Q9XXV8 · MYOK_DICDI

Function

function

Myosins are actin-based motor molecules with ATPase activity. Involved in phagocytosis and motility, and in the maintenance and dynamics of cell cortex.

Features

Showing features for binding site.

1858100200300400500600700800
TypeIDPosition(s)Description
Binding site100-107ATP (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 cytoskeleton
Cellular Componentcell leading edge
Cellular Componentcytoplasm
Cellular Componentearly phagosome
Cellular Componentmacropinocytic cup
Cellular Componentmyosin complex
Cellular Componentphagocytic cup
Cellular Componentphagocytic cup lip
Cellular Componentplasma membrane
Cellular Componentruffle
Molecular Functionactin filament binding
Molecular FunctionATP binding
Molecular Functionmicrofilament motor activity
Molecular Functionprofilin binding
Biological Processactin filament organization
Biological Processchemotaxis to cAMP
Biological Processcortical actin cytoskeleton organization
Biological Processendocytosis
Biological Processphagocytosis, engulfment
Biological Processpositive regulation of cell motility
Biological Processpositive regulation of phagocytosis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Myosin-K heavy chain

Gene names

    • Name
      myoK
    • Synonyms
      myoIG
    • ORF names
      DDB_G0274575

Organism names

Accessions

  • Primary accession
    Q9XXV8
  • Secondary accessions
    • Q555W0
    • Q86J00
    • Q9UA70

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003286071-858Myosin-K heavy chain

Proteomic databases

Expression

Developmental stage

Expression stimulated at early developmental stages, before aggregation.

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain7-820Myosin motor
Region121-265Disordered
Compositional bias178-231Pro residues
Region712-722Actin-binding
Region821-858Tail

Domain

The head domain possess two actin-binding sites, a classic ATP-dependent one and a secondary salt-dependent one (located inside the GPR domain).

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    858
  • Mass (Da)
    94,364
  • Last updated
    1999-11-01 v1
  • Checksum
    E459F2AFDC9C2C1E
MFRLFSSGVDDLVLVSNPSNGEVTSQIGARFDRELIYTNIGEVLIAVNPYKALPITGPEFIKLYQNASGSDASPHIYALAERAYRRMVDENESQCVIISGESGAGKTVSAKLILQYVTSVSPNNSSGGGIGGSGGGNGGIPQYDGGSDDRPSPPMGRGMGMPGMVGRGGLPTRGGGPPSRGGGPPPTRGRGGPPPPIPQNRGAPPPVSNGGAPPPVARGPVAPPPTRGAPPTRGGGPANRGGRGGGPPPVSTSRGGGGYGGSSKTVDVEHIKKVILDSNPLMEAIGNAKTVRNDNSSRFGKYLEIQFDDNNAPVGGLISTFLLEKTRVTFQQKNERNFHIFYQMLGGLDQTTKSEWGLTQATDFYYLAQSKCTTVEDVDDGKDFHEVKAAMETVGISRDEQTEIFRILAAILHVGNIRFQGEAPASVIDETPLQWAASLLGCDPTFLCQSLNHRQIQSGSARHTQYQVPQNPDQSAGLRDALAKTLYERIFDFIVARVNKAMSFSGNCKVIGVLDIYGFEVFERNSFEQFCINYVNERLQQIFIDLTVRGEQREYHEEGMKWKDISFFDNKIVVDLIDGNKPPGIMRVLDDVCKTVHAVDSAAADIKFMEKLIHSIQSHPHLVISNTGSSADEFTIKHYAGEVSYSIEEFCFKNNDNLYASIVGCLQNSTYQFIVSLFPENIQDNKQAPTTSSFKIRQSSSYLVTRLSACTPHYIRCIKPNDKKQPMNFVSSRVEHQVKYLGILENIKVKRSGYAYRQLKDIFLNRFGKIMDVQPRNVQEFVEYITRTHKDINADEFEEGKTKIFVKNPETIFVMEDLLMQKIDPIGYKNRVQAYKENEKLAQMKQGKHSMKQKCLIQ

Features

Showing features for compositional bias, sequence conflict.

Type
IDPosition(s)Description
Compositional bias178-231Pro residues
Sequence conflict659in Ref. 2; AAD47904

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB017909
EMBL· GenBank· DDBJ
BAA76319.1
EMBL· GenBank· DDBJ
Genomic DNA
AF090534
EMBL· GenBank· DDBJ
AAD47904.1
EMBL· GenBank· DDBJ
mRNA
AAFI02000012
EMBL· GenBank· DDBJ
EAL70180.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help