P05095 · ACTNA_DICDI

Function

function

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Increases the actin-stimulated ATPase activity of myosin. Involved in vegetative cell growth, phagocytosis, motility and development, probably through stabilization of the actin network in the cortical cytoskeleton.

Features

Showing features for binding site.

1861100200300400500600700800
TypeIDPosition(s)Description
Binding site742Ca2+ 1 (UniProtKB | ChEBI)
Binding site744Ca2+ 1 (UniProtKB | ChEBI)
Binding site746Ca2+ 1 (UniProtKB | ChEBI)
Binding site748Ca2+ 1 (UniProtKB | ChEBI)
Binding site753Ca2+ 1 (UniProtKB | ChEBI)
Binding site778Ca2+ 2 (UniProtKB | ChEBI)
Binding site780Ca2+ 2 (UniProtKB | ChEBI)
Binding site782Ca2+ 2 (UniProtKB | ChEBI)
Binding site784Ca2+ 2 (UniProtKB | ChEBI)
Binding site789Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentactin filament
Cellular Componentcell cortex
Cellular Componentcell junction
Cellular Componentcell leading edge
Cellular Componentcell projection
Cellular Componentcontractile vacuole
Cellular Componentcortical actin cytoskeleton
Cellular Componentcytosol
Cellular Componentextracellular matrix
Cellular Componentmacropinocytic cup
Cellular Componentphagocytic vesicle
Cellular Componentpseudopodium
Molecular Functionactin filament binding
Molecular Functioncalcium ion binding
Molecular Functionprotein-macromolecule adaptor activity
Molecular Functionstructural constituent of cytoskeleton
Biological Processactin crosslink formation
Biological Processactin cytoskeleton organization
Biological Processactin filament bundle assembly
Biological Processcell motility
Biological Processcellular response to starvation
Biological Processhyperosmotic response
Biological Processphagocytosis
Biological Processsorocarp development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-actinin A
  • Alternative names
    • Actin-binding protein A
    • F-actin cross-linking protein

Gene names

    • Name
      abpA
    • Synonyms
      actnA
    • ORF names
      DDB_G0268632

Organism names

Accessions

  • Primary accession
    P05095
  • Secondary accessions
    • Q55EP1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Cells show a minor impairment of growth under conditions of reduced temperature and hyperosmotic stress. Fruiting body development and spore production on soil plates is strongly impaired in mutants lacking abpA, but is only mildly affected in mutants on agar plates. Double mutants lacking both abpA and abpC show a marked reduction in growth, cell size and resistance to osmotic shock, and decreased motility and phagocytosis rates. Development is blocked at the tip stage of aggregation, although expression of developmentally regulated genes does not appear to be affected. Double mutants lacking abpA and abpB show a significant reduction in growth and a slight reduction in motility. Development appears to proceed normally until culmination when aberrant fruiting bodies are formed. The phenotypes of the double mutants suggests a partial redundancy in the microfilament system.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis742Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-744; A-746 and A-753.
Mutagenesis744Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-746 and A-753.
Mutagenesis746Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-753.
Mutagenesis753Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-746.
Mutagenesis778Decreases sensitivity to inhibition by calcium; when associated with A-780; A-786 and A-789.
Mutagenesis780Decreases sensitivity to inhibition by calcium; when associated with A-778; A-786 and A-789.
Mutagenesis786Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-789.
Mutagenesis789Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-786.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000734451-861Alpha-actinin A

Proteomic databases

Expression

Developmental stage

Expressed throughout development. Levels increase during aggregation (1-6 hours) and are then maintained until late culmination when they start to decrease.

Interaction

Subunit

Homodimer; antiparallel.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, repeat.

TypeIDPosition(s)Description
Region1-239Actin-binding
Domain22-127Calponin-homology (CH) 1
Domain136-242Calponin-homology (CH) 2
Repeat240-365Spectrin 1
Repeat366-480Spectrin 2
Repeat481-601Spectrin 3
Repeat602-714Spectrin 4
Domain729-764EF-hand 1
Domain765-800EF-hand 2

Sequence similarities

Belongs to the alpha-actinin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    861
  • Mass (Da)
    97,358
  • Last updated
    2007-03-20 v2
  • Checksum
    17F4364B8059EAFA
MSEEPTPVSGNDKQLLNKAWEITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKTPKLRIHNIQNVGLCLKHIESHGVKLVGIGAEELVDKNLKMTLGMIWTIILRFAIQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFSASRKAETAGKQVGKVLDTFMLLEQTKSDYLKRANELVQWINDKQASLESRDFGDSIESVQSFMNAHKEYKKTEKPPKGQEVSELEAIYNSLQTKLRLIKREPFVAPAGLTPNEIDSTWSALEKAEQEHAEALRIELKRQKKIAVLLQKYNRILKKLENWATTKSVYLGSNETGDSITAVQAKLKNLEAFDGECQSLEGQSNSDLLSILAQLTELNYNGVPELTERKDTFFAQQWTGVKSSAETYKNTLLAELERLQKIEDSLVEFAKRAAQLNVWIEAADDHVFDPINVDSVQGVQEIQEKFDAFLHDQSQQFAELEALAALTQQLRELGRSENDYSVISYDELSAKWNNLLAGIEERKVQLANELTTQTNNDVLCQSFSVKANEISDYVRVTLDAISQNTSSDPQEQLNNIRAIITAHAEKKPELDELYTIASQLEEAQVVDNKHTQHSLESIKLKWDKLNTLAKKNEQVVEGEILAKQLTGVTAEELSEFKACFSHFDKDNDNKLNRLEFSSCLKSIGDELTEEQLNQVISKIDTDGNGTISFEEFIDYMVSSRKGTDSVESTKAAFKVMAEDKDFITEAQIRAAISDSKQIDYLLASMPAVEGGFDYNSFAEKLYQ

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict78in Ref. 1; CAA68685
Sequence conflict359in Ref. 3; CAA27855
Sequence conflict500in Ref. 3; CAA27855
Sequence conflict675in Ref. 1; CAA68685
Sequence conflict696in Ref. 1; CAA68685

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Y00689
EMBL· GenBank· DDBJ
CAA68685.1
EMBL· GenBank· DDBJ
mRNA
AAFI02000004
EMBL· GenBank· DDBJ
EAL72905.1
EMBL· GenBank· DDBJ
Genomic DNA
X04324
EMBL· GenBank· DDBJ
CAA27855.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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