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P97685

- NFASC_RAT

UniProt

P97685 - NFASC_RAT

Protein

Neurofascin

Gene

Nfasc

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (14 Nov 2003)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. protein domain specific binding Source: RGD

    GO - Biological processi

    1. axon guidance Source: InterPro
    2. cell adhesion Source: UniProtKB-KW
    3. myelination Source: BHF-UCL
    4. peripheral nervous system development Source: BHF-UCL
    5. protein targeting to plasma membrane Source: BHF-UCL
    6. synapse organization Source: InterPro
    7. transmission of nerve impulse Source: InterPro

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neurofascin
    Gene namesi
    Name:Nfasc
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620911. Nfasc.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. axon initial segment Source: BHF-UCL
    2. integral component of membrane Source: UniProtKB-KW
    3. intracellular Source: BHF-UCL
    4. node of Ranvier Source: BHF-UCL
    5. plasma membrane Source: Reactome
    6. Schwann cell microvillus Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 12401216NeurofascinPRO_0000015051Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi63 ↔ 118PROSITE-ProRule annotation
    Disulfide bondi162 ↔ 213PROSITE-ProRule annotation
    Disulfide bondi268 ↔ 316PROSITE-ProRule annotation
    Glycosylationi305 – 3051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi358 ↔ 408PROSITE-ProRule annotation
    Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi446 – 4461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi452 ↔ 501PROSITE-ProRule annotation
    Modified residuei481 – 4811PhosphotyrosineBy similarity
    Glycosylationi483 – 4831N-linked (GlcNAc...)Sequence Analysis
    Modified residuei485 – 4851PhosphoserineBy similarity
    Disulfide bondi543 ↔ 592PROSITE-ProRule annotation
    Glycosylationi752 – 7521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi778 – 7781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi866 – 8661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi881 – 8811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1015 – 10151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1026 – 10261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1047 – 10471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1101 – 11011N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Isoform 2/isoform 3 is phosphorylated at P12. Dephosphorylation is required for ankyrin binding.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP97685.
    PRIDEiP97685.

    PTM databases

    PhosphoSiteiP97685.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed at Nodes of Ranvier while isoform 2/isoform 3 is expressed in unmyelinated axons.1 Publication

    Developmental stagei

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

    Gene expression databases

    GenevestigatoriP97685.

    Interactioni

    Subunit structurei

    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/isoform 3 is likely to interact with axonal proteins in close association with CNTNAP1. Interacts with GLDN/gliomedin. Interacts with MYOC By similarity.By similarity

    Protein-protein interaction databases

    BioGridi250572. 2 interactions.
    MINTiMINT-205368.

    Structurei

    3D structure databases

    ProteinModelPortaliP97685.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 11101086ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1132 – 1240109CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1111 – 113121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 13797Ig-like C2-type 1Add
    BLAST
    Domaini143 – 23088Ig-like C2-type 2Add
    BLAST
    Domaini244 – 33289Ig-like C2-type 3Add
    BLAST
    Domaini337 – 42488Ig-like C2-type 4Add
    BLAST
    Domaini429 – 51789Ig-like C2-type 5Add
    BLAST
    Domaini521 – 60383Ig-like C2-type 6Add
    BLAST
    Domaini630 – 72596Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini727 – 82397Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini827 – 92296Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1007 – 109993Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi913 – 100694Thr-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG293951.
    HOGENOMiHOG000231380.
    HOVERGENiHBG000144.
    InParanoidiP97685.
    KOiK06757.
    PhylomeDBiP97685.
    TreeFamiTF351098.

    Family and domain databases

    Gene3Di2.60.40.10. 10 hits.
    InterProiIPR003961. 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]
    PANTHERiPTHR10489:SF41. PTHR10489:SF41. 1 hit.
    PfamiPF13882. Bravo_FIGEY. 1 hit.
    PF00041. fn3. 4 hits.
    PF07679. I-set. 5 hits.
    [Graphical view]
    SMARTiSM00060. FN3. 4 hits.
    SM00409. IG. 2 hits.
    SM00408. IGc2. 4 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 3 hits.
    PROSITEiPS50853. FN3. 4 hits.
    PS50835. IG_LIKE. 6 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P97685-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MARQQAPPWV HVALILFLLS LGGAIEIPMD PSIQNELTQP PTITKQSVKD     50
    HIVDPRDNIL IECEAKGNPA PSFHWTRNSR FFNIAKDPRV SMRRRSGTLV 100
    IDFRSGGRPE EYEGEYQCFA RNKFGTALSN RIRLQVSKSP LWPKENLDPV 150
    VVQEGAPLTL QCNPPPGLPS PVIFWMSSSM EPITQDKRVS QGHNGDLYFS 200
    NVMLQDMQTD YSCNARFHFT HTIQQKNPFT LKVLTTRGVA ERTPSFMYPQ 250
    GTSSSQMVLR GMDLLLECIA SGVPTPDIAW YKKGGDLPSD KAKFENFNKA 300
    LRITNVSEED SGEYFCLASN KMGSIRHTIS VRVKAAPYWL DEPKNLILAP 350
    GEDGRLVCRA NGNPKPTVQW LVNGDPLQSA PPNPNREVAG DTIIFRDTQI 400
    SSRAVYQCNT SNEHGYLLAN AFVSVLDVPP RMLSPRNQLI RVILYNRTRL 450
    DCPFFGSPIP TLRWFKNGQG SNLDGGNYHV YENGSLEIKM IRKEDQGIYT 500
    CVATNILGKA ENQVRLEVKD PTRIYRMPED QVAKRGTTVQ LECRVKHDPS 550
    LKLTVSWLKD DEPLYIGNRM KKEDDSLTIF GVAERDQGSY TCMASTELDQ 600
    DLAKAYLTVL ADQATPTNRL AALPKGRPDR PRDLELTDLA ERSVRLTWIP 650
    GDDNNSPITD YVVQFEEDQF QPGVWHDHSK FPGSVNSAVL HLSPYVNYQF 700
    RVIAVNEVGS SHPSLPSERY RTSGAPPESN PSDVKGEGTR KNNMEITWTP 750
    MNATSAFGPN LRYIVKWRRR ETRETWNNVT VWGSRYVVGQ TPVYVPYEIR 800
    VQAENDFGKG PEPETVIGYS GEDLPSAPRR FRVRQPNLET INLEWDHPEH 850
    PNGILIGYTL RYVPFNGTKL GKQMVENFSP NQTKFSVQRA DPVSRYRFSL 900
    SARTQVGSGE AATEESPTPP NEATPTAAPP TLPPTTVGTT GLVSSTDATA 950
    LAATSEATTV PIIPTVVPTT VATTIATTTT TTAAATTTTT TESPPTTTTG 1000
    TKIHETAPDE QSIWNVTVLP NSKWANITWK HNFRPGTDFV VEYIDSNHTK 1050
    KTVPVKAQAQ PIQLTDLFPG MTYTLRVYSR DNEGISSTVI TFMTSTAYTN 1100
    NQTDIATQGW FIGLMCAIAL LVLILLIVCF IKRSRGGKYP VREKKDVPLG 1150
    PEDPKEEDGS FDYSDEDNKP LQGSQTSLDG TIKQQESDDS LVDYGEGGEG 1200
    QFNEDGSFIG QYTVRKDKEE TEGNESSEAT SPVNAIYSLA 1240
    Length:1,240
    Mass (Da):138,004
    Last modified:November 14, 2003 - v2
    Checksum:i636A187BC3772513
    GO
    Isoform 2 (identifier: P97685-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,189
    Mass (Da):133,776
    Checksum:iC63224BE3EE83B1B
    GO
    Isoform 3 (identifier: P97685-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,174
    Mass (Da):132,228
    Checksum:iB9FF83D9A2C20F30
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti482 – 4821E → Q in AAB47753. (PubMed:8947556)Curated
    Sequence conflicti482 – 4821E → Q in AAB47754. (PubMed:8947556)Curated
    Sequence conflicti675 – 6751W → L in AAB47753. (PubMed:8947556)Curated
    Sequence conflicti675 – 6751W → L in AAB47754. (PubMed:8947556)Curated
    Sequence conflicti699 – 6991Q → D in AAB47753. (PubMed:8947556)Curated
    Sequence conflicti699 – 6991Q → D in AAB47754. (PubMed:8947556)Curated
    Sequence conflicti763 – 7631Y → YY in AAB47753. (PubMed:8947556)Curated
    Sequence conflicti763 – 7631Y → YY in AAB47754. (PubMed:8947556)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei31 – 366Missing in isoform 2 and isoform 3. 2 PublicationsVSP_050416
    Alternative sequencei236 – 2361T → NNPYNDSSLRNHPDIYSA in isoform 2 and isoform 3. 2 PublicationsVSP_050417
    Alternative sequencei611 – 62515Missing in isoform 3. 2 PublicationsVSP_008941Add
    BLAST
    Alternative sequencei824 – 8241L → YPRAAPTEVKIRVLNSTAIS LQWNRVYPDTVQGQLREYRA YYWRESSLLKNLWVSQKRQQ ASFPGDRPRGVVGRLFPYSN YKLEMVVVNGRGDGPRSETK EFTTPEGV in isoform 2 and isoform 3. 2 PublicationsVSP_050418
    Alternative sequencei928 – 1096169Missing in isoform 2 and isoform 3. 2 PublicationsVSP_050419Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY061639 mRNA. Translation: AAL27854.1.
    U81035 mRNA. Translation: AAB47753.1.
    U81036 mRNA. Translation: AAB47754.1.
    RefSeqiNP_001153785.1. NM_001160313.1. [P97685-2]
    NP_001153786.1. NM_001160314.1. [P97685-1]
    NP_446361.1. NM_053909.2. [P97685-3]
    UniGeneiRn.3048.

    Genome annotation databases

    GeneIDi116690.
    KEGGirno:116690.
    UCSCiRGD:620911. rat. [P97685-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY061639 mRNA. Translation: AAL27854.1 .
    U81035 mRNA. Translation: AAB47753.1 .
    U81036 mRNA. Translation: AAB47754.1 .
    RefSeqi NP_001153785.1. NM_001160313.1. [P97685-2 ]
    NP_001153786.1. NM_001160314.1. [P97685-1 ]
    NP_446361.1. NM_053909.2. [P97685-3 ]
    UniGenei Rn.3048.

    3D structure databases

    ProteinModelPortali P97685.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 250572. 2 interactions.
    MINTi MINT-205368.

    PTM databases

    PhosphoSitei P97685.

    Proteomic databases

    PaxDbi P97685.
    PRIDEi P97685.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 116690.
    KEGGi rno:116690.
    UCSCi RGD:620911. rat. [P97685-1 ]

    Organism-specific databases

    CTDi 23114.
    RGDi 620911. Nfasc.

    Phylogenomic databases

    eggNOGi NOG293951.
    HOGENOMi HOG000231380.
    HOVERGENi HBG000144.
    InParanoidi P97685.
    KOi K06757.
    PhylomeDBi P97685.
    TreeFami TF351098.

    Miscellaneous databases

    NextBioi 619556.
    PROi P97685.

    Gene expression databases

    Genevestigatori P97685.

    Family and domain databases

    Gene3Di 2.60.40.10. 10 hits.
    InterProi IPR003961. 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 ]
    PANTHERi PTHR10489:SF41. PTHR10489:SF41. 1 hit.
    Pfami PF13882. Bravo_FIGEY. 1 hit.
    PF00041. fn3. 4 hits.
    PF07679. I-set. 5 hits.
    [Graphical view ]
    SMARTi SM00060. FN3. 4 hits.
    SM00409. IG. 2 hits.
    SM00408. IGc2. 4 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 3 hits.
    PROSITEi PS50853. FN3. 4 hits.
    PS50835. IG_LIKE. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiNFASC_RAT
    AccessioniPrimary (citable) accession number: P97685
    Secondary accession number(s): P97684, Q91Z60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 14, 2003
    Last sequence update: November 14, 2003
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3