P05095 · ACTNA_DICDI
- ProteinAlpha-actinin A
- GeneabpA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids861 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 742 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 744 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 746 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 748 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 753 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 778 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 780 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 782 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 784 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 789 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | actin filament | |
Cellular Component | cell cortex | |
Cellular Component | cell junction | |
Cellular Component | cell leading edge | |
Cellular Component | cell projection | |
Cellular Component | contractile vacuole | |
Cellular Component | cortical actin cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | extracellular matrix | |
Cellular Component | macropinocytic cup | |
Cellular Component | phagocytic vesicle | |
Cellular Component | pseudopodium | |
Molecular Function | actin filament binding | |
Molecular Function | calcium ion binding | |
Molecular Function | protein-macromolecule adaptor activity | |
Molecular Function | structural constituent of cytoskeleton | |
Biological Process | actin crosslink formation | |
Biological Process | actin cytoskeleton organization | |
Biological Process | actin filament bundle assembly | |
Biological Process | cell motility | |
Biological Process | cellular response to starvation | |
Biological Process | hyperosmotic response | |
Biological Process | phagocytosis | |
Biological Process | sorocarp development |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-actinin A
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Amoebozoa > Evosea > Eumycetozoa > Dictyostelia > Dictyosteliales > Dictyosteliaceae > Dictyostelium
Accessions
- Primary accessionP05095
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Expressed diffusely throughout the cytoplasm. Accumulates in the cell cortex, contractile vesicle and phagosome.
Keywords
- Cellular component
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 742 | Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-744; A-746 and A-753. | ||||
Sequence: D → A | ||||||
Mutagenesis | 744 | Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-746 and A-753. | ||||
Sequence: D → A | ||||||
Mutagenesis | 746 | Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-753. | ||||
Sequence: D → A | ||||||
Mutagenesis | 753 | Abolishes cross-linking activity and reduces calcium binding by 55%; when associated with A-742; A-744 and A-746. | ||||
Sequence: E → A | ||||||
Mutagenesis | 778 | Decreases sensitivity to inhibition by calcium; when associated with A-780; A-786 and A-789. | ||||
Sequence: D → A | ||||||
Mutagenesis | 780 | Decreases sensitivity to inhibition by calcium; when associated with A-778; A-786 and A-789. | ||||
Sequence: D → A | ||||||
Mutagenesis | 786 | Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-789. | ||||
Sequence: S → A | ||||||
Mutagenesis | 789 | Decreases sensitivity to inhibition by calcium; when associated with A-778; A-780 and A-786. | ||||
Sequence: E → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000073445 | 1-861 | Alpha-actinin A | |||
Sequence: MSEEPTPVSGNDKQLLNKAWEITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKTPKLRIHNIQNVGLCLKHIESHGVKLVGIGAEELVDKNLKMTLGMIWTIILRFAIQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFSASRKAETAGKQVGKVLDTFMLLEQTKSDYLKRANELVQWINDKQASLESRDFGDSIESVQSFMNAHKEYKKTEKPPKGQEVSELEAIYNSLQTKLRLIKREPFVAPAGLTPNEIDSTWSALEKAEQEHAEALRIELKRQKKIAVLLQKYNRILKKLENWATTKSVYLGSNETGDSITAVQAKLKNLEAFDGECQSLEGQSNSDLLSILAQLTELNYNGVPELTERKDTFFAQQWTGVKSSAETYKNTLLAELERLQKIEDSLVEFAKRAAQLNVWIEAADDHVFDPINVDSVQGVQEIQEKFDAFLHDQSQQFAELEALAALTQQLRELGRSENDYSVISYDELSAKWNNLLAGIEERKVQLANELTTQTNNDVLCQSFSVKANEISDYVRVTLDAISQNTSSDPQEQLNNIRAIITAHAEKKPELDELYTIASQLEEAQVVDNKHTQHSLESIKLKWDKLNTLAKKNEQVVEGEILAKQLTGVTAEELSEFKACFSHFDKDNDNKLNRLEFSSCLKSIGDELTEEQLNQVISKIDTDGNGTISFEEFIDYMVSSRKGTDSVESTKAAFKVMAEDKDFITEAQIRAAISDSKQIDYLLASMPAVEGGFDYNSFAEKLYQ |
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
Structure
Family & Domains
Features
Showing features for region, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-239 | Actin-binding | ||||
Sequence: MSEEPTPVSGNDKQLLNKAWEITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKTPKLRIHNIQNVGLCLKHIESHGVKLVGIGAEELVDKNLKMTLGMIWTIILRFAIQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDVSDMLDVVRPDERSVMTYVAQYYH | ||||||
Domain | 22-127 | Calponin-homology (CH) 1 | ||||
Sequence: ITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKTPKLRIHNIQNVGLCLKHIESHGVKLVGIGAEELVDKNLKMTLGMIWTIILRFA | ||||||
Domain | 136-242 | Calponin-homology (CH) 2 | ||||
Sequence: LSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFS | ||||||
Repeat | 240-365 | Spectrin 1 | ||||
Sequence: HFSASRKAETAGKQVGKVLDTFMLLEQTKSDYLKRANELVQWINDKQASLESRDFGDSIESVQSFMNAHKEYKKTEKPPKGQEVSELEAIYNSLQTKLRLIKREPFVAPAGLTPNEIDSTWSALEK | ||||||
Repeat | 366-480 | Spectrin 2 | ||||
Sequence: AEQEHAEALRIELKRQKKIAVLLQKYNRILKKLENWATTKSVYLGSNETGDSITAVQAKLKNLEAFDGECQSLEGQSNSDLLSILAQLTELNYNGVPELTERKDTFFAQQWTGVK | ||||||
Repeat | 481-601 | Spectrin 3 | ||||
Sequence: SSAETYKNTLLAELERLQKIEDSLVEFAKRAAQLNVWIEAADDHVFDPINVDSVQGVQEIQEKFDAFLHDQSQQFAELEALAALTQQLRELGRSENDYSVISYDELSAKWNNLLAGIEERK | ||||||
Repeat | 602-714 | Spectrin 4 | ||||
Sequence: VQLANELTTQTNNDVLCQSFSVKANEISDYVRVTLDAISQNTSSDPQEQLNNIRAIITAHAEKKPELDELYTIASQLEEAQVVDNKHTQHSLESIKLKWDKLNTLAKKNEQVV | ||||||
Domain | 729-764 | EF-hand 1 | ||||
Sequence: EELSEFKACFSHFDKDNDNKLNRLEFSSCLKSIGDE | ||||||
Domain | 765-800 | EF-hand 2 | ||||
Sequence: LTEEQLNQVISKIDTDGNGTISFEEFIDYMVSSRKG |
Sequence similarities
Belongs to the alpha-actinin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length861
- Mass (Da)97,358
- Last updated2007-03-20 v2
- Checksum17F4364B8059EAFA
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 78 | in Ref. 1; CAA68685 | ||||
Sequence: R → RR | ||||||
Sequence conflict | 359 | in Ref. 3; CAA27855 | ||||
Sequence: T → P | ||||||
Sequence conflict | 500 | in Ref. 3; CAA27855 | ||||
Sequence: I → T | ||||||
Sequence conflict | 675 | in Ref. 1; CAA68685 | ||||
Sequence: A → R | ||||||
Sequence conflict | 696 | in Ref. 1; CAA68685 | ||||
Sequence: I → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |