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IID90046
UniprotP03524
ProteinGlycoprotein
GeneG
OrganismRabies virus (strain ERA)
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
524
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 512-524 Hetero dimer : IID00656Complex
 Evidence X-RAY 3nfk D Reference
       Region 3nfk D 512-519 disorder
       Region 3nfk D 520-524 order
Seq 512-524 Hetero dimer : IID00656Complex
 Evidence X-RAY 3nfk C Reference
       Region 3nfk C 512-524 order
SeqProS possible 512-524 PDZ binding motif (Class I) ; this region is predicted to be disordered by ColabFold (pLDDT <68.5) and NeProc. Hetero dimer : IID00656Complex
       Region 3nfk C 512-524 order
SeqProS possible 512-524 PDZ binding motif (Class I) ; this region is predicted to be disordered by ColabFold (pLDDT <68.5) and NeProc. Hetero dimer : IID00656Complex
       Region 3nfk D 520-524 order
 
Prediction
NeProc
Disorder 1-4,477-524
Order 5-476
ProS 1-4,477-487,496-524
SEG 6-16 ,288-303
Function
Function in SwissProt
Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane. There is convincing in vitro evidence that the muscular form of the nicotinic acetylcholine receptor (nAChR), the neuronal cell adhesion molecule (NCAM), and the p75 neurotrophin receptor (p75NTR) bind glycoprotein and thereby facilitate rabies virus entry into cells.