Q9Z1P2 · ACTN1_RAT

Function

function

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation.

Features

Showing features for binding site.

1892100200300400500600700800
TypeIDPosition(s)Description
Binding site759Ca2+ (UniProtKB | ChEBI)
Binding site761Ca2+ (UniProtKB | ChEBI)
Binding site763Ca2+ (UniProtKB | ChEBI)
Binding site765Ca2+ (UniProtKB | ChEBI)
Binding site770Ca2+ (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 Componentbrush border
Cellular Componentcell junction
Cellular Componentcell projection
Cellular Componentcell-cell junction
Cellular Componentcortical actin cytoskeleton
Cellular Componentcytoplasm
Cellular Componentcytoskeleton
Cellular Componentcytosol
Cellular Componentdendritic spine
Cellular Componentfascia adherens
Cellular Componentfocal adhesion
Cellular Componentglutamatergic synapse
Cellular Componentplasma membrane
Cellular Componentpostsynaptic actin cytoskeleton
Cellular Componentruffle
Cellular Componentsarcomere
Cellular Componentstress fiber
Cellular Componentsynapse
Cellular ComponentZ disc
Molecular Functionactin filament binding
Molecular Functioncalcium ion binding
Molecular Functioncytoskeletal regulatory protein binding
Molecular Functiondouble-stranded RNA binding
Molecular Functionintegrin binding
Molecular Functionnuclear receptor coactivator activity
Molecular Functionprotein domain specific binding
Molecular Functionprotein homodimerization activity
Molecular Functionstructural constituent of postsynapse
Molecular Functiontransmembrane transporter binding
Molecular Functionvinculin binding
Biological Processactin cytoskeleton organization
Biological Processactin filament bundle assembly
Biological Processactin filament network formation
Biological Processactin filament organization
Biological Processfocal adhesion assembly
Biological Processmuscle cell development
Biological Processplatelet formation
Biological Processplatelet morphogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-actinin-1
  • Alternative names
    • Alpha-actinin cytoskeletal isoform
    • F-actin cross-linking protein
    • Non-muscle alpha-actinin-1

Gene names

    • Name
      Actn1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q9Z1P2

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00000734331-892Alpha-actinin-1
Modified residue6Phosphoserine
Modified residue12Phosphotyrosine; by FAK1
Modified residue95N6-acetyllysine
Modified residue195N6-acetyllysine
Modified residue471Phosphoserine
Modified residue676N6-acetyllysine
Modified residue677Phosphoserine
Modified residue890Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP (By similarity).
Interacts with DDN (PubMed:16464232).
Interacts with PSD. Interacts with MICALL2 (By similarity).
Interacts with DNM2 and CTTN (PubMed:21210813).
Interacts with PDLIM1 (PubMed:22659164).
Interacts with PDLIM2 (PubMed:15505042).
Interacts with PDLIM4 (via PDZ domain) (PubMed:14729062).
Interacts with IGSF8 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, domain, repeat.

TypeIDPosition(s)Description
Region1-247Actin-binding
Domain31-135Calponin-homology (CH) 1
Domain144-250Calponin-homology (CH) 2
Repeat274-384Spectrin 1
Region274-733Interaction with DDN
Repeat394-499Spectrin 2
Repeat509-620Spectrin 3
Repeat630-733Spectrin 4
Domain746-781EF-hand 1
Domain787-822EF-hand 2

Sequence similarities

Belongs to the alpha-actinin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    892
  • Mass (Da)
    102,960
  • Last updated
    1999-05-01 v1
  • Checksum
    2360D496D0A84095
MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAERYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMQAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHSRQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDPQGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITGDELRRELPPDQAEYCIARMAPYAGPDSVPGALDYMSFSTALYGESDL

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I6AV34A0A8I6AV34_RATActn1890
Q6GMN8Q6GMN8_RATActn1887
A0A8I6GDI3A0A8I6GDI3_RATActn1859
A0A8I6A472A0A8I6A472_RATActn1907
Q6T487Q6T487_RATActn1914

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF115386
EMBL· GenBank· DDBJ
AAD12064.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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