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IID00648
 UniprotP09486
ProteinSPARC
GeneSPARC
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
303
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 70-212,221-303 Hetero tetramer : P02461
 Evidence X-RAY 2v53 A Reference
       Region 2v53 A 70-91 disorder
       Region 2v53 A 92-204 order
       Region 2v53 A 205-212 disorder
       Region 2v53 A 221-222 disorder
       Region 2v53 A 223-302 order
       Region 2v53 A 303-303 disorder
Seq 71-212,221-303 Monomer :
 Evidence X-RAY 1nub B Reference
       Region 1nub B 71-91 disorder
       Region 1nub B 92-208 order
       Region 1nub B 209-212 disorder
       Region 1nub B 221-222 disorder
       Region 1nub B 223-303 order
 Evidence X-RAY 1nub A Reference
       Region 1nub A 71-91 disorder
       Region 1nub A 92-208 order
       Region 1nub A 209-212 disorder
       Region 1nub A 221-222 disorder
       Region 1nub A 223-303 order
Seq 71-303 Homo dimer :
 Evidence X-RAY 1bmo B Reference
       Region 1bmo B 71-91 disorder
       Region 1bmo B 92-303 order
 Evidence X-RAY 1bmo A Reference
       Region 1bmo A 71-91 disorder
       Region 1bmo A 92-303 order
Seq 153-303 Monomer :
 Evidence X-RAY 1sra A Reference
       Region 1sra A 153-303 order
 
Prediction
NeProc
Disorder 1-64
Order 65-303
ProS 1-19,39-55
AlphaFold
Disorder 1-68
Order 69-303
Pfam Hmmer
PF00050 95-149 5.6e-16
SEG 27-43 ,53-69
Function
Function in SwissProt
Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity.