Q04439 · MYO5_YEAST

Function

function

One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.

Miscellaneous

Present with 2280 molecules/cell in log phase SD medium.

Features

Showing features for binding site.

112191002003004005006007008009001,0001,1001,200
TypeIDPosition(s)Description
Binding site129-136ATP (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 cortical patch
Cellular Componentactin cytoskeleton
Cellular Componentcell periphery
Cellular Componentcell tip
Cellular Componentcellular bud
Cellular Componentcytoplasm
Cellular Componentmating projection tip
Cellular Componentmyosin I complex
Cellular Componentplasma membrane
Molecular Functionactin filament binding
Molecular FunctionATP binding
Molecular Functionhydrolase activity
Molecular Functionidentical protein binding
Molecular Functionmicrofilament motor activity
Biological Processactin cortical patch localization
Biological Processactin filament organization
Biological Processbipolar cellular bud site selection
Biological Processendocytosis
Biological Processexocytosis
Biological Processfungal-type cell wall organization
Biological Processpositive regulation of Arp2/3 complex-mediated actin nucleation
Biological Processreceptor-mediated endocytosis
Biological Processresponse to osmotic stress
Biological Processresponse to salt stress
Biological Processreticulophagy

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Myosin-5
  • Alternative names
    • Actin-dependent myosin-I MYO5
    • Class I unconventional myosin MYO5
    • Type I myosin MYO5

Gene names

    • Name
      MYO5
    • ORF names
      YM9718.08
    • Ordered locus names
      YMR109W

Organism names

Accessions

  • Primary accession
    Q04439
  • Secondary accessions
    • D6VZT2

Proteomes

Organism-specific databases

Subcellular Location

Note: Localizes to cortical patch-like protein structures that assemble actin patches. Enriched at sites of polarized growth.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis164Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization.
Mutagenesis168Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization.
Mutagenesis209Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization.
Mutagenesis357Leads to a depolarized actin cytoskeleton and a strong defect in the capacity to internalize STE2.
Mutagenesis357No growth defect, but leads to a partially depolarized actin cytoskeleton. Accelerates the constitutive internalization of STE2.
Mutagenesis377Bypasses the requirement of SHE4 for proper actin cytoskeleton polarization.
Mutagenesis472In MYO5-1; temperature sensitive loss of function.
Mutagenesis1123Abolishes interaction with BBC1 and VRP1.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 16 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001234921-1219Myosin-5
Modified residue357Phosphoserine
Modified residue359Phosphotyrosine
Modified residue777Phosphoserine
Modified residue992Phosphoserine
Modified residue1205Phosphoserine

Post-translational modification

Phosphorylation of the TEDS site (Ser-357) is required for the polarization of the actin cytoskeleton and for ligand-induced, but not for constitutive internalization of STE2. Phosphorylation probably activates the myosin-I ATPase activity. Ser-357 is phosphorylated by YPK2 in vitro.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts (via myosin motor domain) with SHE4; this interaction is important for proper localization and may regulate the interaction of the motor domain with actin. Interacts (via SH3 domain) with VRP1; this interaction is required for localization to sites of polarized growth and may regulate the interaction of the tail domain with actin. Interacts (via SH3 domain) with PAN1; this interaction is important for late stages of endocytopsis. Interacts (via SH3 domain) with BBC1 and LAS17. Interacts (via C-terminal acidic tail) with ARC19 and ARC40; ARC19 and ARC40 are Arp2/3 complex subunits. Interacts with BZZ1, PKH1, PKH2, YPK1 and YPK2.

Binary interactions

View interactors in UniProtKB
View CPX-1470 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-20Disordered
Domain36-715Myosin motor
Region588-610Actin-binding
Domain719-739IQ 1
Domain740-765IQ 2
Domain771-961TH1
Region951-1106Disordered
Compositional bias975-991Polar residues
Compositional bias1023-1052Polar residues
Compositional bias1070-1086Pro residues
Domain1085-1147SH3
Region1139-1167Disordered
Compositional bias1143-1167Polar residues

Domain

The myosin motor domain displays actin-stimulated ATPase activity and generates a mechanochemical force.
The tail domain participates in molecular interactions that specify the role of the motor domain. It is composed of several tail homology (TH) domains, namely a putative phospholipid-binding myosin tail domain (also named TH1), an Ala- and Pro-rich domain (TH2), followed by an SH3 domain and a C-terminal acidic domain (TH3).

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,219
  • Mass (Da)
    136,899
  • Last updated
    1997-11-01 v1
  • Checksum
    DFFB9EC16B61CD29
MAILKRGARKKVHQEPAKRSANIKKATFDSSKKKEVGVSDLTLLSKISDEAINENLKKRFLNATIYTYIGHVLISVNPFRDLGIYTDAVMNEYKGKNRLEVPPHVFAIAESMYYNMKSYNENQCVIISGESGAGKTEAAKRIMQYIAAASSTHTESIGKIKDMVLATNPLLESFGCAKTLRNNNSSRHGKYLEIKFNNQFEPCAGNITNYLLEKQRVVSQIKNERNFHIFYQFTKGASDAYRQTFGVQKPEQYVYTAAAGCISAETIDDLQDYQETLKAMRVIGLGQEEQDQIFRMLAAILWIGNVSFIENEEGNAQVRDTSVTDFVAYLLQIDSQLLIKSLVERIMETNHGMKRGSVYHVPLNIVQADAVRDALAKAIYNNLFDWIVSRVNKSLQAFPGAEKSIGILDIYGFEIFEHNSFEQICINYVNEKLQQIFIQLTLKSEQETYEREKIQWTPIKYFDNKVVCDLIEARRPPGIFAAMNDSVATAHADSNAADQAFAQRLNLFTTNPHFDLRSNKFVIKHYAGDVTYDIDGITDKNKDQLQKDLVELIGTTTNTFLATIFPDTVDRESKRRPPTAGDKIIKSANDLVETLSKAQPSYIRTIKPNETKSPNDYDDRQVLHQIKYLGLQENVRIRRAGFAYRQVFEKFVERFYLLSPHCSYAGDYTWQGDTLDAVKYILQDSSIPQQEYQLGVTSVFIKTPETLFALEHMRDRYWHNMAARIQRAWRRFLQRRIDAATKIQRTIRERKEGNKYEKLRDYGTKVLGGRKERRSMSLLGYRAFMGDYLSCNESKSKGAYIKRQVSIKEKVIFSIHGEALHTKFGRSAQRLKKTFLLTPTTLYIVGQTLVQNAMTYTQDYKIDVRNIQAVSLTNLQDDWVAIKLASSGQPDPLINTYFKTELITHLKRLNDKIQIKIGSAIEYQKKPGKLHSVKCQINESAPKYGDIYKSSTISVRRGNPPNSQVHKKPRKKSSISSGYHASSSQATRRPVSIAAAQHVPTAPASRHSKKPAPPPPGMQNKAATRRSVPNPASTLTASQSNARPSPPTAATRATPAATPAAAAMGSGRQANIPPPPPPPPPSSKPKEPMFEAAYDFPGSGSPSELPLKKGDVIYITREEPSGWSLGKLLDGSKEGWVPTAYMKPHSGNNNIPTPPQNRDVPKPVLNSVQHDNTSANVIPAAAQASLGDGLANALAARANKMRLESDDEEANEDEEEDDW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias975-991Polar residues
Compositional bias1023-1052Polar residues
Compositional bias1070-1086Pro residues
Compositional bias1143-1167Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z49702
EMBL· GenBank· DDBJ
CAA89745.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006946
EMBL· GenBank· DDBJ
DAA10006.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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