P36006 · MYO3_YEAST
- ProteinMyosin-3
- GeneMYO3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1272 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 155 molecules/cell in log phase SD medium.
Features
Showing features for binding site.
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | actin cortical patch | |
Cellular Component | actin cytoskeleton | |
Cellular Component | cell periphery | |
Cellular Component | cell tip | |
Cellular Component | cytoplasm | |
Cellular Component | myosin I complex | |
Cellular Component | plasma membrane | |
Molecular Function | actin filament binding | |
Molecular Function | ATP binding | |
Molecular Function | hydrolase activity | |
Molecular Function | microfilament motor activity | |
Molecular Function | myosin binding | |
Biological Process | actin cortical patch localization | |
Biological Process | actin filament organization | |
Biological Process | bipolar cellular bud site selection | |
Biological Process | endocytosis | |
Biological Process | exocytosis | |
Biological Process | fungal-type cell wall organization | |
Biological Process | positive regulation of Arp2/3 complex-mediated actin nucleation | |
Biological Process | response to osmotic stress | |
Biological Process | reticulophagy |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMyosin-3
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP36006
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to cortical patch-like protein structures that assemble actin patches. Enriched at sites of polarized growth.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 132 | Loss of function. | ||||
Sequence: G → R | ||||||
Mutagenesis | 357 | Loss of function. | ||||
Sequence: S → A | ||||||
Mutagenesis | 357 | Has a constitutive higher activity in actin assembly. | ||||
Sequence: S → D | ||||||
Mutagenesis | 1158 | Abolishes interaction with LAS17 and causes severe mislocalization of the protein. | ||||
Sequence: W → S | ||||||
Mutagenesis | 1272 | Abolishes interaction with ARC40. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 24 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000123490 | 1-1272 | Myosin-3 | |||
Sequence: MAVIKKGARRKDVKEPKKRSAKIKKATFDANKKKEVGISDLTLLSKISDESINENLKKRFKNGIIYTYIGHVLISVNPFRDLGIYTNAVLESYKGKNRLEVPPHVFAIAESMYYNLKSYNENQCVIISGESGAGKTEAAKRIMQYIAAASNSHSESIGKIKDMVLATNPLLESFGCAKTLRNNNSSRHGKYLEIKFNSQFEPCAGNITNYLLEKQRVVGQIKNERNFHIFYQFTKGASDTYKQMFGVQMPEQYIYTAAAGCTTADTIDDVKDYEGTLEAMRTIGLVQEEQDQIFRMLAAILWIGNISFIENEEGNAQVGDTSVTDFVAYLLQVDASLLVKCLVERIMQTSHGMKRGSVYHVPLNPVQATAVRDALAKAIYNNLFDWIVDRVNVSLQAFPGADKSIGILDIYGFEIFEHNSFEQICINYVNEKLQQIFIQLTLKAEQETYEREKIKWTPIKYFDNKVVCDLIEAKNPPGILAAMNDSIATAHADSNAADQAFAQRLNLFNSNPYFELRANKFVIKHYAGDVTYDINGITDKNKDQLQKDLIELIGTTTNTFLSTIFPDDVDKDSKRRPPTAGDKIIKSANELVETLSKAEPSYIRTIKPNQTKSPNDYDDHQVLHQVKYLGLQENVRIRRAGFAYRQTFEKFVERFYLLSPDCSYAGDYTWDGDTLEAVKLILRDAMIPEKEFQLGVTSVFIKTPESLFALEDMRDKYWYNMAARIQRAWRRFLQRRIDAAIKIQRTIREKKGGNKYVKLRDYGTKLLAGKKERRSMSLLGYRAFMGDYLSCNESKTKGSYIRRQVGIKDKVVFSIKGECLHSKFGRSAQRLKKVFILTKKTFYIIGQTREQNAMKYTQDYKIDVGKIKQVSLTNLQDDWMGVILVNSTQSDPLINTPFKTELMTRLKKLNEKIMIKVGPTIEYHKQPNKLHTVRSKISDSAPKYGDIYKSSTIYVRRGHPANSKSNKKPKNPGGLSGKPIKSKKSKHKSTHKHTHSHRSHRDAAKKQPLPSQKPVNPLSLAATAAQAAYNPKPDKTVPIKSSAIPAAKVSSKHSSKPSSKEKVAVKKASSSHKSSSAKQNQVSMPPSKGVEKNKEPLKETTATATANIPIPPPPPPMGQPKDPKFEAAYDFPGSGSSSELPLKKGDIVFISRDEPSGWSLAKLLDGSKEGWVPTAYMTPYKDTRNTVPVAATGAVNDVTNQKSSQIDNTISSAQEGVQFGSATVGPTSDNQSNPVGTFSDGLASALAARANKMRAESADDDDNDDGDDDDDW | ||||||
Modified residue | 357 | Phosphoserine | ||||
Sequence: S |
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 (By similarity).
Ser-357 is phosphorylated by CLA4 and STE20 in vitro
Ser-357 is phosphorylated by CLA4 and STE20 in vitro
Keywords
- PTM
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.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P36006 | AIM21 P40563 | 3 | EBI-11670, EBI-25376 | |
BINARY | P36006 | ARC40 P38328 | 3 | EBI-11670, EBI-2777 | |
BINARY | P36006 | BBC1 P47068 | 5 | EBI-11670, EBI-3437 | |
BINARY | P36006 | BCK1 Q01389 | 6 | EBI-11670, EBI-3470 | |
BINARY | P36006 | BNI1 P41832 | 3 | EBI-11670, EBI-3692 | |
BINARY | P36006 | BNR1 P40450 | 6 | EBI-11670, EBI-3711 | |
BINARY | P36006 | LAS17 Q12446 | 3 | EBI-11670, EBI-10022 | |
BINARY | P36006 | OSH2 Q12451 | 3 | EBI-11670, EBI-12621 | |
BINARY | P36006 | PRP8 P33334 | 4 | EBI-11670, EBI-465 | |
BINARY | P36006 | SAP1 P39955 | 3 | EBI-11670, EBI-16463 | |
BINARY | P36006 | STE20 Q03497 | 3 | EBI-11670, EBI-18285 | |
BINARY | P36006 | UBP7 P40453 | 3 | EBI-11670, EBI-19857 | |
BINARY | P36006 | VRP1 P37370 | 12 | EBI-11670, EBI-20502 | |
BINARY | P36006 | YOR389W Q08912 | 2 | EBI-11670, EBI-38289 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MAVIKKGARRKDVKEPKKRS | ||||||
Domain | 36-715 | Myosin motor | ||||
Sequence: VGISDLTLLSKISDESINENLKKRFKNGIIYTYIGHVLISVNPFRDLGIYTNAVLESYKGKNRLEVPPHVFAIAESMYYNLKSYNENQCVIISGESGAGKTEAAKRIMQYIAAASNSHSESIGKIKDMVLATNPLLESFGCAKTLRNNNSSRHGKYLEIKFNSQFEPCAGNITNYLLEKQRVVGQIKNERNFHIFYQFTKGASDTYKQMFGVQMPEQYIYTAAAGCTTADTIDDVKDYEGTLEAMRTIGLVQEEQDQIFRMLAAILWIGNISFIENEEGNAQVGDTSVTDFVAYLLQVDASLLVKCLVERIMQTSHGMKRGSVYHVPLNPVQATAVRDALAKAIYNNLFDWIVDRVNVSLQAFPGADKSIGILDIYGFEIFEHNSFEQICINYVNEKLQQIFIQLTLKAEQETYEREKIKWTPIKYFDNKVVCDLIEAKNPPGILAAMNDSIATAHADSNAADQAFAQRLNLFNSNPYFELRANKFVIKHYAGDVTYDINGITDKNKDQLQKDLIELIGTTTNTFLSTIFPDDVDKDSKRRPPTAGDKIIKSANELVETLSKAEPSYIRTIKPNQTKSPNDYDDHQVLHQVKYLGLQENVRIRRAGFAYRQTFEKFVERFYLLSPDCSYAGDYTWDGDTLEAVKLILRDAMIPEKEFQLGVTSVFIKTPESLFALEDMRD | ||||||
Region | 588-610 | Actin-binding | ||||
Sequence: ANELVETLSKAEPSYIRTIKPNQ | ||||||
Domain | 719-739 | IQ 1 | ||||
Sequence: YNMAARIQRAWRRFLQRRIDA | ||||||
Domain | 740-765 | IQ 2 | ||||
Sequence: AIKIQRTIREKKGGNKYVKLRDYGTK | ||||||
Domain | 771-961 | TH1 | ||||
Sequence: KERRSMSLLGYRAFMGDYLSCNESKTKGSYIRRQVGIKDKVVFSIKGECLHSKFGRSAQRLKKVFILTKKTFYIIGQTREQNAMKYTQDYKIDVGKIKQVSLTNLQDDWMGVILVNSTQSDPLINTPFKTELMTRLKKLNEKIMIKVGPTIEYHKQPNKLHTVRSKISDSAPKYGDIYKSSTIYVRRGHPA | ||||||
Region | 951-1015 | Disordered | ||||
Sequence: STIYVRRGHPANSKSNKKPKNPGGLSGKPIKSKKSKHKSTHKHTHSHRSHRDAAKKQPLPSQKPV | ||||||
Compositional bias | 980-1002 | Basic residues | ||||
Sequence: IKSKKSKHKSTHKHTHSHRSHRD | ||||||
Region | 1029-1141 | Disordered | ||||
Sequence: YNPKPDKTVPIKSSAIPAAKVSSKHSSKPSSKEKVAVKKASSSHKSSSAKQNQVSMPPSKGVEKNKEPLKETTATATANIPIPPPPPPMGQPKDPKFEAAYDFPGSGSSSELP | ||||||
Compositional bias | 1054-1068 | Basic and acidic residues | ||||
Sequence: SSKPSSKEKVAVKKA | ||||||
Compositional bias | 1069-1087 | Polar residues | ||||
Sequence: SSSHKSSSAKQNQVSMPPS | ||||||
Compositional bias | 1107-1121 | Pro residues | ||||
Sequence: NIPIPPPPPPMGQPK | ||||||
Domain | 1120-1182 | SH3 | ||||
Sequence: PKDPKFEAAYDFPGSGSSSELPLKKGDIVFISRDEPSGWSLAKLLDGSKEGWVPTAYMTPYKD | ||||||
Compositional bias | 1217-1239 | Polar residues | ||||
Sequence: VQFGSATVGPTSDNQSNPVGTFS | ||||||
Region | 1217-1272 | Disordered | ||||
Sequence: VQFGSATVGPTSDNQSNPVGTFSDGLASALAARANKMRAESADDDDNDDGDDDDDW |
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
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,272
- Mass (Da)142,451
- Last updated2011-09-21 v4
- Checksum6CB13AD3CD669600
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 95 | in Ref. 1; AAB34124 | ||||
Sequence: G → RK | ||||||
Sequence conflict | 168-169 | in Ref. 1; AAB34124 | ||||
Sequence: NP → T | ||||||
Sequence conflict | 263-270 | in Ref. 2; CAA81970 | ||||
Sequence: TADTIDDV → SADQLMR | ||||||
Sequence conflict | 917-918 | in Ref. 1; AAB34124 | ||||
Sequence: VG → RLV | ||||||
Compositional bias | 980-1002 | Basic residues | ||||
Sequence: IKSKKSKHKSTHKHTHSHRSHRD | ||||||
Sequence conflict | 1021 | in Ref. 2; CAA81970 | ||||
Sequence: A → R | ||||||
Compositional bias | 1054-1068 | Basic and acidic residues | ||||
Sequence: SSKPSSKEKVAVKKA | ||||||
Compositional bias | 1069-1087 | Polar residues | ||||
Sequence: SSSHKSSSAKQNQVSMPPS | ||||||
Compositional bias | 1107-1121 | Pro residues | ||||
Sequence: NIPIPPPPPPMGQPK | ||||||
Compositional bias | 1217-1239 | Polar residues | ||||
Sequence: VQFGSATVGPTSDNQSNPVGTFS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S76960 EMBL· GenBank· DDBJ | AAB34124.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z28129 EMBL· GenBank· DDBJ | CAA81970.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006944 EMBL· GenBank· DDBJ | DAA09032.2 EMBL· GenBank· DDBJ | Genomic DNA |