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IID00965
 UniprotQ01344
ProteinInterleukin-5 receptor subunit alpha
GeneIL5RA
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
420
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 20-335 Hetero trimer : P05113
 Evidence X-RAY 3qt2 A Reference
       Region 3qt2 A 20-26 disorder
       Region 3qt2 A 27-333 order
       Region 3qt2 A 334-335 disorder
 Evidence X-RAY 3qt2 B Reference
       Region 3qt2 B 20-27 disorder
       Region 3qt2 B 28-334 order
       Region 3qt2 B 335-335 disorder
 Evidence X-RAY 3va2 C Reference
       Region 3va2 C 21-26 disorder
       Region 3va2 C 27-333 order
       Region 3va2 C 334-335 disorder
Seq 27-332 Hetero dimer :
 Evidence X-RAY 6h41 A Reference
       Region 6h41 A 27-332 order
Seq 413-420 Hetero tetramer : O00560
 Evidence X-RAY 1obx B Reference
       Region 1obx B 413-416 disorder
       Region 1obx B 417-420 order
Seq 413-420 Hetero trimer : O00560
 Evidence X-RAY 1obz P Reference
       Region 1obz P 413-416 disorder
       Region 1obz P 417-420 order
SeqProS possible 417-420 This region is predicted to be disordered by AlphaFold (pLDDT <68.5) and NeProc; PDZ binding motif (Class I) Hetero trimer : O00560
       Region 1obz P 417-420 order
SeqProS possible 417-420 This region is predicted to be disordered by AlphaFold (pLDDT <68.5) and NeProc; PDZ binding motif (Class I) Hetero tetramer : O00560
       Region 1obx B 417-420 order
 
Prediction
NeProc
Disorder 1-27,112-117,335-341,362-382,390-420
Order 28-111,118-334,342-361,383-389
ProS 1-27,112-117,335-341,362-382,390-394,401-420
AlphaFold
Disorder 1-27,58-60,143-147,335-341,368-420
Order 28-57,61-142,148-334,342-367
SEG 107-120 ,351-367
Function
Function in SwissProt
Cell surface receptor that plays an important role in the survival, differentiation, and chemotaxis of eosinophils (PubMed:9378992). Acts by forming an heterodimeric receptor with CSF2RB subunit and subsequently binding to interleukin-5 (PubMed:1495999, PubMed:22528658). In unstimulated conditions, interacts constitutively with JAK2. Heterodimeric receptor activation leads to JAK2 stimulation and subsequent activation of the JAK-STAT pathway (PubMed:9516124).