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0TENR_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionTenascin-r precursor (tn-r) (restrictin) (janusin).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0007411 axon guidance (NAS)
0007155 cell adhesion (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Fibrinogen plays key roles in both blood clotting and platelet aggregation. During blood clot formation.he conversion of soluble fibrinogen to insoluble fibrin is triggered by thrombin.esulting in the polymerisation of fibrin.hich forms a soft clot; this is then converted to a hard clot by factor XIIIA.hich further cross-links fibrin molecules. Platelet aggregation involves the binding of the platelet protein receptor integrin alpha(IIb)-beta(3) to the C-terminal domain of the fibrinogen gamma chain.ediating a range of adhesive reactions that include adhesion.latelet aggregation and fibrin clot retraction .Fibrinogen occurs as a each monomer is composed of three non-identical chains.lpha.eta and gamma.inked together by several disulphide bonds . The N-terminals of all six chains come together to form the centre of the molecule.rom which the monomers extend in opposite directions as coiled coils.ollowed by C-terminal globular domains. The C-terminal globular domains are referred to as the D regions.hile the coiled-coil and N-terminal central region are referred to as the E region. During clot formation.he N-terminal alpha and beta chains are cleaved.nabling them to bind to the C-terminal gamma and beta chains.espectively.f adjacent molecules.ausing the proteins to polymerise .This entry represents the C-terminal globular domains (D region) of the alpha.eta and gamma chains. These domains are related to domains in other proteins: in the sea cucumber fibrogen-like FreP-A and FreP-B proteins; in the C-terminus of Drosophila scabrous protein that is involved in the regulation of neurogenesis.ossibly through the inhibition of R8 cell differentiation; and in ficolin proteins.hich display lectin activity towards N-acetylglucosamine through their fibrogen-like domains .
  IPR002181:Fibrinogen, alpha/beta/gamma chain, C-terminal globular
Fibronectins are multi-domain glycoproteins found in a soluble form in plasma.nd in an insoluble form in loose connective tissue and basement membranes . They contain multiple copies of 3 repeat regions (types I.I and III).hich bind to a variety of substances including heparin.ollagen.NA.ctin.ibrin and fibronectin receptors on cell surfaces. The wide variety of these substances means that fibronectins are involved in a number of important functions: e.g..ound healing; cell adhesion; blood coagulation; cell differentiation and migration; maintenance of the cellular cytoskeleton; and tumour metastasis . The role of fibronectin in cell differentiation is demonstrated by the marked reduction in the expression of its gene when neoplastic transformation occurs. Cell attachment has been found to be mediated by the binding of the tetrapeptide RGDS to integrins on the cell surface .lthough related sequences can also display cell adhesion activity.Plasma fibronectin occurs as a dimer of 2 different subunits.inked together by 2 disulphide bonds near the C-terminus. The difference in the 2 chains occurs in the type III repeat region and is caused by alternative splicing of the mRNA from one gene . The observation that.n a given protein.n individual repeat of one of the 3 types (e.g..he first FnIII repeat) shows much less similarity to its subsequent tandem repeats within that protein than to its equivalent repeat between fibronectins from other suggested that the repeating structure of fibronectin arose at an early stage of evolution. It also seems to suggest that the structure is subject to high selective pressure .The fibronectin type III repeat region is an approximately 100 amino acid domain.ifferent tandem repeats of which contain binding sites for DNA.eparin and the cell surface . The superfamily of sequences believed to contain FnIII repeats represents 45 different families.he majority of which are involved in cell surface binding in some manner.r are receptor protein tyrosine kinases.r cytokine receptors.
  IPR003961:Fibronectin, type III
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.This entry contains EGF domains found in a variety of extracellular and membrane proteins
  IPR013111:EGF, extracellular
Fibronectin is composed of three repeating structural motifs.f which one is the FnIII module. The three modules form a linear sequence of multiple tandem copies connected by short linker peptides. The secondary structure of the FnIII10 module.hich is the only fibronectin module to possess an integrin binding RGD motif.onsists of two beta-sheets containing the antiparallel beta-strands ABE and DCFG.espectively.hich fold up to form a beta-sandwich. The RGD sequence is located in the loop connecting the beta-strands .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008957:Fibronectin, type III-like fold
SequencesProtein: TENR_HUMAN (1358 aa)
mRNA: NM_003285
Local Annotation
Synapse Ontology
The gaps (approximately 1 micrometer wide) formed between myelin sheath cells along the axons are called Nodes of Ranvier.
sdb:0242 Ranvier node  (Evidence:keywords)
Na channel plays an important role in the course of action potential.
sdb:0287 Na channel  (Evidence:keywords)
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
KO assignmentK06252
  Level 3 annotation:
  Level 2 annotation:
    ECM-receptor interaction
    CAM ligands
    Focal adhesion
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 227 residues, 173558557-173559235Exon2: 56 residues, 173560114-173560278Exon3: 56 residues, 173565832-173565994Exon4: 34 residues, 173571469-173571566Exon5: 52 residues, 173573286-173573438Exon6: 46 residues, 173590149-173590282Exon7: 45 residues, 173591261-173591392Exon8: 50 residues, 173592077-173592221Exon9: 42 residues, 173595370-173595490Exon10: 51 residues, 173598421-173598568Exon11: 42 residues, 173599466-173599586Exon12: 92 residues, 173600768-173601038Exon13: 90 residues, 173601633-173601897Exon14: 32 residues, 173602966-173603056Exon15: 64 residues, 173615310-173615496Exon16: 92 residues, 173621790-173622060Exon17: 52 residues, 173627046-173627197Exon18: 40 residues, 173629538-173629654Exon19: 90 residues, 173632302-173632566Exon20: 161 residues, 173638898-173639375Exon21: 195 residues, 173641974-173642554Exon22: 2 residues, -Jump to TENR_HUMAN  
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