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{{Infobox_gene}}
{{PBB_Controls
'''Neurofascin''' is a [[protein]] that in humans is encoded by the ''NFASC'' [[gene]].<ref name="pmid1377696">{{cite journal | vauthors = Volkmer H, Hassel B, Wolff JM, Frank R, Rathjen FG | title = Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily | journal = The Journal of Cell Biology | volume = 118 | issue = 1 | pages = 149–61 | date = July 1992 | pmid = 1377696 | pmc = 2289533 | doi = 10.1083/jcb.118.1.149 }}</ref><ref name="pmid8672144">{{cite journal | vauthors = Burmeister M, Ren Q, Makris GJ, Samson D, Bennett V | title = Genes for the neuronal immunoglobulin domain cell adhesion molecules neurofascin and Nr-CAM map to mouse chromosomes 1 and 12 and homologous human chromosomes | journal = Mammalian Genome | volume = 7 | issue = 7 | pages = 558–9 | date = July 1996 | pmid = 8672144 | pmc =  | doi = 10.1007/s003359900168 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: NFASC neurofascin homolog (chicken)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23114| access-date = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Neurofascin homolog (chicken)
| HGNCid = 29866
| Symbol = NFASC
| AltSymbols =; DKFZp686P2250; FLJ46866; KIAA0756; NF; NRCAML
| OMIM = 609145
| ECnumber = 
| Homologene = 24945
| MGIid = 104753
| GeneAtlas_image1 = PBB_GE_NFASC_213438_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030424 |text = axon}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007411 |text = axon guidance}} {{GNF_GO|id=GO:0050808 |text = synapse organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 23114
    | Hs_Ensembl = ENSG00000163531
    | Hs_RefseqProtein = NP_055905
    | Hs_RefseqmRNA = NM_015090
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 203064402
    | Hs_GenLoc_end = 203258587
    | Hs_Uniprot = O94856
    | Mm_EntrezGene = 269116
    | Mm_Ensembl = ENSMUSG00000026442
    | Mm_RefseqmRNA = NM_182716
    | Mm_RefseqProtein = NP_874385
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 134396796
    | Mm_GenLoc_end = 134534872
    | Mm_Uniprot = Q6P6Q1
  }}
}}
'''Neurofascin homolog (chicken)''', also known as '''NFASC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NFASC neurofascin homolog (chicken)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23114| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Neurofascin is an [[L1 family]] immunoglobulin [[cell adhesion molecule]] (see [[L1CAM]]) involved in [[axon]] subcellular targeting and [[synapse]] formation during [[neural development]].<ref name="entrez"/><ref name="pmid15479642">{{cite journal | vauthors = Ango F, di Cristo G, Higashiyama H, Bennett V, Wu P, Huang ZJ | title = Ankyrin-based subcellular gradient of neurofascin, an immunoglobulin family protein, directs GABAergic innervation at purkinje axon initial segment | journal = Cell | volume = 119 | issue = 2 | pages = 257–72 | date = October 2004 | pmid = 15479642 | doi = 10.1016/j.cell.2004.10.004 }}</ref>
{{PBB_Summary
| section_title =
| summary_text = Neurofascin is an L1 family immunoglobulin cell adhesion molecule (see L1CAM; MIM 308840) involved in axon subcellular targeting and synapse formation during neural development (Ango et al., 2004).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NFASC neurofascin homolog (chicken)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23114| accessdate = }}</ref>
}}


==References==
==Clinical importance==
{{reflist|2}}
 
==Further reading==
A homozygous mutation causing loss of Nfasc155 causes severe congenital hypotonia, contractures of fingers and toes and no reaction to touch or pain.<ref name=Smigiel2018>{{cite journal | vauthors = 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 | title = Homozygous mutation in the Neurofascin gene affecting the glial isoform of Neurofascin causes severe neurodevelopment disorder with hypotonia, amimia and areflexia | journal = Human Molecular Genetics | volume =  | issue =  | date = August 2018 | pmid = 30124836 | doi = 10.1093/hmg/ddy277 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Hortsch M | title = The L1 family of neural cell adhesion molecules: old proteins performing new tricks | journal = Neuron | volume = 17 | issue = 4 | pages = 587–93 | date = October 1996 | pmid = 8893017 | doi = 10.1016/S0896-6273(00)80192-0 }}
| citations =
* {{cite journal | vauthors = Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T | title = Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones | journal = DNA Research | volume = 9 | issue = 3 | pages = 99–106 | date = June 2002 | pmid = 12168954 | doi = 10.1093/dnares/9.3.99 }}
*{{cite journal | author=Hortsch M |title=The L1 family of neural cell adhesion molecules: old proteins performing new tricks. |journal=Neuron |volume=17 |issue= 4 |pages= 587-93 |year= 1996 |pmid= 8893017 |doi= }}
* {{cite journal | vauthors = Tuvia S, Garver TD, Bennett V | title = The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 24 | pages = 12957–62 | date = November 1997 | pmid = 9371782 | pmc = 24245 | doi = 10.1073/pnas.94.24.12957 }}
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
* {{cite journal | vauthors = Ren Q, Bennett V | title = Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules | journal = Journal of Neurochemistry | volume = 70 | issue = 5 | pages = 1839–49 | date = May 1998 | pmid = 9572267 | doi = 10.1046/j.1471-4159.1998.70051839.x }}
*{{cite journal  | author=Volkmer H, Hassel B, Wolff JM, ''et al.'' |title=Structure of the axonal surface recognition molecule neurofascin and its relationship to a neural subgroup of the immunoglobulin superfamily. |journal=J. Cell Biol. |volume=118 |issue= 1 |pages= 149-61 |year= 1992 |pmid= 1377696 |doi=  }}
* {{cite journal | vauthors = Zhang X, Davis JQ, Carpenter S, Bennett V | title = Structural requirements for association of neurofascin with ankyrin | journal = The Journal of Biological Chemistry | volume = 273 | issue = 46 | pages = 30785–94 | date = November 1998 | pmid = 9804856 | doi = 10.1074/jbc.273.46.30785 }}
*{{cite journal | author=Burmeister M, Ren Q, Makris GJ, ''et al.'' |title=Genes for the neuronal immunoglobulin domain cell adhesion molecules neurofascin and Nr-CAM map to mouse chromosomes 1 and 12 and homologous human chromosomes. |journal=Mamm. Genome |volume=7 |issue= 7 |pages= 558-9 |year= 1996 |pmid= 8672144 |doi=  }}
* {{cite journal | vauthors = Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O | title = 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 | journal = DNA Research | volume = 5 | issue = 5 | pages = 277–86 | date = October 1998 | pmid = 9872452 | doi = 10.1093/dnares/5.5.277 }}
*{{cite journal  | author=Tuvia S, Garver TD, Bennett V |title=The phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 24 |pages= 12957-62 |year= 1998 |pmid= 9371782 |doi= }}
* {{cite journal | vauthors = Koroll M, Rathjen FG, Volkmer H | title = The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity | journal = The Journal of Biological Chemistry | volume = 276 | issue = 14 | pages = 10646–54 | date = April 2001 | pmid = 11152476 | doi = 10.1074/jbc.M010647200 }}
*{{cite journal | author=Ren Q, Bennett V |title=Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules. |journal=J. Neurochem. |volume=70 |issue= 5 |pages= 1839-49 |year= 1998 |pmid= 9572267 |doi= }}
* {{cite journal | vauthors = Ratcliffe CF, Westenbroek RE, Curtis R, Catterall WA | title = Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain | journal = The Journal of Cell Biology | volume = 154 | issue = 2 | pages = 427–34 | date = July 2001 | pmid = 11470829 | pmc = 2150779 | doi = 10.1083/jcb.200102086 }}
*{{cite journal | author=Zhang X, Davis JQ, Carpenter S, Bennett V |title=Structural requirements for association of neurofascin with ankyrin. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30785-94 |year= 1998 |pmid= 9804856 |doi= }}
* {{cite journal | vauthors = Jenkins SM, Kizhatil K, Kramarcy NR, Sen A, Sealock R, Bennett V | title = FIGQY phosphorylation defines discrete populations of L1 cell adhesion molecules at sites of cell-cell contact and in migrating neurons | journal = Journal of Cell Science | volume = 114 | issue = Pt 21 | pages = 3823–35 | date = November 2001 | pmid = 11719549 | doi =  }}
*{{cite journal | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=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. |journal=DNA Res. |volume=5 |issue= 5 |pages= 277-86 |year= 1999 |pmid= 9872452 |doi= }}
* {{cite journal | vauthors = Jenkins SM, Bennett V | title = Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments | journal = The Journal of Cell Biology | volume = 155 | issue = 5 | pages = 739–46 | date = November 2001 | pmid = 11724816 | pmc = 2150881 | doi = 10.1083/jcb.200109026 }}
*{{cite journal | author=Koroll M, Rathjen FG, Volkmer H |title=The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activity. |journal=J. Biol. Chem. |volume=276 |issue= 14 |pages= 10646-54 |year= 2001 |pmid= 11152476 |doi= 10.1074/jbc.M010647200 }}
* {{cite journal | vauthors = Charles P, Tait S, Faivre-Sarrailh C, Barbin G, Gunn-Moore F, Denisenko-Nehrbass N, Guennoc AM, Girault JA, Brophy PJ, Lubetzki C | title = Neurofascin is a glial receptor for the paranodin/Caspr-contactin axonal complex at the axoglial junction | journal = Current Biology | volume = 12 | issue = 3 | pages = 217–20 | date = February 2002 | pmid = 11839274 | doi = 10.1016/S0960-9822(01)00680-7 }}
*{{cite journal | author=Ratcliffe CF, Westenbroek RE, Curtis R, Catterall WA |title=Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain. |journal=J. Cell Biol. |volume=154 |issue= 2 |pages= 427-34 |year= 2001 |pmid= 11470829 |doi= }}
* {{cite journal | vauthors = Kizhatil K, Wu YX, Sen A, Bennett V | title = A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin | journal = The Journal of Neuroscience | volume = 22 | issue = 18 | pages = 7948–58 | date = September 2002 | pmid = 12223548 | doi =  }}
*{{cite journal | author=Jenkins SM, Kizhatil K, Kramarcy NR, ''et al.'' |title=FIGQY phosphorylation defines discrete populations of L1 cell adhesion molecules at sites of cell-cell contact and in migrating neurons. |journal=J. Cell. Sci. |volume=114 |issue= Pt 21 |pages= 3823-35 |year= 2002 |pmid= 11719549 |doi=  }}
* {{cite journal | vauthors = Gollan L, Salomon D, Salzer JL, Peles E | title = Caspr regulates the processing of contactin and inhibits its binding to neurofascin | journal = The Journal of Cell Biology | volume = 163 | issue = 6 | pages = 1213–8 | date = December 2003 | pmid = 14676309 | pmc = 2173730 | doi = 10.1083/jcb.200309147 }}
*{{cite journal | author=Jenkins SM, Bennett V |title=Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments. |journal=J. Cell Biol. |volume=155 |issue= 5 |pages= 739-46 |year= 2002 |pmid= 11724816 |doi= 10.1083/jcb.200109026 }}
*{{cite journal | author=Charles P, Tait S, Faivre-Sarrailh C, ''et al.'' |title=Neurofascin is a glial receptor for the paranodin/Caspr-contactin axonal complex at the axoglial junction. |journal=Curr. Biol. |volume=12 |issue= 3 |pages= 217-20 |year= 2002 |pmid= 11839274 |doi= }}
*{{cite journal | author=Kizhatil K, Wu YX, Sen A, Bennett V |title=A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin. |journal=J. Neurosci. |volume=22 |issue= 18 |pages= 7948-58 |year= 2002 |pmid= 12223548 |doi=  }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Gollan L, Salomon D, Salzer JL, Peles E |title=Caspr regulates the processing of contactin and inhibits its binding to neurofascin. |journal=J. Cell Biol. |volume=163 |issue= 6 |pages= 1213-8 |year= 2004 |pmid= 14676309 |doi= 10.1083/jcb.200309147 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Ango F, di Cristo G, Higashiyama H, ''et al.'' |title=Ankyrin-based subcellular gradient of neurofascin, an immunoglobulin family protein, directs GABAergic innervation at purkinje axon initial segment. |journal=Cell |volume=119 |issue= 2 |pages= 257-72 |year= 2004 |pmid= 15479642 |doi= 10.1016/j.cell.2004.10.004 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
[[Category:Human proteins]]
{{WikiDoc Sources}}
 
{{gene-1-stub}}

Latest revision as of 08:46, 21 August 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Neurofascin is a protein that in humans is encoded by the NFASC gene.[1][2][3]

Function

Neurofascin is an L1 family immunoglobulin cell adhesion molecule (see L1CAM) involved in axon subcellular targeting and synapse formation during neural development.[3][4]

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.[5]

References

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: NFASC neurofascin homolog (chicken)".
  4. ↑ 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.
  5. ↑ 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. doi:10.1093/hmg/ddy277. PMID 30124836.

Further reading

Retrieved from "https://www.wikidoc.org/index.php?title=NFASC&oldid=1530610"