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IID50041
UniprotP19803
ProteinRho GDP-dissociation inhibitor 1
GeneARHGDIA
OrganismBos taurus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
204
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-204 Hetero dimer : IID00274Complex
 Evidence X-RAY 5fr2 B Reference
       Region 5fr2 B 1-24 disorder
       Region 5fr2 B 25-58 order
       Region 5fr2 B 59-60 disorder
       Region 5fr2 B 61-204 order
 Evidence X-RAY 5fr1 B Reference
       Region 5fr1 B 1-25 disorder
       Region 5fr1 B 26-56 order
       Region 5fr1 B 57-66 disorder
       Region 5fr1 B 67-202 order
       Region 5fr1 B 203-204 disorder
Seq 1-204 Hetero dimer : IID00308Complex
 Evidence X-RAY 1doa B Reference
       Region 1doa B 1-4 disorder
       Region 1doa B 5-204 order
Seq 60-204 Monomer :
 Evidence NMR 1gdf A Reference
       Region 1gdf A 60-68 disorder
       Region 1gdf A 69-204 order
 Evidence NMR 1ajw A Reference
       Region 1ajw A 60-68 disorder
       Region 1ajw A 60-66 high_rmsd
       Region 1ajw A 69-204 order
SeqProS possible 6-68 The N-terminal region (1-59) of the human GDI1 is described to be disordered in the free state. (PubMed=11320308, PubMed=9195882) Hetero dimer : IID00308Complex
       Region 1doa B 5-204 order
Seqphosphorylation
    34-34 Phosphoserine
    115-115 Phosphoserine; by PKC
    101-101 Phosphoserine; by PKA
    47-47 Phosphoserine
Seqacetylation
    105-105 N6-acetyllysine
    2-2 N-acetylalanine
    43-43 N6-acetyllysine
    127-127 N6-acetyllysine
    141-141 N6-acetyllysine; alternate
    178-178 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-46
Order 47-204
ProS 5-13,24-46
AlphaFold
Disorder 1-4,20-24,58-63,204-204
Order 5-19,25-57,64-203
Pfam Hmmer
PF02115 1-204 1.1e-165
Function
Function in SwissProt
Controls Rho proteins homeostasis. Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Retains Rho proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool, regulating their stability and protecting them from degradation. Actively involved in the recycling and distribution of activated Rho GTPases in the cell, mediates extraction from membranes of both inactive and activated molecules due its exceptionally high affinity for prenylated forms. Through the modulation of Rho proteins, may play a role in cell motility regulation. In glioma cells, inhibits cell migration and invasion by mediating the signals of SEMA5A and PLXNB3 that lead to inactivation of RAC1.