LMPD Database

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LMP002276

UniProt Annotations

Entry Information
Gene Nametenascin R
Protein EntryTENR_MOUSE
UniProt IDQ8BYI9
SpeciesMouse
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; Synonyms=J1-180, TN-R 180; IsoId=Q8BYI9-1; Sequence=Displayed; Name=2; Synonyms=J1-160, TN-R 160; IsoId=Q8BYI9-2; Sequence=VSP_012994;
Developmental StageIsoform 1 is barely detectable at E17 embryo and increases in intensity until postnatal day 15, when it reaches adult levels. Isoform 2 is detectable from postnatal day 5 and reaches adult levels also at postnatal day 15. {ECO:0000269|PubMed:2477380}.
DomainThe EGF-like domains mediate interaction with CNTN1. The fibronectin type-III domains 3-5 mediate interaction with BCAN. The fibronectin type-III domains 1-2 and 7-9 mediate interaction with SCN2B (By similarity). {ECO:0000250}.
FunctionNeural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. Theses interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediates inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance (By similarity). {ECO:0000250}.
MiscellaneousKnockout mice display alterations of the extracellular matrix, and decreased axonal conduction velocities in the CNS.
PtmContains N-linked oligosaccharides with a sulfated carbohydrate structures (By similarity). Contains N-linked oligosaccharides, O-linked sialylated structures and O-linked chondroitin sulfate glycosaminoglycans. {ECO:0000250, ECO:0000269|PubMed:10406848, ECO:0000269|PubMed:10773191}.
SimilarityBelongs to the tenascin family. {ECO:0000305}.
SimilarityContains 1 fibrinogen C-terminal domain. {ECO:0000255|PROSITE-ProRule:PRU00739}.
SimilarityContains 5 EGF-like domains. {ECO:0000305}.
SimilarityContains 9 fibronectin type-III domains. {ECO:0000255|PROSITE-ProRule:PRU00316}.
Subcellular LocationSecreted, extracellular space, extracellular matrix.
SubunitInteracts with BCAN and ACAN in a calcium-dependent manner. Interacts with SCN2B, PTPRZ1, and CSPG3 (By similarity). Forms oligomers. Isoforms 1 and 2 form respectively trimeric (tribrachion) and dimeric kink-armed rodlike structures, which are linked by disulfide bridges. Interacts with CNTN1, TNC and FN1. {ECO:0000250, ECO:0000269|PubMed:10773191, ECO:0000269|PubMed:7678967}.
Tissue SpecificityBrain-specific. {ECO:0000269|PubMed:2477380}.