NRCAM_HUMAN
ID NRCAM_HUMAN Reviewed; 1304 AA.
AC Q92823; A4D0S3; E9PDA4; O15051; O15179; Q14BM2; Q9UHI3; Q9UHI4;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Neuronal cell adhesion molecule;
DE Short=Nr-CAM;
DE AltName: Full=Neuronal surface protein Bravo {ECO:0000303|PubMed:8812479};
DE Short=hBravo {ECO:0000303|PubMed:8812479};
DE AltName: Full=NgCAM-related cell adhesion molecule;
DE Short=Ng-CAM-related;
DE Flags: Precursor;
GN Name=NRCAM; Synonyms=KIAA0343;
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 [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8812479; DOI=10.1006/geno.1996.0385;
RA Lane R.P., Chen X.-N., Yamakawa K., Vielmetter J., Korenberg J.R.,
RA Dreyer W.J.;
RT "Characterization of a highly conserved human homolog to the chicken neural
RT cell surface protein Bravo/Nr-CAM that maps to chromosome band 7q31.";
RL Genomics 35:456-465(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 5).
RX PubMed=11483367; DOI=10.1016/s0378-1119(01)00493-0;
RA Dry K., Kenwrick S., Rosenthal A., Platzer M.;
RT "The complete sequence of the human locus for NgCAM-related cell adhesion
RT molecule reveals a novel alternative exon in chick and man and conserved
RT genomic organization for the L1 subfamily.";
RL Gene 273:115-122(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT ALA-545.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Amygdala;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-545.
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-545.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), AND VARIANT ALA-545.
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-1304 (ISOFORM 1).
RC TISSUE=Brain;
RA Wang B., Williams H., Du J., Terrett J., Kenwricl S.;
RT "Temporal and spatial regulation of alternative splicing for human NrCAM in
RT neural and non neural tissues.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-276.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-276.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP GLYCOSYLATION AT ASN-858.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [13]
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 [14]
RP STRUCTURE BY NMR OF 638-751.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first fibronectin type III domain of human
RT KIAA0343 protein.";
RL Submitted (NOV-2003) to the PDB data bank.
RN [15]
RP STRUCTURE BY NMR OF 838-950.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the third fibronectin III domain of human KIAA0343
RT protein.";
RL Submitted (NOV-2003) to the PDB data bank.
RN [16]
RP VARIANTS [LARGE SCALE ANALYSIS] PRO-1093 AND VAL-1116.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Cell adhesion protein that is required for normal responses
CC to cell-cell contacts in brain and in the peripheral nervous system.
CC Plays a role in neurite outgrowth in response to contactin binding.
CC Plays a role in mediating cell-cell contacts between Schwann cells and
CC axons. Plays a role in the formation and maintenance of the nodes of
CC Ranvier on myelinated axons. Nodes of Ranvier contain clustered sodium
CC channels that are crucial for the saltatory propagation of action
CC potentials along myelinated axons. During development, nodes of Ranvier
CC are formed by the fusion of two heminodes. Required for normal
CC clustering of sodium channels at heminodes; not required for the
CC formation of mature nodes with normal sodium channel clusters.
CC Required, together with GLDN, for maintaining NFASC and sodium channel
CC clusters at mature nodes of Ranvier. {ECO:0000250|UniProtKB:Q810U4}.
CC -!- SUBUNIT: Constituent of a NFASC/NRCAM/ankyrin-G complex. Detected in a
CC complex with CNTN1 and PTPRB. Interacts with GLDN/gliomedin (By
CC similarity). Interacts with MYOC (PubMed:23897819).
CC {ECO:0000250|UniProtKB:Q810U4, ECO:0000269|PubMed:23897819}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q810U4};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q810U4}.
CC Cell projection, axon {ECO:0000250|UniProtKB:Q810U4}. Secreted
CC {ECO:0000250|UniProtKB:Q810U4}. Note=Detected at nodes of Ranvier.
CC {ECO:0000250|UniProtKB:Q810U4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q92823-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92823-2; Sequence=VSP_007841, VSP_007842;
CC Name=3;
CC IsoId=Q92823-3; Sequence=VSP_007838, VSP_007840;
CC Name=4;
CC IsoId=Q92823-4; Sequence=VSP_007837, VSP_007839, VSP_007840;
CC Name=5;
CC IsoId=Q92823-5; Sequence=VSP_007843;
CC Name=6;
CC IsoId=Q92823-6; Sequence=VSP_007838, VSP_045040;
CC -!- TISSUE SPECIFICITY: Detected in all the examined tissues. In the brain
CC it was detected in the amygdala, caudate nucleus, corpus callosum,
CC hippocampus, hypothalamus, substantia nigra, subthalamic nucleus and
CC thalamus.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA20801.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NRCAMID41578ch7q31.html";
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DR EMBL; U55258; AAC50765.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF172277; AAF22282.1; -; Genomic_DNA.
DR EMBL; AF172277; AAF22283.1; -; Genomic_DNA.
DR EMBL; AB002341; BAA20801.2; ALT_INIT; mRNA.
DR EMBL; BX538010; CAD97960.1; -; mRNA.
DR EMBL; AC005683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236947; EAL24386.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83429.1; -; Genomic_DNA.
DR EMBL; BC115736; AAI15737.1; -; mRNA.
DR EMBL; AJ001054; CAA04504.1; -; mRNA.
DR EMBL; AJ001057; CAA04507.1; -; mRNA.
DR CCDS; CCDS47686.1; -. [Q92823-1]
DR CCDS; CCDS55153.1; -. [Q92823-6]
DR CCDS; CCDS5751.1; -. [Q92823-4]
DR RefSeq; NP_001032209.1; NM_001037132.2. [Q92823-1]
DR RefSeq; NP_001180511.1; NM_001193582.1.
DR RefSeq; NP_001180512.1; NM_001193583.1. [Q92823-6]
DR RefSeq; NP_001180513.1; NM_001193584.1. [Q92823-3]
DR RefSeq; NP_005001.3; NM_005010.4. [Q92823-4]
DR RefSeq; XP_005250430.1; XM_005250373.2.
DR RefSeq; XP_006716066.1; XM_006716003.1. [Q92823-5]
DR RefSeq; XP_016867746.1; XM_017012257.1.
DR PDB; 1UEN; NMR; -; A=839-950.
DR PDB; 1UEY; NMR; -; A=638-751.
DR PDBsum; 1UEN; -.
DR PDBsum; 1UEY; -.
DR AlphaFoldDB; Q92823; -.
DR SMR; Q92823; -.
DR BioGRID; 110953; 14.
DR IntAct; Q92823; 6.
DR MINT; Q92823; -.
DR STRING; 9606.ENSP00000368314; -.
DR GlyConnect; 821; 17 N-Linked glycans (9 sites).
DR GlyGen; Q92823; 22 sites, 20 N-linked glycans (9 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q92823; -.
DR PhosphoSitePlus; Q92823; -.
DR SwissPalm; Q92823; -.
DR BioMuta; NRCAM; -.
DR DMDM; 215274127; -.
DR EPD; Q92823; -.
DR MassIVE; Q92823; -.
DR MaxQB; Q92823; -.
DR PaxDb; Q92823; -.
DR PeptideAtlas; Q92823; -.
DR PRIDE; Q92823; -.
DR ProteomicsDB; 19619; -.
DR ProteomicsDB; 75497; -. [Q92823-1]
DR ProteomicsDB; 75498; -. [Q92823-2]
DR ProteomicsDB; 75499; -. [Q92823-3]
DR ProteomicsDB; 75500; -. [Q92823-4]
DR ProteomicsDB; 75501; -. [Q92823-5]
DR Antibodypedia; 17285; 361 antibodies from 39 providers.
DR DNASU; 4897; -.
DR Ensembl; ENST00000351718.8; ENSP00000325269.6; ENSG00000091129.22. [Q92823-4]
DR Ensembl; ENST00000379024.8; ENSP00000368310.4; ENSG00000091129.22. [Q92823-6]
DR Ensembl; ENST00000379028.8; ENSP00000368314.3; ENSG00000091129.22. [Q92823-1]
DR GeneID; 4897; -.
DR KEGG; hsa:4897; -.
DR MANE-Select; ENST00000379028.8; ENSP00000368314.3; NM_001037132.4; NP_001032209.1.
DR UCSC; uc003vfc.4; human. [Q92823-1]
DR CTD; 4897; -.
DR DisGeNET; 4897; -.
DR GeneCards; NRCAM; -.
DR HGNC; HGNC:7994; NRCAM.
DR HPA; ENSG00000091129; Tissue enhanced (adrenal gland, brain, epididymis, retina).
DR MIM; 601581; gene.
DR neXtProt; NX_Q92823; -.
DR OpenTargets; ENSG00000091129; -.
DR PharmGKB; PA31773; -.
DR VEuPathDB; HostDB:ENSG00000091129; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000155419; -.
DR HOGENOM; CLU_005756_1_1_1; -.
DR InParanoid; Q92823; -.
DR OMA; MVQPPTI; -.
DR OrthoDB; 434404at2759; -.
DR PhylomeDB; Q92823; -.
DR TreeFam; TF351098; -.
DR PathwayCommons; Q92823; -.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-447038; NrCAM interactions.
DR Reactome; R-HSA-447043; Neurofascin interactions.
DR SignaLink; Q92823; -.
DR SIGNOR; Q92823; -.
DR BioGRID-ORCS; 4897; 4 hits in 1073 CRISPR screens.
DR ChiTaRS; NRCAM; human.
DR EvolutionaryTrace; Q92823; -.
DR GeneWiki; NRCAM; -.
DR GenomeRNAi; 4897; -.
DR Pharos; Q92823; Tbio.
DR PRO; PR:Q92823; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q92823; protein.
DR Bgee; ENSG00000091129; Expressed in lateral nuclear group of thalamus and 163 other tissues.
DR ExpressionAtlas; Q92823; baseline and differential.
DR Genevisible; Q92823; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0043194; C:axon initial segment; ISS:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030506; F:ankyrin binding; IDA:UniProtKB.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEP:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007413; P:axonal fasciculation; NAS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; NAS:UniProtKB.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; IDA:UniProtKB.
DR GO; GO:0001764; P:neuron migration; NAS:UniProtKB.
DR GO; GO:0019227; P:neuronal action potential propagation; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; NAS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0030516; P:regulation of axon extension; NAS:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0099175; P:regulation of postsynapse organization; IEA:Ensembl.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; TAS:UniProtKB.
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; IPR003006; Ig/MHC_CS.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 3.
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.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1304
FT /note="Neuronal cell adhesion molecule"
FT /id="PRO_0000015057"
FT TOPO_DOM 25..1167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1168..1190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1191..1304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..134
FT /note="Ig-like 1"
FT DOMAIN 141..235
FT /note="Ig-like 2"
FT DOMAIN 267..356
FT /note="Ig-like 3"
FT DOMAIN 361..448
FT /note="Ig-like 4"
FT DOMAIN 454..541
FT /note="Ig-like 5"
FT DOMAIN 545..632
FT /note="Ig-like 6"
FT DOMAIN 649..744
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 746..843
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 848..950
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 954..1051
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1064..1156
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1199..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT MOD_RES 1225
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT MOD_RES 1226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT MOD_RES 1251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT MOD_RES 1271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97686"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT MOD_RES 1295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810U4"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 716
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 993
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1009
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1072
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 68..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 167..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 292..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 382..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 476..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 567..616
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 35..40
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_007837"
FT VAR_SEQ 241..259
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9205841"
FT /id="VSP_007838"
FT VAR_SEQ 635..644
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_007839"
FT VAR_SEQ 1051..1155
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:9205841"
FT /id="VSP_007840"
FT VAR_SEQ 1063..1155
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045040"
FT VAR_SEQ 1225
FT /note="Y -> YRSLE (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_007843"
FT VAR_SEQ 1226..1236
FT /note="SDAEDHKPLKK -> RLFSFVSSASF (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_007841"
FT VAR_SEQ 1237..1304
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_007842"
FT VARIANT 545
FT /note="P -> A (in dbSNP:rs6958498)"
FT /evidence="ECO:0000269|PubMed:12690205,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9205841,
FT ECO:0000269|Ref.7"
FT /id="VAR_047550"
FT VARIANT 1093
FT /note="H -> P (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035528"
FT VARIANT 1116
FT /note="G -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035529"
FT CONFLICT 487
FT /note="E -> Q (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="I -> IKDATWIVKEI (in Ref. 1; AAC50765)"
FT /evidence="ECO:0000305"
FT CONFLICT 541..550
FT /note="Missing (in Ref. 1; AAC50765)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="F -> L (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 679..682
FT /note="KFII -> TIHD (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="K -> N (in Ref. 3; BAA20801)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="V -> E (in Ref. 1; AAC50765)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="S -> F (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 790
FT /note="D -> V (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="F -> L (in Ref. 4; CAD97960)"
FT /evidence="ECO:0000305"
FT CONFLICT 954
FT /note="A -> V (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 994
FT /note="S -> N (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="A -> T (in Ref. 4; CAD97960)"
FT /evidence="ECO:0000305"
FT CONFLICT 1021
FT /note="S -> T (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 1068
FT /note="P -> T (in Ref. 1; AAC50765)"
FT /evidence="ECO:0000305"
FT CONFLICT 1093..1094
FT /note="HV -> YA (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="V -> F (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141..1143
FT /note="DSG -> GPR (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 1149
FT /note="D -> G (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT CONFLICT 1256
FT /note="V -> L (in Ref. 9; CAA04507)"
FT /evidence="ECO:0000305"
FT STRAND 651..656
FT /evidence="ECO:0007829|PDB:1UEY"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:1UEY"
FT STRAND 663..668
FT /evidence="ECO:0007829|PDB:1UEY"
FT STRAND 677..686
FT /evidence="ECO:0007829|PDB:1UEY"
FT TURN 687..689
FT /evidence="ECO:0007829|PDB:1UEY"
FT STRAND 694..703
FT /evidence="ECO:0007829|PDB:1UEY"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:1UEY"
FT STRAND 720..727
FT /evidence="ECO:0007829|PDB:1UEY"
FT STRAND 853..858
FT /evidence="ECO:0007829|PDB:1UEN"
FT STRAND 861..865
FT /evidence="ECO:0007829|PDB:1UEN"
FT HELIX 871..874
FT /evidence="ECO:0007829|PDB:1UEN"
FT STRAND 878..889
FT /evidence="ECO:0007829|PDB:1UEN"
FT STRAND 901..909
FT /evidence="ECO:0007829|PDB:1UEN"
FT STRAND 911..917
FT /evidence="ECO:0007829|PDB:1UEN"
FT STRAND 923..934
FT /evidence="ECO:0007829|PDB:1UEN"
FT STRAND 936..939
FT /evidence="ECO:0007829|PDB:1UEN"
FT STRAND 943..946
FT /evidence="ECO:0007829|PDB:1UEN"
SQ SEQUENCE 1304 AA; 143890 MW; 1F2698BC7DB5C363 CRC64;
MQLKIMPKKK RLSAGRVPLI LFLCQMISAL EVPLDPKLLE DLVQPPTITQ QSPKDYIIDP
RENIVIQCEA KGKPPPSFSW TRNGTHFDID KDPLVTMKPG TGTLIINIMS EGKAETYEGV
YQCTARNERG AAVSNNIVVR PSRSPLWTKE KLEPITLQSG QSLVLPCRPP IGLPPPIIFW
MDNSFQRLPQ SERVSQGLNG DLYFSNVLPE DTREDYICYA RFNHTQTIQQ KQPISVKVIS
VDELNDTIAA NLSDTEFYGA KSSRERPPTF LTPEGNASNK EELRGNVLSL ECIAEGLPTP
IIYWAKEDGM LPKNRTVYKN FEKTLQIIHV SEADSGNYQC IAKNALGAIH HTISVRVKAA
PYWITAPQNL VLSPGEDGTL ICRANGNPKP RISWLTNGVP IEIAPDDPSR KIDGDTIIFS
NVQERSSAVY QCNASNEYGY LLANAFVNVL AEPPRILTPA NTLYQVIANR PALLDCAFFG
SPLPTIEWFK GAKGSALHED IYVLHENGTL EIPVAQKDST GTYTCVARNK LGMAKNEVHL
EIKDPTWIVK QPEYAVVQRG SMVSFECKVK HDHTLSLTVL WLKDNRELPS DERFTVDKDH
LVVADVSDDD SGTYTCVANT TLDSVSASAV LSVVAPTPTP APVYDVPNPP FDLELTDQLD
KSVQLSWTPG DDNNSPITKF IIEYEDAMHK PGLWHHQTEV SGTQTTAQLK LSPYVNYSFR
VMAVNSIGKS LPSEASEQYL TKASEPDKNP TAVEGLGSEP DNLVITWKPL NGFESNGPGL
QYKVSWRQKD GDDEWTSVVV ANVSKYIVSG TPTFVPYLIK VQALNDMGFA PEPAVVMGHS
GEDLPMVAPG NVRVNVVNST LAEVHWDPVP LKSIRGHLQG YRIYYWKTQS SSKRNRRHIE
KKILTFQGSK THGMLPGLEP FSHYTLNVRV VNGKGEGPAS PDRVFNTPEG VPSAPSSLKI
VNPTLDSLTL EWDPPSHPNG ILTEYTLKYQ PINSTHELGP LVDLKIPANK TRWTLKNLNF
STRYKFYFYA QTSAGSGSQI TEEAVTTVDE AGILPPDVGA GKVQAVNPRI SNLTAAAAET
YANISWEYEG PEHVNFYVEY GVAGSKEEWR KEIVNGSRSF FGLKGLMPGT AYKVRVGAVG
DSGFVSSEDV FETGPAMASR QVDIATQGWF IGLMCAVALL ILILLIVCFI RRNKGGKYPV
KEKEDAHADP EIQPMKEDDG TFGEYSDAED HKPLKKGSRT PSDRTVKKED SDDSLVDYGE
GVNGQFNEDG SFIGQYSGKK EKEPAEGNES SEAPSPVNAM NSFV
