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tenascin-R (TN-R, restrictin, janusin, TNR)
Function:
1) neural extracellular matrix protein
2) interactions with different cells & matrix components
- influences cellular behavior by either evoking a stable adhesion & differentiation, or repulsion & inhibition of neurite growth.
3) binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion
- results in an inhibition of PTK2 phosphorylation & cell detachment
4) binding to membrane surface sulfatides results in oligodendrocyte adhesion & differentiation
5) interaction with CNTN1 induces a repulsion of neurons & an inhibition of neurite outgrowt
6) interacts with SCN2B
- F3 modules 1-2 & 7-9 mediate interaction with SCN2B
7) clustering & regulation of activity of Na+ channels at nodes of Ranvier
8) interacts with BCAN & AGC1 (Ca+2-dependent)
- F3 modules 3-5 mediate interaction with BCAN interacts with SCN2B, PTPRZ1, CSPG3 interacts with CNTN1, TNC, FN1
- EGF-like domains mediate interaction with CNTN1
9) TNR-linked chondroitin sulfate glycosaminoglycans are involved in interaction with FN1 & mediate inhibition of cell adhesion & neurite outgrowth
10) addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development & during synapse maintenance
11) contains N-linked oligosaccharides, O-linked sialylated structures & O-linked chondroitin sulfate glycosaminoglycans
12) contains N-linked oligosaccharides with a sulfated carbohydrate structure
Structure:
- forms oligomers
- contains 5 EGF-like domains.
- contains 1 fibrinogen C-terminal domain
- contains 9 fibronectin F3-modules
Compartment: secreted, extracellular matrix
Alternative splicing: named isoforms=2
Expression:
- brain specific
General
oligomerizing protein
tenascin family
Properties
SIZE: MW = 150 kD
entity length = 1358 aa
COMPARTMENT: plasma membrane
MOTIF: signal sequence {1-31}
N-glycosylation site {N55}
coiled coil {127-157}
cysteine-rich region {155-314}
MOTIF: N-glycosylation site {N180}
EGF domain {188-199}
N-glycosylation site {N198}
EGF domain {219-230}
EGF domain {250-261}
N-glycosylation site {N278}
EGF domain {281-292}
cysteine residue {C292}
MODIFICATION: cysteine residue {C301}
cysteine residue {C297}
MODIFICATION: cysteine residue {C312}
cysteine residue {C301}
MODIFICATION: cysteine residue {C292}
EGF domain {312-323}
MOTIF: cysteine residue {C312}
MODIFICATION: cysteine residue {C297}
cysteine residue {C314}
MODIFICATION: cysteine residue {C323}
cysteine residue {C323}
MODIFICATION: cysteine residue {C314}
fibronectin type III domain or F3 module {325-413}
MOTIF: N-glycosylation site {N392}
fibronectin type III domain or F3 module {414-502}
MOTIF: N-glycosylation site {N470}
fibronectin type III domain or F3 module {503-592}
MOTIF: N-glycosylation site {N581}
fibronectin type III domain or F3 module {593-684}
fibronectin type III domain or F3 module {685-772}
fibronectin type III domain or F3 module {773-862}
MOTIF: N-glycosylation site {N791}
fibronectin type III domain or F3 module {863-951}
MOTIF: N-glycosylation site {N874}
fibronectin type III domain or F3 module {952-1039}
MOTIF: N-glycosylation site {N1036}
fibronectin type III domain or F3 module {1040-1127}
MOTIF: N-glycosylation site {N1046}
FIBRINOGEN C-TERMINAL {1134-1343}
MOTIF: N-glycosylation site {N1261}
Database Correlations
OMIM 601995
UniProt Q92752
PFAM correlations
References
UniProt :accession Q92752