubMed:30124836}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Name=1;
CC IsoId=O94856-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94856-2; Sequence=VSP_016426, VSP_008938;
CC Name=3;
CC IsoId=O94856-3; Sequence=VSP_016424, VSP_016425, VSP_008937,
CC VSP_008940;
CC Name=4;
CC IsoId=O94856-4; Sequence=VSP_016427, VSP_016428, VSP_008940;
CC Name=5;
CC IsoId=O94856-5; Sequence=VSP_008937, VSP_016429;
CC Name=6;
CC IsoId=O94856-6; Sequence=VSP_016430, VSP_016434;
CC Name=7;
CC IsoId=O94856-7; Sequence=VSP_016433;
CC Name=8; Synonyms=Nfasc155 {ECO:0000303|PubMed:30124836};
CC IsoId=O94856-8; Sequence=VSP_016424, VSP_016425, VSP_008937,
CC VSP_016432;
CC Name=9;
CC IsoId=O94856-9; Sequence=VSP_016427, VSP_016428;
CC Name=10;
CC IsoId=O94856-10; Sequence=VSP_016424, VSP_008937, VSP_016432;
CC Name=11;
CC IsoId=O94856-11; Sequence=VSP_016424, VSP_016425, VSP_016432;
CC Name=12;
CC IsoId=O94856-12; Sequence=VSP_016427, VSP_016428, VSP_016432;
CC Name=13;
CC IsoId=O94856-13; Sequence=VSP_016431;
CC -!- DOMAIN: Homophilic adhesion is primarily mediated by the interaction of
CC the second Ig-like domains.
CC -!- DISEASE: Neurodevelopmental disorder with central and peripheral motor
CC dysfunction (NEDCPMD) [MIM:618356]: An autosomal recessive
CC neurodevelopmental disorder with early onset and a highly variable
CC phenotype. Disease features include hypotonia apparent from birth, poor
CC feeding, global developmental delay with absence of reaction to touch
CC and no eye contact, infantile-onset progressive ataxia and
CC demyelinating peripheral neuropathy. {ECO:0000269|PubMed:28940097,
CC ECO:0000269|PubMed:30124836, ECO:0000269|PubMed:30850329}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to intron retention.
CC {ECO:0000305}.
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};
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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.
DR RefSeq; XP_011507630.1; XM_011509328.1.
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 AlphaFoldDB; O94856; -.
DR SMR; O94856; -.
DR BioGRID; 116737; 6.
DR IntAct; O94856; 9.
DR STRING; 9606.ENSP00000344786; -.
DR CarbonylDB; O94856; -.
DR GlyConnect; 1552; 15 N-Linked glycans (6 sites).
DR GlyGen; O94856; 9 sites, 15 N-linked glycans (6 sites).
DR iPTMnet; O94856; -.
DR PhosphoSitePlus; O94856; -.
DR SwissPalm; O94856; -.
DR BioMuta; NFASC; -.
DR EPD; O94856; -.
DR jPOST; O94856; -.
DR MassIVE; O94856; -.
DR MaxQB; O94856; -.
DR PaxDb; O94856; -.
DR PeptideAtlas; O94856; -.
DR PRIDE; O94856; -.
DR ProteomicsDB; 50490; -. [O94856-1]
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 ABCD; O94856; 1 sequenced antibody.
DR Antibodypedia; 2194; 227 antibodies from 35 providers.
DR DNASU; 23114; -.
DR Ensembl; ENST00000339876.11; ENSP00000344786.6; ENSG00000163531.17. [O94856-9]
DR Ensembl; ENST00000401399.5; ENSP00000385637.1; ENSG00000163531.17. [O94856-9]
DR Ensembl; ENST00000403080.5; ENSP00000384875.1; ENSG00000163531.17. [O94856-2]
DR Ensembl; ENST00000404076.5; ENSP00000385676.1; ENSG00000163531.17. [O94856-10]
DR Ensembl; ENST00000430393.7; ENSP00000415031.3; ENSG00000163531.17. [O94856-8]
DR Ensembl; ENST00000513543.6; ENSP00000425908.1; ENSG00000163531.17. [O94856-3]
DR Ensembl; ENST00000539706.6; ENSP00000438614.2; ENSG00000163531.17. [O94856-11]
DR GeneID; 23114; -.
DR KEGG; hsa:23114; -.
DR MANE-Select; ENST00000339876.11; ENSP00000344786.6; NM_001005388.3; NP_001005388.2. [O94856-9]
DR UCSC; uc001hbh.4; human. [O94856-1]
DR CTD; 23114; -.
DR DisGeNET; 23114; -.
DR GeneCards; NFASC; -.
DR HGNC; HGNC:29866; NFASC.
DR HPA; ENSG00000163531; Tissue enhanced (brain).
DR MalaCards; NFASC; -.
DR MIM; 609145; gene.
DR MIM; 618356; phenotype.
DR neXtProt; NX_O94856; -.
DR OpenTargets; ENSG00000163531; -.
DR PharmGKB; PA128395771; -.
DR VEuPathDB; HostDB:ENSG00000163531; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000157024; -.
DR HOGENOM; CLU_005756_2_0_1; -.
DR InParanoid; O94856; -.
DR OMA; AGRGDYP; -.
DR OrthoDB; 434404at2759; -.
DR PhylomeDB; O94856; -.
DR TreeFam; TF351098; -.
DR PathwayCommons; O94856; -.
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 SignaLink; O94856; -.
DR SIGNOR; O94856; -.
DR BioGRID-ORCS; 23114; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; NFASC; human.
DR EvolutionaryTrace; O94856; -.
DR GeneWiki; NFASC; -.
DR GenomeRNAi; 23114; -.
DR Pharos; O94856; Tbio.
DR PRO; PR:O94856; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O94856; protein.
DR Bgee; ENSG00000163531; Expressed in inferior olivary complex and 185 other tissues.
DR ExpressionAtlas; O94856; baseline and differential.
DR Genevisible; O94856; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
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:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0097454; C:Schwann cell microvillus; IEA:Ensembl.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
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:0042552; P:myelination; ISS:BHF-UCL.
DR GO; GO:0007422; P:peripheral nervous system development; ISS:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0050808; P:synapse organization; IEA:InterPro.
DR GO; GO:0019226; P:transmission of nerve impulse; IEA:InterPro.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 11.
DR InterPro; IPR043204; Basigin-like.
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; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF35; PTHR10075:SF35; 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 junction;
KW Cell membrane; Disease variant; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1347
FT /note="Neurofascin"
FT /id="PRO_0000015049"
FT TOPO_DOM 25..1217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1218..1238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1239..1347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..137
FT /note="Ig-like C2-type 1"
FT DOMAIN 143..230
FT /note="Ig-like C2-type 2"
FT DOMAIN 244..332
FT /note="Ig-like C2-type 3"
FT DOMAIN 337..424
FT /note="Ig-like C2-type 4"
FT DOMAIN 429..517
FT /note="Ig-like C2-type 5"
FT DOMAIN 521..603
FT /note="Ig-like C2-type 6"
FT DOMAIN 630..725
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 730..823
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 828..930
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 934..1030
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1114..1206
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 713..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 481
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U3"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97685"
FT MOD_RES 1294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97685"
FT MOD_RES 1297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97685"
FT MOD_RES 1333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U3"
FT MOD_RES 1334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U3"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U3"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21047790"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
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 973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 988
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21047790"
FT DISULFID 162..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21047790"
FT DISULFID 268..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21047790"
FT DISULFID 358..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21047790"
FT DISULFID 452..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 543..592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 31..36
FT /note="Missing (in isoform 3, isoform 8, isoform 10 and
FT isoform 11)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_016424"
FT VAR_SEQ 236
FT /note="T -> NHPYNDSSLRNHPDMYSA (in isoform 3, isoform 8 and
FT isoform 11)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_016425"
FT VAR_SEQ 611..625
FT /note="Missing (in isoform 3, isoform 5, isoform 8 and
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15491607, ECO:0000303|PubMed:9872452"
FT /id="VSP_008937"
FT VAR_SEQ 611..619
FT /note="ADQATPTNR -> GNCPCSPWH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_016426"
FT VAR_SEQ 620..1347
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008938"
FT VAR_SEQ 824..930
FT /note="Missing (in isoform 4, isoform 9 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016427"
FT VAR_SEQ 931
FT /note="V -> L (in isoform 4, isoform 9 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016428"
FT VAR_SEQ 1030..1203
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_008940"
FT VAR_SEQ 1030..1152
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016430"
FT VAR_SEQ 1030..1043
FT /note="ATPTAAPPTLPPTT -> GRCMAAAPGVKGPS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15491607"
FT /id="VSP_016429"
FT VAR_SEQ 1035..1203
FT /note="Missing (in isoform 8, isoform 10, isoform 11 and
FT isoform 12)"
FT /evidence="ECO:0000305"
FT /id="VSP_016432"
FT VAR_SEQ 1035..1113
FT /note="Missing (in isoform 13)"
FT /evidence="ECO:0000305"
FT /id="VSP_016431"
FT VAR_SEQ 1114..1203
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016433"
FT VAR_SEQ 1153
FT /note="S -> G (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016434"
FT VARIANT 159
FT /note="T -> M (in dbSNP:rs3795564)"
FT /id="VAR_017251"
FT VARIANT 359
FT /note="R -> P (in NEDCPMD; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28940097"
FT /id="VAR_083116"
FT VARIANT 835..1347
FT /note="Missing (in NEDCPMD; no protein expression; unknown
FT pathological significance)"
FT /evidence="ECO:0000269|PubMed:30124836"
FT /id="VAR_083117"
FT VARIANT 1229
FT /note="V -> E (in NEDCPMD; decreased protein abundance in
FT patient-derived cells; decreased cell surface localization;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:30850329"
FT /id="VAR_083118"
FT CONFLICT 807
FT /note="F -> L (in Ref. 3; BAB55195)"
FT /evidence="ECO:0000305"
FT CONFLICT 972
FT /note="F -> V (in Ref. 3; AK127424)"
FT /evidence="ECO:0000305"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3P40"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:3P3Y"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3P3Y"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3P3Y"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:3P40"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3P3Y"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3P3Y"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3P40"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:3P3Y"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:3P3Y"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:3P3Y"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 324..341
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:3P3Y"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 405..412
FT /evidence="ECO:0007829|PDB:3P3Y"
FT STRAND 415..425
FT /evidence="ECO:0007829|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
