Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P97685 (NFASC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurofascin
Gene names
Name:Nfasc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1240 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell adhesion, ankyrin-binding protein which may be involved in neurite extension, axonal guidance, synaptogenesis, myelination and neuron-glial cell interactions. Isoform 2/isoform3 may be responsible for mediating and signaling axon-glial interaction during the early stages of myelination. Ref.3 Ref.4 Ref.6

Subunit structure

Horseshoe-shaped homodimer By similarity. Probable constituent of a neurofascin/NRCAM/ankyrin G complex. Associates with the sodium channel beta-1 (SCN1B) and beta-3 (SCN3B) subunits. Associates to subunit beta-1 in developing axons as early as postanatal day 5, during the period that nodes of Ranvier are forming. Isoform 2/isoform3 is likely to interact with axonal proteins in close association with CNTNAP1. Interacts with GLDN/gliomedin. Interacts with MYOC By similarity. Ref.2 Ref.5 Ref.6

Subcellular location

Cell membrane; Single-pass type I membrane protein. Note: Isoform 1 colocalizes with ankyrin G at the nodes of Ranvier. Isoform 2/isoform 3 is a glial component of the paranodal axo-glial junction.

Tissue specificity

Isoform 1 is expressed at Nodes of Ranvier while isoform 2/isoform3 is expressed in unmyelinated axons. Ref.4

Developmental stage

Strongly but transiently up-regulated in oligodendrocytes at the onset of myelinogenesis. Once these last have engaged their target exons, expression declines precipitously.

Domain

Homophilic adhesion is primarily mediated by the interaction of the second Ig-like domains By similarity.

Post-translational modification

Isoform 2/isoform3 is phosphorylated at P12. Dephosphorylation is required for ankyrin binding. Ref.4

Sequence similarities

Belongs to the immunoglobulin superfamily. L1/neurofascin/NgCAM family.

Contains 4 fibronectin type-III domains.

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from electronic annotation. Source: InterPro

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

myelination

Inferred from expression pattern PubMed 16652168PubMed 16652168. Source: BHF-UCL

peripheral nervous system development

Inferred from expression pattern PubMed 16652168. Source: BHF-UCL

protein targeting to plasma membrane

Inferred from direct assay PubMed 16525039. Source: BHF-UCL

synapse organization

Inferred from electronic annotation. Source: InterPro

transmission of nerve impulse

Inferred from electronic annotation. Source: InterPro

   Cellular_componentSchwann cell microvillus

Inferred from direct assay PubMed 17045809. Source: RGD

axon initial segment

Inferred from direct assay PubMed 11724816. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular

Inferred from direct assay PubMed 16525039. Source: BHF-UCL

node of Ranvier

Inferred from direct assay PubMed 16652168. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionprotein domain specific binding

Inferred from physical interaction PubMed 17045809. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P97685-1)

Also known as: NF186; 186 kDa isoform;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P97685-2)

Also known as: NF155; 155 kDa isoform;

The sequence of this isoform differs from the canonical sequence as follows:
     31-36: Missing.
     236-236: T → NNPYNDSSLRNHPDIYSA
     824-824: L → YPRAAPTEVK...TKEFTTPEGV
     928-1096: Missing.
Isoform 3 (identifier: P97685-3)

Also known as: NF155; 155 kDa isoform;

The sequence of this isoform differs from the canonical sequence as follows:
     31-36: Missing.
     236-236: T → NNPYNDSSLRNHPDIYSA
     611-625: Missing.
     824-824: L → YPRAAPTEVK...TKEFTTPEGV
     928-1096: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 12401216Neurofascin
PRO_0000015051

Regions

Topological domain25 – 11101086Extracellular Potential
Transmembrane1111 – 113121Helical; Potential
Topological domain1132 – 1240109Cytoplasmic Potential
Domain41 – 13797Ig-like C2-type 1
Domain143 – 23088Ig-like C2-type 2
Domain244 – 33289Ig-like C2-type 3
Domain337 – 42488Ig-like C2-type 4
Domain429 – 51789Ig-like C2-type 5
Domain521 – 60383Ig-like C2-type 6
Domain630 – 72596Fibronectin type-III 1
Domain727 – 82397Fibronectin type-III 2
Domain827 – 92296Fibronectin type-III 3
Domain1007 – 109993Fibronectin type-III 4
Compositional bias913 – 100694Thr-rich

Amino acid modifications

Modified residue4811Phosphotyrosine By similarity
Modified residue4851Phosphoserine By similarity
Glycosylation3051N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4461N-linked (GlcNAc...) Potential
Glycosylation4831N-linked (GlcNAc...) Potential
Glycosylation7521N-linked (GlcNAc...) Potential
Glycosylation7781N-linked (GlcNAc...) Potential
Glycosylation8661N-linked (GlcNAc...) Potential
Glycosylation8811N-linked (GlcNAc...) Potential
Glycosylation10151N-linked (GlcNAc...) Potential
Glycosylation10261N-linked (GlcNAc...) Potential
Glycosylation10471N-linked (GlcNAc...) Potential
Glycosylation11011N-linked (GlcNAc...) Potential
Disulfide bond63 ↔ 118 By similarity
Disulfide bond162 ↔ 213 By similarity
Disulfide bond268 ↔ 316 By similarity
Disulfide bond358 ↔ 408 By similarity
Disulfide bond452 ↔ 501 Potential
Disulfide bond543 ↔ 592 Potential

Natural variations

Alternative sequence31 – 366Missing in isoform 2 and isoform 3.
VSP_050416
Alternative sequence2361T → NNPYNDSSLRNHPDIYSA in isoform 2 and isoform 3.
VSP_050417
Alternative sequence611 – 62515Missing in isoform 3.
VSP_008941
Alternative sequence8241L → YPRAAPTEVKIRVLNSTAIS LQWNRVYPDTVQGQLREYRA YYWRESSLLKNLWVSQKRQQ ASFPGDRPRGVVGRLFPYSN YKLEMVVVNGRGDGPRSETK EFTTPEGV in isoform 2 and isoform 3.
VSP_050418
Alternative sequence928 – 1096169Missing in isoform 2 and isoform 3.
VSP_050419

Experimental info

Sequence conflict4821E → Q in AAB47753. Ref.2
Sequence conflict4821E → Q in AAB47754. Ref.2
Sequence conflict6751W → L in AAB47753. Ref.2
Sequence conflict6751W → L in AAB47754. Ref.2
Sequence conflict6991Q → D in AAB47753. Ref.2
Sequence conflict6991Q → D in AAB47754. Ref.2
Sequence conflict7631Y → YY in AAB47753. Ref.2
Sequence conflict7631Y → YY in AAB47754. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NF186) (186 kDa isoform) [UniParc].

Last modified November 14, 2003. Version 2.
Checksum: 636A187BC3772513

FASTA1,240138,004
        10         20         30         40         50         60 
MARQQAPPWV HVALILFLLS LGGAIEIPMD PSIQNELTQP PTITKQSVKD HIVDPRDNIL 

        70         80         90        100        110        120 
IECEAKGNPA PSFHWTRNSR FFNIAKDPRV SMRRRSGTLV IDFRSGGRPE EYEGEYQCFA 

       130        140        150        160        170        180 
RNKFGTALSN RIRLQVSKSP LWPKENLDPV VVQEGAPLTL QCNPPPGLPS PVIFWMSSSM 

       190        200        210        220        230        240 
EPITQDKRVS QGHNGDLYFS NVMLQDMQTD YSCNARFHFT HTIQQKNPFT LKVLTTRGVA 

       250        260        270        280        290        300 
ERTPSFMYPQ GTSSSQMVLR GMDLLLECIA SGVPTPDIAW YKKGGDLPSD KAKFENFNKA 

       310        320        330        340        350        360 
LRITNVSEED SGEYFCLASN KMGSIRHTIS VRVKAAPYWL DEPKNLILAP GEDGRLVCRA 

       370        380        390        400        410        420 
NGNPKPTVQW LVNGDPLQSA PPNPNREVAG DTIIFRDTQI SSRAVYQCNT SNEHGYLLAN 

       430        440        450        460        470        480 
AFVSVLDVPP RMLSPRNQLI RVILYNRTRL DCPFFGSPIP TLRWFKNGQG SNLDGGNYHV 

       490        500        510        520        530        540 
YENGSLEIKM IRKEDQGIYT CVATNILGKA ENQVRLEVKD PTRIYRMPED QVAKRGTTVQ 

       550        560        570        580        590        600 
LECRVKHDPS LKLTVSWLKD DEPLYIGNRM KKEDDSLTIF GVAERDQGSY TCMASTELDQ 

       610        620        630        640        650        660 
DLAKAYLTVL ADQATPTNRL AALPKGRPDR PRDLELTDLA ERSVRLTWIP GDDNNSPITD 

       670        680        690        700        710        720 
YVVQFEEDQF QPGVWHDHSK FPGSVNSAVL HLSPYVNYQF RVIAVNEVGS SHPSLPSERY 

       730        740        750        760        770        780 
RTSGAPPESN PSDVKGEGTR KNNMEITWTP MNATSAFGPN LRYIVKWRRR ETRETWNNVT 

       790        800        810        820        830        840 
VWGSRYVVGQ TPVYVPYEIR VQAENDFGKG PEPETVIGYS GEDLPSAPRR FRVRQPNLET 

       850        860        870        880        890        900 
INLEWDHPEH PNGILIGYTL RYVPFNGTKL GKQMVENFSP NQTKFSVQRA DPVSRYRFSL 

       910        920        930        940        950        960 
SARTQVGSGE AATEESPTPP NEATPTAAPP TLPPTTVGTT GLVSSTDATA LAATSEATTV 

       970        980        990       1000       1010       1020 
PIIPTVVPTT VATTIATTTT TTAAATTTTT TESPPTTTTG TKIHETAPDE QSIWNVTVLP 

      1030       1040       1050       1060       1070       1080 
NSKWANITWK HNFRPGTDFV VEYIDSNHTK KTVPVKAQAQ PIQLTDLFPG MTYTLRVYSR 

      1090       1100       1110       1120       1130       1140 
DNEGISSTVI TFMTSTAYTN NQTDIATQGW FIGLMCAIAL LVLILLIVCF IKRSRGGKYP 

      1150       1160       1170       1180       1190       1200 
VREKKDVPLG PEDPKEEDGS FDYSDEDNKP LQGSQTSLDG TIKQQESDDS LVDYGEGGEG 

      1210       1220       1230       1240 
QFNEDGSFIG QYTVRKDKEE TEGNESSEAT SPVNAIYSLA 

« Hide

Isoform 2 (NF155) (155 kDa isoform) [UniParc].

Checksum: C63224BE3EE83B1B
Show »

FASTA1,189133,776
Isoform 3 (NF155) (155 kDa isoform) [UniParc].

Checksum: B9FF83D9A2C20F30
Show »

FASTA1,174132,228

References

[1]Tait S., Collinson J.M., Brophy P.J.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Strain: Wistar.
[2]"Molecular composition of the node of Ranvier: identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain-) and NrCAM at nodal axon segments."
Davis J.Q., Lambert S., Bennett V.
J. Cell Biol. 135:1355-1367(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-1240 (ISOFORMS 1; 2 AND 3), SUBUNIT.
Tissue: Brain.
[3]"Transient expression of neurofascin by oligodendrocytes at the onset of myelinogenesis: implications for mechanisms of axon-glial interaction."
Collinson J.M., Marshall D., Gillespie C.S., Brophy P.J.
Glia 23:11-23(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF ISOFORMS 2/3.
[4]"An oligodendrocyte cell adhesion molecule at the site of assembly of the paranodal axo-glial junction."
Tait S., Gunn-Moore F., Collinson J.M., Huang J., Lubetzki C., Pedraza L., Sherman D.L., Colman D.R., Brophy P.J.
J. Cell Biol. 150:657-666(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF ISOFORMS 1 AND 2/3, INDIRECT ASSOCIATION WITH CNTNAP1, PHOSPHORYLATION, TISSUE SPECIFICITY.
[5]"Sodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain."
Ratcliffe C.F., Westenbroek R.E., Curtis R., Catterall W.A.
J. Cell Biol. 154:427-434(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCN1B AND SCN3B.
[6]"Gliomedin mediates Schwann cell-axon interaction and the molecular assembly of the nodes of Ranvier."
Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O., Spiegel I., Bermingham J.R. Jr., Peles E.
Neuron 47:215-229(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GLDN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY061639 mRNA. Translation: AAL27854.1.
U81035 mRNA. Translation: AAB47753.1.
U81036 mRNA. Translation: AAB47754.1.
RefSeqNP_001153785.1. NM_001160313.1.
NP_001153786.1. NM_001160314.1.
NP_446361.1. NM_053909.2.
UniGeneRn.3048.

3D structure databases

ProteinModelPortalP97685.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250572. 2 interactions.
MINTMINT-205368.

PTM databases

PhosphoSiteP97685.

Proteomic databases

PaxDbP97685.
PRIDEP97685.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID116690.
KEGGrno:116690.
UCSCRGD:620911. rat. [P97685-1]

Organism-specific databases

CTD23114.
RGD620911. Nfasc.

Phylogenomic databases

eggNOGNOG293951.
HOGENOMHOG000231380.
HOVERGENHBG000144.
InParanoidP97685.
KOK06757.
PhylomeDBP97685.
TreeFamTF351098.

Enzyme and pathway databases

ReactomeREACT_195021. Developmental Biology.

Gene expression databases

GenevestigatorP97685.

Family and domain databases

Gene3D2.60.40.10. 10 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR026966. Neurofascin/L1/NrCAM_C.
IPR026965. NFASC.
[Graphical view]
PANTHERPTHR10489:SF41. PTHR10489:SF41. 1 hit.
PfamPF13882. Bravo_FIGEY. 1 hit.
PF00041. fn3. 4 hits.
PF07679. I-set. 5 hits.
[Graphical view]
SMARTSM00060. FN3. 4 hits.
SM00409. IG. 2 hits.
SM00408. IGc2. 4 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 3 hits.
PROSITEPS50853. FN3. 4 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio619556.
PROP97685.

Entry information

Entry nameNFASC_RAT
AccessionPrimary (citable) accession number: P97685
Secondary accession number(s): P97684, Q91Z60
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 14, 2003
Last modified: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families