O00159 · MYO1C_HUMAN
- ProteinUnconventional myosin-Ic
- GeneMYO1C
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1063 (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 are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes.
Isoform 3
Involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation.
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUnconventional myosin-Ic
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00159
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on the cell membrane (By similarity).
Colocalizes in adipocytes with GLUT4 at actin-based membranes (By similarity).
Colocalizes with GLUT4 at insulin-induced ruffles at the cell membrane (By similarity).
Localizes transiently at cell membrane to region known to be enriched in PIP2 (By similarity).
Activation of phospholipase C results in its redistribution to the cytoplasm (By similarity).
Colocalizes with RNA polymerase II (PubMed:22736583).
Translocates to nuclear speckles upon exposure to inhibitors of RNA polymerase II transcription (PubMed:22736583).
Colocalizes in adipocytes with GLUT4 at actin-based membranes (By similarity).
Colocalizes with GLUT4 at insulin-induced ruffles at the cell membrane (By similarity).
Localizes transiently at cell membrane to region known to be enriched in PIP2 (By similarity).
Activation of phospholipase C results in its redistribution to the cytoplasm (By similarity).
Colocalizes with RNA polymerase II (PubMed:22736583).
Translocates to nuclear speckles upon exposure to inhibitors of RNA polymerase II transcription (PubMed:22736583).
Isoform 3
Note: Colocalizes with RNA polymerase II in the nucleus (By similarity).
Colocalizes with RNA polymerase I in nucleoli (By similarity).
In the nucleolus, is localized predominantly in dense fibrillar component (DFC) and in granular component (GC) (PubMed:16133118, PubMed:16877530).
Accumulates strongly in DFC and GC during activation of transcription (PubMed:16133118).
Colocalizes with transcription sites (By similarity).
Colocalizes in the granular cortex at the periphery of the nucleolus with RPS6 (PubMed:16877530).
Colocalizes in nucleoplasm with RPS6 and actin that are in contact with RNP particles (PubMed:16877530).
Colocalizes with RPS6 at the nuclear pore level (PubMed:16877530).
Colocalizes with RNA polymerase I in nucleoli (By similarity).
In the nucleolus, is localized predominantly in dense fibrillar component (DFC) and in granular component (GC) (PubMed:16133118, PubMed:16877530).
Accumulates strongly in DFC and GC during activation of transcription (PubMed:16133118).
Colocalizes with transcription sites (By similarity).
Colocalizes in the granular cortex at the periphery of the nucleolus with RPS6 (PubMed:16877530).
Colocalizes in nucleoplasm with RPS6 and actin that are in contact with RNP particles (PubMed:16877530).
Colocalizes with RPS6 at the nuclear pore level (PubMed:16877530).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 736 | Abolishes interaction with YWHAB. | ||||
Sequence: S → A | ||||||
Mutagenesis | 736 | Increases affinity for YWHAB. | ||||
Sequence: S → E | ||||||
Natural variant | VAR_054855 | 795 | in dbSNP:rs8081370 | |||
Sequence: V → I | ||||||
Natural variant | VAR_054856 | 826 | in dbSNP:rs9905106 | |||
Sequence: Q → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,380 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | In isoform O00159-2; N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000123445 | 1-1063 | UniProt | Unconventional myosin-Ic | |||
Sequence: MALQVELVPTGEIIRVVHPHRPCKLALGSDGVRVTMESALTARDRVGVQDFVLLENFTSEAAFIENLRRRFRENLIYTYIGPVLVSVNPYRDLQIYSRQHMERYRGVSFYEVPPHLFAVADTVYRALRTERRDQAVMISGESGAGKTEATKRLLQFYAETCPAPERGGAVRDRLLQSNPVLEAFGNAKTLRNDNSSRFGKYMDVQFDFKGAPVGGHILSYLLEKSRVVHQNHGERNFHIFYQLLEGGEEETLRRLGLERNPQSYLYLVKGQCAKVSSINDKSDWKVVRKALTVIDFTEDEVEDLLSIVASVLHLGNIHFAANEESNAQVTTENQLKYLTRLLSVEGSTLREALTHRKIIAKGEELLSPLNLEQAAYARDALAKAVYSRTFTWLVGKINRSLASKDVESPSWRSTTVLGLLDIYGFEVFQHNSFEQFCINYCNEKLQQLFIELTLKSEQEEYEAEGIAWEPVQYFNNKIICDLVEEKFKGIISILDEECLRPGEATDLTFLEKLEDTVKHHPHFLTHKLADQRTRKSLGRGEFRLLHYAGEVTYSVTGFLDKNNDLLFRNLKETMCSSKNPIMSQCFDRSELSDKKRPETVATQFKMSLLQLVEILQSKEPAYVRCIKPNDAKQPGRFDEVLIRHQVKYLGLLENLRVRRAGFAYRRKYEAFLQRYKSLCPETWPTWAGRPQDGVAVLVRHLGYKPEEYKMGRTKIFIRFPKTLFATEDALEVRRQSLATKIQAAWRGFHWRQKFLRVKRSAICIQSWWRGTLGRRKAAKRKWAAQTIRRLIRGFVLRHAPRCPENAFFLDHVRTSFLLNLRRQLPQNVLDTSWPTPPPALREASELLRELCIKNMVWKYCRSISPEWKQQLQQKAVASEIFKGKKDNYPQSVPRLFISTRLGTDEISPRVLQALGSEPIQYAVPVVKYDRKGYKPRSRQLLLTPNAVVIVEDAKVKQRIDYANLTGISVSSLSDSLFVLHVQRADNKQKGDVVLQSDHVIETLTKTALSANRVNSININQGSITFAGGPGRDGTIDFTPGSELLITKAKNGHLAVVAPRLNSR | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 343 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 383 | UniProt | N6-methyllysine | ||||
Sequence: K | |||||||
Modified residue | 408 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 408 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 410 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 486 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 536 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 592 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 648 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 736 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 864 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 864 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 916 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1034 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1038 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1041 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1041 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1062 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Isoform 2 contains a N-acetylmethionine at position 1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts (via its IQ motifs) with CABP1 and CIB1; the interaction with CABP1 and CIB1 is calcium-dependent (By similarity).
Interacts (via tail domain) with PLEKHB1 (via PH domain); the interaction is not affected by the presence or absence of calcium and CALM (By similarity).
Interacts with POLR1A (By similarity).
Interacts with POLR2A (By similarity).
Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (PubMed:16603771).
Interacts (via its IQ motifs) with CALM; this precludes interaction with YWHAB (PubMed:24636949).
Interacts with YWHAB; this precludes interaction with CALM (PubMed:24636949).
Interacts with RPS6 (PubMed:16877530).
Interacts with actin (PubMed:16877530).
Interacts with LLPH (By similarity).
Interacts with GLUT4 (By similarity).
Interacts (via its IQ motifs) with SH3BGRL3; the interaction is dependent on calcium and takes place at membrane ruffles (PubMed:34380438).
Interacts (via tail domain) with PLEKHB1 (via PH domain); the interaction is not affected by the presence or absence of calcium and CALM (By similarity).
Interacts with POLR1A (By similarity).
Interacts with POLR2A (By similarity).
Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (PubMed:16603771).
Interacts (via its IQ motifs) with CALM; this precludes interaction with YWHAB (PubMed:24636949).
Interacts with YWHAB; this precludes interaction with CALM (PubMed:24636949).
Interacts with RPS6 (PubMed:16877530).
Interacts with actin (PubMed:16877530).
Interacts with LLPH (By similarity).
Interacts with GLUT4 (By similarity).
Interacts (via its IQ motifs) with SH3BGRL3; the interaction is dependent on calcium and takes place at membrane ruffles (PubMed:34380438).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00159 | CALM3 P0DP25 | 3 | EBI-350423, EBI-397435 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 47-731 | Myosin motor | ||||
Sequence: GVQDFVLLENFTSEAAFIENLRRRFRENLIYTYIGPVLVSVNPYRDLQIYSRQHMERYRGVSFYEVPPHLFAVADTVYRALRTERRDQAVMISGESGAGKTEATKRLLQFYAETCPAPERGGAVRDRLLQSNPVLEAFGNAKTLRNDNSSRFGKYMDVQFDFKGAPVGGHILSYLLEKSRVVHQNHGERNFHIFYQLLEGGEEETLRRLGLERNPQSYLYLVKGQCAKVSSINDKSDWKVVRKALTVIDFTEDEVEDLLSIVASVLHLGNIHFAANEESNAQVTTENQLKYLTRLLSVEGSTLREALTHRKIIAKGEELLSPLNLEQAAYARDALAKAVYSRTFTWLVGKINRSLASKDVESPSWRSTTVLGLLDIYGFEVFQHNSFEQFCINYCNEKLQQLFIELTLKSEQEEYEAEGIAWEPVQYFNNKIICDLVEEKFKGIISILDEECLRPGEATDLTFLEKLEDTVKHHPHFLTHKLADQRTRKSLGRGEFRLLHYAGEVTYSVTGFLDKNNDLLFRNLKETMCSSKNPIMSQCFDRSELSDKKRPETVATQFKMSLLQLVEILQSKEPAYVRCIKPNDAKQPGRFDEVLIRHQVKYLGLLENLRVRRAGFAYRRKYEAFLQRYKSLCPETWPTWAGRPQDGVAVLVRHLGYKPEEYKMGRTKIFIRFPKTLFATEDALE | ||||||
Region | 608-630 | Actin-binding | ||||
Sequence: LLQLVEILQSKEPAYVRCIKPND | ||||||
Domain | 734-757 | IQ 1 | ||||
Sequence: RQSLATKIQAAWRGFHWRQKFLRV | ||||||
Domain | 758-786 | IQ 2 | ||||
Sequence: KRSAICIQSWWRGTLGRRKAAKRKWAAQT | ||||||
Domain | 885-1059 | TH1 | ||||
Sequence: KDNYPQSVPRLFISTRLGTDEISPRVLQALGSEPIQYAVPVVKYDRKGYKPRSRQLLLTPNAVVIVEDAKVKQRIDYANLTGISVSSLSDSLFVLHVQRADNKQKGDVVLQSDHVIETLTKTALSANRVNSININQGSITFAGGPGRDGTIDFTPGSELLITKAKNGHLAVVAPR |
Domain
Binds directly to large unilamellar vesicles (LUVs) containing phosphatidylinositol 4,5-bisphosphate (PIP2) or inositol 1,4,5-trisphosphate (InsP3). The PIP2-binding site corresponds to the myosin tail domain (PH-like) present in its tail domain (By similarity).
Sequence similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O00159-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsA
- Length1,063
- Mass (Da)121,682
- Last updated2011-01-11 v4
- ChecksumB105197BA07317B8
O00159-2
- Name2
- SynonymsC
- Differences from canonical
- 1-35: Missing
O00159-3
- Name3
- SynonymsB, Nuclear myosin 1, NM1, NMI
- Differences from canonical
- 1-25: MALQVELVPTGEIIRVVHPHRPCKL → MRYRAS
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_036862 | 1-25 | in isoform 3 | |||
Sequence: MALQVELVPTGEIIRVVHPHRPCKL → MRYRAS | ||||||
Alternative sequence | VSP_036861 | 1-35 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 37 | in Ref. 1; CAA67131 | ||||
Sequence: E → D | ||||||
Sequence conflict | 152 | in Ref. 1; CAA67131 | ||||
Sequence: R → K | ||||||
Sequence conflict | 165 | in Ref. 1; CAA67131 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 200 | in Ref. 6; BU855623 | ||||
Sequence: K → E | ||||||
Sequence conflict | 324 | in Ref. 1; CAA67131 | ||||
Sequence: E → D | ||||||
Sequence conflict | 379 | in Ref. 1; CAA67131 | ||||
Sequence: D → N | ||||||
Sequence conflict | 453 | in Ref. 1; CAA67131 | ||||
Sequence: T → P | ||||||
Sequence conflict | 832 | in Ref. 1; CAA67131 | ||||
Sequence: S → Y | ||||||
Sequence conflict | 986 | in Ref. 1; CAA67131 | ||||
Sequence: N → I | ||||||
Sequence conflict | 1062 | in Ref. 1; CAA67131 | ||||
Sequence: S → Y |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X98507 EMBL· GenBank· DDBJ | CAA67131.1 EMBL· GenBank· DDBJ | mRNA | ||
AK292910 EMBL· GenBank· DDBJ | BAF85599.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AB210015 EMBL· GenBank· DDBJ | BAE06097.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC100748 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC044891 EMBL· GenBank· DDBJ | AAH44891.2 EMBL· GenBank· DDBJ | mRNA | ||
BC068013 EMBL· GenBank· DDBJ | AAH68013.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BU855623 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |