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IID00989
 UniprotQ7Z6K5
ProteinArpin
GeneARPIN
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
226
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 211-222 Hetero dimer : Q9H2K2
 Evidence X-RAY 4z68 E Reference
       Region 4z68 E 211-222 order
Seqdisorder 211-226
 Evidence SAXS The above SAXS analysis of unbound Arpin proteins suggests that the C-terminal tail forms an elongated peptide which makes few interactions with the rest of the protein. Reference
       Region 211-226 disorder
SeqProS verified 211-222 Hetero dimer : Q9H2K2
       Region 4z68 E 211-222 order
       Region 211-226 disorder
 
Prediction
NeProc
Disorder 202-226
Order 1-201
ProS 202-205,215-226
AlphaFold
Disorder 1-11,85-92,94-108,177-226
Order 12-84,93-93,109-176
Function
Function in SwissProt
Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence.