Q63356 · MYO1E_RAT
- ProteinUnconventional myosin-Ie
- GeneMyo1e
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1107 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Involved in clathrin-mediated endocytosis and intracellular movement of clathrin-coated ve (By similarity)sicles. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function (By similarity).
In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14 (By similarity).
In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14 (By similarity).
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 | |||
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Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameUnconventional myosin-Ie
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ63356
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In cultured podocytes, it localizes close to and is associated with the cytoplasmic membrane, with enrichment at the lamellipodia tips. Colocalizes with cytoplasmic vesicles, including endocytic clathrin-coated vesicles. Colocalizes with dynamin at cytoplasmic vesicles (By similarity).
Detected in cytoplasmic punctae. Colocalizes with F-actin
Detected in cytoplasmic punctae. Colocalizes with F-actin
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000123451 | 1-1107 | Unconventional myosin-Ie | |||
Sequence: MGSKGAYRYHWQSHNVKHSGVDDMVLLSKITESSIVENLKKRYMDDYIFTYIGSVLISVNPFKQMPYFGEKEIEMYQGAAQYENPPHIYALADSMYRNMIIDRENQCVIISGESGAGKTVAAKYIMSYVSRVSGGGPKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSPGGEPDGGKISNFLLEKSRVVMRNPGERSFHIFYQLIEGASPEQKQSLGITSMDYYYYLSLSGSYKVDDIDDKRDFQETLHAMNVIGIFSEEQTLVLQIVAGILHLGNINFKEVGNYAAVESEEFLAFPAYLLGINQDRLKEKLTSRQMDSKWGGKSESIHVTLNVEQACYTRDALAKALHARVFDFLVDSINKAMEKDHEEYNIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGIRWTPIEYFNNKIVCDLIESKVNPPGIMSILDDVCATMHAVGEGADQTLLQKLQMQIGSHEHFNSWNQGFIIHHYAGKVSYDMDGFCERNRDVLFMDLIELMQSSELPFIKSLFPENLQADKKGRPTTAGSKIKKQANDLVSTLMKCTPHYIRCIKPNETKKPKDWEESRVKHQVEYLGLKENIRVRRAGYAYRRVFQKFLQRYAILTKATWPVWRGDEKQGVLHLLQSVNMDSDQFQLGRSKVFIKAPESLFLLEEMRERKYDGYARVIQKTWRKFVARKKYVQMREDASDLLLNKKERRRNSINRNFIGDYIGMEEHPELQQFVGKREKIDFADIVTKYDRRFKGVKRDLLLTPKCLYLIGREKVKQGPDKGLVKEVLKRKIEVERILSVSLSTMQDDIFILHEQEYDSLLESVFKTEFLSLLTKRYEEKTQKQLPLKFSNTLELKLKKENWGPWSAGGSRQVQFYQGFGDLAILKPSNKVLQVSIGPGLPKNARPTRRNTVSSRGYSGGTNNNYPMRAAPAPPGCHRNGLTRNQFVHPPRASGNQRSNQKSLYTSMARPPLPRQQSTGSDRLSQTPESLDFLKVPDQGAAGVRRQTTSRPPPAGGRPKPQPKPKPQVPQCKALYAYDAQDTDELSFNANDVIDIIKEDPSGWWTGRLRGKQGLFPNNYVTKI | ||||||
Modified residue | 1001 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in brain stem, brain cortex, cerebellum, stomach, colon, heart, lung, liver, spleen and kidney. Detected in utricle, cochlea, outer hair cell bundle cuticular plate and vestibular epithelia (at protein level). Detected in cochlea and vestibular tissues. Detected in kidney, lung, spleen and intestine.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 19-692 | Myosin motor | ||||
Sequence: SGVDDMVLLSKITESSIVENLKKRYMDDYIFTYIGSVLISVNPFKQMPYFGEKEIEMYQGAAQYENPPHIYALADSMYRNMIIDRENQCVIISGESGAGKTVAAKYIMSYVSRVSGGGPKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSPGGEPDGGKISNFLLEKSRVVMRNPGERSFHIFYQLIEGASPEQKQSLGITSMDYYYYLSLSGSYKVDDIDDKRDFQETLHAMNVIGIFSEEQTLVLQIVAGILHLGNINFKEVGNYAAVESEEFLAFPAYLLGINQDRLKEKLTSRQMDSKWGGKSESIHVTLNVEQACYTRDALAKALHARVFDFLVDSINKAMEKDHEEYNIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGIRWTPIEYFNNKIVCDLIESKVNPPGIMSILDDVCATMHAVGEGADQTLLQKLQMQIGSHEHFNSWNQGFIIHHYAGKVSYDMDGFCERNRDVLFMDLIELMQSSELPFIKSLFPENLQADKKGRPTTAGSKIKKQANDLVSTLMKCTPHYIRCIKPNETKKPKDWEESRVKHQVEYLGLKENIRVRRAGYAYRRVFQKFLQRYAILTKATWPVWRGDEKQGVLHLLQSVNMDSDQFQLGRSKVFIKAPESLFLLEEMRE | ||||||
Region | 581-591 | Actin-binding | ||||
Sequence: PHYIRCIKPNE | ||||||
Domain | 695-724 | IQ | ||||
Sequence: YDGYARVIQKTWRKFVARKKYVQMREDASD | ||||||
Domain | 730-922 | TH1 | ||||
Sequence: KERRRNSINRNFIGDYIGMEEHPELQQFVGKREKIDFADIVTKYDRRFKGVKRDLLLTPKCLYLIGREKVKQGPDKGLVKEVLKRKIEVERILSVSLSTMQDDIFILHEQEYDSLLESVFKTEFLSLLTKRYEEKTQKQLPLKFSNTLELKLKKENWGPWSAGGSRQVQFYQGFGDLAILKPSNKVLQVSIGP | ||||||
Region | 920-1052 | Disordered | ||||
Sequence: IGPGLPKNARPTRRNTVSSRGYSGGTNNNYPMRAAPAPPGCHRNGLTRNQFVHPPRASGNQRSNQKSLYTSMARPPLPRQQSTGSDRLSQTPESLDFLKVPDQGAAGVRRQTTSRPPPAGGRPKPQPKPKPQV | ||||||
Compositional bias | 930-949 | Polar residues | ||||
Sequence: PTRRNTVSSRGYSGGTNNNY | ||||||
Compositional bias | 970-1011 | Polar residues | ||||
Sequence: FVHPPRASGNQRSNQKSLYTSMARPPLPRQQSTGSDRLSQTP | ||||||
Compositional bias | 1037-1051 | Pro residues | ||||
Sequence: PAGGRPKPQPKPKPQ | ||||||
Domain | 1050-1107 | SH3 | ||||
Sequence: PQVPQCKALYAYDAQDTDELSFNANDVIDIIKEDPSGWWTGRLRGKQGLFPNNYVTKI |
Sequence similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,107
- Mass (Da)126,827
- Last updated1996-11-01 v1
- ChecksumB9D8FBB0CE047148
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2K9E8 | A0A0G2K9E8_RAT | Myo1e | 989 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 930-949 | Polar residues | ||||
Sequence: PTRRNTVSSRGYSGGTNNNY | ||||||
Compositional bias | 970-1011 | Polar residues | ||||
Sequence: FVHPPRASGNQRSNQKSLYTSMARPPLPRQQSTGSDRLSQTP | ||||||
Compositional bias | 1037-1051 | Pro residues | ||||
Sequence: PAGGRPKPQPKPKPQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X74815 EMBL· GenBank· DDBJ | CAA52815.1 EMBL· GenBank· DDBJ | mRNA |