NFASC

NFASC
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3P3Y, 3P40
Identifiers
Aliases	NFASC , NF, NRCAML, neurofascin, NEDCPMD
External IDs	OMIM: 609145; MGI: 104753; HomoloGene: 24945; GeneCards: NFASC; OMA:NFASC - orthologs
Gene location (Human) Chr. Chromosome 1 (human) [1] Band 1q32.1 Start 204,828,651 bp [1] End 205,022,822 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1 E4|1 57.42 cM Start 132,492,428 bp [2] End 132,669,535 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in inferior olivary nucleus lateral nuclear group of thalamus external globus pallidus corpus callosum dorsal motor nucleus of vagus nerve inferior ganglion of vagus nerve glomerulus metanephric glomerulus pars reticulata pars compacta Top expressed in neural layer of retina visual cortex primary visual cortex central gray substance of midbrain cerebellar cortex superior cervical ganglion superior frontal gyrus anterior horn of spinal cord pontine nuclei lumbar subsegment of spinal cord More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein domain specific binding protein binding protein binding involved in heterotypic cell-cell adhesion Cellular component integral component of membrane membrane focal adhesion myelin sheath plasma membrane Schwann cell microvillus intracellular anatomical structure axon paranodal junction axon initial segment paranode region of axon extracellular exosome node of Ranvier ficolin-1-rich granule membrane dendrite integral component of plasma membrane Biological process clustering of voltage-gated sodium channels peripheral nervous system development transmission of nerve impulse heterotypic cell-cell adhesion synapse organization protein localization to paranode region of axon cell adhesion paranodal junction assembly myelination protein localization to juxtaparanode region of axon axon guidance neutrophil degranulation protein localization to plasma membrane Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23114 269116 Ensembl ENSG00000163531 ENSMUSG00000026442 UniProt O94856 Q810U3 RefSeq (mRNA) NM_001005387 NM_001005388 NM_001005389 NM_001160331 NM_001160332 NM_001160333 NM_015090 NM_001365986 NM_001378330 NM_001378331 NM_001378329 NM_001160316 NM_001160317 NM_001160318 NM_182716 RefSeq (protein) NP_001005388 NP_001005389 NP_001153803 NP_001153804 NP_001153805 NP_055905 NP_001352915 NP_001365259 NP_001365260 NP_001365258 NP_001153788 NP_001153789 NP_001153790 NP_874385 Location (UCSC) Chr 1: 204.83 – 205.02 Mb Chr 1: 132.49 – 132.67 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Neurofascin is a protein that in humans is encoded by the NFASC gene. ^{[5] [6] [7]}

Function

Neurofascin is an L1 family immunoglobulin cell adhesion molecule (see L1CAM) involved in axon subcellular targeting and synapse formation during neural development. ^{[7] [8]}

Clinical importance

A homozygous mutation causing loss of Nfasc155 causes severe congenital hypotonia, contractures of fingers and toes and no reaction to touch or pain. ^[9]

References

1. GRCh38: Ensembl release 89: ENSG00000163531 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026442 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Volkmer H, Hassel B, Wolff JM, Frank R, Rathjen FG (July 1992). "Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily". The Journal of Cell Biology. 118 (1): 149–61. doi:10.1083/jcb.118.1.149. PMC   2289533 . PMID   1377696.
6. Burmeister M, Ren Q, Makris GJ, Samson D, Bennett V (July 1996). "Genes for the neuronal immunoglobulin domain cell adhesion molecules neurofascin and Nr-CAM map to mouse chromosomes 1 and 12 and homologous human chromosomes". Mammalian Genome. 7 (7): 558–9. doi:10.1007/s003359900168. PMID   8672144. S2CID   29190292.
7. "Entrez Gene: NFASC neurofascin homolog (chicken)".
8. Ango F, di Cristo G, Higashiyama H, Bennett V, Wu P, Huang ZJ (October 2004). "Ankyrin-based subcellular gradient of neurofascin, an immunoglobulin family protein, directs GABAergic innervation at purkinje axon initial segment". Cell. 119 (2): 257–72. doi: 10.1016/j.cell.2004.10.004 . PMID   15479642. S2CID   16245348.
9. Smigiel R, Sherman DL, Rydzanicz M, Walczak A, Mikolajkow D, Krolak-Olejnik B, Kosinska J, Gasperowicz P, Biernacka A, Stawinski P, Marciniak M, Andrzejewski W, Boczar M, Krajewski P, Sasiadek MM, Brophy PJ, Ploski R (August 2018). "Homozygous mutation in the Neurofascin gene affecting the glial isoform of Neurofascin causes severe neurodevelopment disorder with hypotonia, amimia and areflexia". Human Molecular Genetics. 27 (21): 3669–3674. doi:10.1093/hmg/ddy277. PMC   6196652 . PMID   30124836.

Further reading

• Hortsch M (October 1996). "The L1 family of neural cell adhesion molecules: old proteins performing new tricks". Neuron. 17 (4): 587–93. doi: 10.1016/S0896-6273(00)80192-0 . PMID   8893017. S2CID   9625203.
• Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (June 2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research. 9 (3): 99–106. CiteSeerX   10.1.1.500.923 . doi:10.1093/dnares/9.3.99. PMID   12168954.
• Tuvia S, Garver TD, Bennett V (November 1997). "The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation". Proceedings of the National Academy of Sciences of the United States of America. 94 (24): 12957–62. Bibcode:1997PNAS...9412957T. doi: 10.1073/pnas.94.24.12957 . PMC   24245 . PMID   9371782.
• Ren Q, Bennett V (May 1998). "Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules". Journal of Neurochemistry. 70 (5): 1839–49. doi: 10.1046/j.1471-4159.1998.70051839.x . PMID   9572267.
• Zhang X, Davis JQ, Carpenter S, Bennett V (November 1998). "Structural requirements for association of neurofascin with ankyrin". The Journal of Biological Chemistry. 273 (46): 30785–94. doi: 10.1074/jbc.273.46.30785 . PMID   9804856.
• Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (October 1998). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 5 (5): 277–86. doi: 10.1093/dnares/5.5.277 . PMID   9872452.
• Koroll M, Rathjen FG, Volkmer H (April 2001). "The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity". The Journal of Biological Chemistry. 276 (14): 10646–54. doi: 10.1074/jbc.M010647200 . PMID   11152476.
• Ratcliffe CF, Westenbroek RE, Curtis R, Catterall WA (July 2001). "Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain". The Journal of Cell Biology. 154 (2): 427–34. doi:10.1083/jcb.200102086. PMC   2150779 . PMID   11470829.
• Jenkins SM, Kizhatil K, Kramarcy NR, Sen A, Sealock R, Bennett V (November 2001). "FIGQY phosphorylation defines discrete populations of L1 cell adhesion molecules at sites of cell-cell contact and in migrating neurons". Journal of Cell Science. 114 (Pt 21): 3823–35. doi:10.1242/jcs.114.21.3823. PMID   11719549.
• Jenkins SM, Bennett V (November 2001). "Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments". The Journal of Cell Biology. 155 (5): 739–46. doi:10.1083/jcb.200109026. PMC   2150881 . PMID   11724816.
• Charles P, Tait S, Faivre-Sarrailh C, Barbin G, Gunn-Moore F, Denisenko-Nehrbass N, Guennoc AM, Girault JA, Brophy PJ, Lubetzki C (February 2002). "Neurofascin is a glial receptor for the paranodin/Caspr-contactin axonal complex at the axoglial junction". Current Biology. 12 (3): 217–20. Bibcode:2002CBio...12..217C. doi: 10.1016/S0960-9822(01)00680-7 . PMID   11839274. S2CID   18017227.
• Kizhatil K, Wu YX, Sen A, Bennett V (September 2002). "A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin". The Journal of Neuroscience. 22 (18): 7948–58. doi:10.1523/jneurosci.22-18-07948.2002. PMC   6758080 . PMID   12223548.
• Gollan L, Salomon D, Salzer JL, Peles E (December 2003). "Caspr regulates the processing of contactin and inhibits its binding to neurofascin". The Journal of Cell Biology. 163 (6): 1213–8. doi:10.1083/jcb.200309147. PMC   2173730 . PMID   14676309.