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IID00122
UniprotP52907
ProteinF-actin-capping protein subunit alpha-1
GeneCAPZA1
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
286
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 265-276 Hetero tetramer : IID50019Complex
 Evidence NMR 1mwn Y Reference
       Region 1mwn Y 265-276 order
 Evidence NMR 1mwn X Reference
       Region 1mwn X 265-276 order
Seqdisorder 265-276
 Evidence CD Reference
       Region 265-276 disorder
Seq 265-276 Hetero tetramer : IID00410Complex
 Evidence NMR 1mq1 D Reference
       Region 1mq1 D 265-276 order
 Evidence NMR 1mq1 C Reference
       Region 1mq1 C 265-276 order
SeqProS verified 265-276 Hetero tetramer : IID50019Complex
       Region 1mwn X 265-276 order
       Region 1mwn Y 265-276 order
       Region 265-276 disorder
SeqProS verified 265-276 Hetero tetramer : IID00410Complex
       Region 1mq1 C 265-276 order
       Region 1mq1 D 265-276 order
       Region 265-276 disorder
Seqphosphorylation
    9-9 Phosphoserine
Seqacetylation
    97-97 N6-acetyllysine
    19-19 N6-acetyllysine
    2-2 N-acetylalanine
 
Prediction
NeProc
Disorder 1-8,285-286
Order 9-284
ProS 5-8,285-286
AlphaFold
Disorder 1-6,279-279,283-286
Order 7-278,280-282
Pfam Hmmer
PF01267 12-282 9.1e-186
SEG 34-47
Function
Function in SwissProt
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions.
Biological Process
See also
Diagram with PDB data
S100B/S100BCALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES