Q9M9G7 · CAPZB_ARATH

Function

function

F-actin-capping proteins bind in a Ca2+-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 (By similarity).

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular ComponentF-actin capping protein complex
Molecular Functionactin binding
Biological Processactin cytoskeleton organization
Biological Processactin filament capping
Biological Processactin filament organization
Biological Processbarbed-end actin filament capping
Biological Processresponse to heat

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    F-actin-capping protein subunit beta
  • Alternative names
    • CapZ-beta

Gene names

    • ORF names
      F14O23.17
    • Ordered locus names
      At1g71790

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9M9G7
  • Secondary accessions
    • A0JQ89

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00002046401-256F-actin-capping protein subunit beta

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Component of the F-actin capping complex, composed of a heterodimer of an alpha and a beta subunit.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    256
  • Mass (Da)
    28,877
  • Last updated
    2000-10-01 v1
  • Checksum
    F52E056D67B6C15F
MEAALGLLRRMPPKQSETALSALLSLIPQHSSDLLSQVDLPLQVLRDIESGKDFILCEYNRDADSYRSPWSNKYLPPLEDALYPSSELRKLEVEANDIFAIYRDQYYEGGISSVYMWEDDNEGFVACFLIKKDGSKSGHGRRGCLEEGAWDAIHVIQVGSEEEEMAQYCLTSTIMLSLTTDDESSGKFGLSGSIRRQMKMELAVADGHLCNMGRMIEELEGKLRNSLDQVYFGKTREMVCTLRPPAEIVQMRLPDT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC012654
EMBL· GenBank· DDBJ
AAF43232.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE35233.1
EMBL· GenBank· DDBJ
Genomic DNA
BT029459
EMBL· GenBank· DDBJ
ABK59688.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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