P11055 · MYH3_HUMAN
- ProteinMyosin-3
- GeneMYH3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1940 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Muscle contraction.
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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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | muscle myosin complex | |
Cellular Component | myosin filament | |
Cellular Component | myosin II complex | |
Cellular Component | sarcomere | |
Molecular Function | actin filament binding | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | calmodulin binding | |
Molecular Function | microfilament motor activity | |
Molecular Function | myosin phosphatase activity | |
Biological Process | actin filament-based movement | |
Biological Process | ATP metabolic process | |
Biological Process | embryonic limb morphogenesis | |
Biological Process | face morphogenesis | |
Biological Process | muscle contraction | |
Biological Process | muscle filament sliding | |
Biological Process | muscle organ development | |
Biological Process | sarcomere organization | |
Biological Process | skeletal muscle contraction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMyosin-3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP11055
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Thick filaments of the myofibrils.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Arthrogryposis, distal, 2A (DA2A)
- Note
- DescriptionA form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA2A is characterized by contractures of the hands and feet, oropharyngeal abnormalities, scoliosis, and a distinctive face that includes a very small oral orifice, puckered lips, and a H-shaped dimple of the chin.
- See alsoMIM:193700
Natural variants in DA2A
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_030370 | 178 | T>I | in DA2A and DA2B3; dbSNP:rs121913619 | |
VAR_030374 | 498 | E>G | in DA2A | |
VAR_030376 | 583 | Y>S | in DA2A; dbSNP:rs1597488038 | |
VAR_030377 | 672 | R>C | in DA2A; dbSNP:rs121913618 | |
VAR_030378 | 672 | R>H | in DA2A; dbSNP:rs121913617 | |
VAR_030380 | 825 | V>D | in DA2A; dbSNP:rs121913620 |
Arthrogryposis, distal, 2B3 (DA2B3)
- Note
- DescriptionA form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. Distal arthrogryposis type 2 is characterized by contractures of the hands and feet, and a distinctive face characterized by prominent nasolabial folds, small mouth and downslanting palpebral fissures. DA2B3 inheritance is autosomal dominant.
- See alsoMIM:618436
Natural variants in DA2B3
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_030370 | 178 | T>I | in DA2A and DA2B3; dbSNP:rs121913619 | |
VAR_082275 | 234 | A>T | in DA2B3; dbSNP:rs121913623 | |
VAR_030371 | 261 | S>F | in DA2B3; dbSNP:rs1597490381 | |
VAR_030372 | 292 | S>C | in DA2B3; uncertain significance; dbSNP:rs139480342 | |
VAR_030373 | 375 | E>K | in DA2B3; uncertain significance; dbSNP:rs121913621 | |
VAR_082278 | 462 | D>G | in DA2B3; uncertain significance; dbSNP:rs121913622 | |
VAR_030375 | 517 | D>Y | in DA2B3; uncertain significance; dbSNP:rs1597488252 | |
VAR_030379 | 769 | G>V | in DA2B3 | |
VAR_030381 | 838 | K>E | in DA2B3 | |
VAR_030382 | 841 | missing | in DA2B3 |
Contractures, pterygia, and spondylocarpotarsal fusion syndrome 1A (CPSFS1A)
- Note
- DescriptionAn autosomal dominant disease characterized by contractures of proximal and distal joints, pterygia involving the neck, axillae, elbows, and/or knees, as well as variable vertebral, carpal, and tarsal fusions and short stature. Progression of vertebral fusions has been observed, and inter- and intrafamilial variability has been reported.
- See alsoMIM:178110
Natural variants in CPSFS1A
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_074668 | 243 | missing | in CPSFS1A; dbSNP:rs1555527166 | |
VAR_082276 | 287 | F>V | in CPSFS1A; dbSNP:rs1567560080 | |
VAR_082277 | 333 | T>R | in CPSFS1A; dbSNP:rs1567559562 | |
VAR_074669 | 1072 | N>NN | in CPSFS1A | |
VAR_074670 | 1075 | Q>P | in CPSFS1A; dbSNP:rs796051884 | |
VAR_082279 | 1344 | L>P | in CPSFS1A; uncertain significance; dbSNP:rs1567553806 |
Contractures, pterygia, and spondylocarpotarsal fusion syndrome 1B (CPSFS1B)
- Note
- DescriptionAn autosomal recessive disease characterized by contractures affecting proximal and distal joints, vertebral fusions and scoliosis, carpal and tarsal fusions as well as webbing of the skin (pterygium) involving the neck, elbows, fingers, and/or knees. Other features include facial dysmorphism, short neck, and absent finger flexion creases. Inter- and intrafamilial variability has been observed.
- See alsoMIM:618469
Natural variants in CPSFS1B
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_082274 | 47-1940 | missing | in CPSFS1B |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_082274 | 47-1940 | in CPSFS1B | |||
Sequence: Missing | ||||||
Natural variant | VAR_030370 | 178 | in DA2A and DA2B3; dbSNP:rs121913619 | |||
Sequence: T → I | ||||||
Natural variant | VAR_082275 | 234 | in DA2B3; dbSNP:rs121913623 | |||
Sequence: A → T | ||||||
Natural variant | VAR_074668 | 243 | in CPSFS1A; dbSNP:rs1555527166 | |||
Sequence: Missing | ||||||
Natural variant | VAR_030371 | 261 | in DA2B3; dbSNP:rs1597490381 | |||
Sequence: S → F | ||||||
Natural variant | VAR_082276 | 287 | in CPSFS1A; dbSNP:rs1567560080 | |||
Sequence: F → V | ||||||
Natural variant | VAR_030372 | 292 | in DA2B3; uncertain significance; dbSNP:rs139480342 | |||
Sequence: S → C | ||||||
Natural variant | VAR_082277 | 333 | in CPSFS1A; dbSNP:rs1567559562 | |||
Sequence: T → R | ||||||
Natural variant | VAR_030373 | 375 | in DA2B3; uncertain significance; dbSNP:rs121913621 | |||
Sequence: E → K | ||||||
Natural variant | VAR_082278 | 462 | in DA2B3; uncertain significance; dbSNP:rs121913622 | |||
Sequence: D → G | ||||||
Natural variant | VAR_030374 | 498 | in DA2A | |||
Sequence: E → G | ||||||
Natural variant | VAR_030375 | 517 | in DA2B3; uncertain significance; dbSNP:rs1597488252 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_030376 | 583 | in DA2A; dbSNP:rs1597488038 | |||
Sequence: Y → S | ||||||
Natural variant | VAR_030377 | 672 | in DA2A; dbSNP:rs121913618 | |||
Sequence: R → C | ||||||
Natural variant | VAR_030378 | 672 | in DA2A; dbSNP:rs121913617 | |||
Sequence: R → H | ||||||
Natural variant | VAR_030379 | 769 | in DA2B3 | |||
Sequence: G → V | ||||||
Natural variant | VAR_030380 | 825 | in DA2A; dbSNP:rs121913620 | |||
Sequence: V → D | ||||||
Natural variant | VAR_030381 | 838 | in DA2B3 | |||
Sequence: K → E | ||||||
Natural variant | VAR_030382 | 841 | in DA2B3 | |||
Sequence: Missing | ||||||
Natural variant | VAR_056173 | 1003 | in dbSNP:rs34088014 | |||
Sequence: A → V | ||||||
Natural variant | VAR_074669 | 1072 | in CPSFS1A | |||
Sequence: N → NN | ||||||
Natural variant | VAR_074670 | 1075 | in CPSFS1A; dbSNP:rs796051884 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_030196 | 1137 | in dbSNP:rs12941197 | |||
Sequence: R → C | ||||||
Natural variant | VAR_030197 | 1192 | in dbSNP:rs2285477 | |||
Sequence: A → T | ||||||
Natural variant | VAR_056174 | 1313 | in dbSNP:rs35230241 | |||
Sequence: T → I | ||||||
Natural variant | VAR_082279 | 1344 | in CPSFS1A; uncertain significance; dbSNP:rs1567553806 | |||
Sequence: L → P | ||||||
Natural variant | VAR_030383 | 1622 | originally found in DA2B3 patients; dbSNP:rs1446303362 | |||
Sequence: D → A | ||||||
Natural variant | VAR_030384 | 1637 | originally found in DA2B3 patients; dbSNP:rs34165480 | |||
Sequence: A → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,967 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000123394 | 1-1940 | UniProt | Myosin-3 | |||
Sequence: MSSDTEMEVFGIAAPFLRKSEKERIEAQNQPFDAKTYCFVVDSKEEYAKGKIKSSQDGKVTVETEDNRTLVVKPEDVYAMNPPKFDRIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFKAGLLGTLEEMRDDRLAKLITRTQAVCRGFLMRVEFQKMVQRRESIFCIQYNIRSFMNVKHWPWMKLFFKIKPLLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRMVVHESEE | |||||||
Modified residue | 130 | UniProt | N6,N6,N6-trimethyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 174 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 181 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 256 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 379 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 411 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 554 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 610 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 643 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 644 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 647 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 729 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 739 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 938 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 949 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1200 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1336 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1337 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1374 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1376 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 1378 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1384 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1477 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1479 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1692 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1696 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1776 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1777 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1916 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 33-82 | Myosin N-terminal SH3-like | ||||
Sequence: DAKTYCFVVDSKEEYAKGKIKSSQDGKVTVETEDNRTLVVKPEDVYAMNP | ||||||
Domain | 86-779 | Myosin motor | ||||
Sequence: DRIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFKAGLLGTLEEMRD | ||||||
Region | 656-678 | Actin-binding | ||||
Sequence: LNKLMSNLRTTHPHFVRCIIPNE | ||||||
Region | 758-772 | Actin-binding | ||||
Sequence: KFGHTKVFFKAGLLG | ||||||
Domain | 782-811 | IQ | ||||
Sequence: LAKLITRTQAVCRGFLMRVEFQKMVQRRES | ||||||
Coiled coil | 840-1933 | |||||
Sequence: LLKSAETEKEMATMKEEFQKTKDELAKSEAKRKELEEKLVTLVQEKNDLQLQVQAESENLLDAEERCDQLIKAKFQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEELSGLDETIAKLTREKKALQEAHQQALDDLQAEEDKVNSLNKTKSKLEQQVEDLESSLEQEKKLRVDLERNKRKLEGDLKLAQESILDLENDKQQLDERLKKKDFEYCQLQSKVEDEQTLGLQFQKKIKELQARIEELEEEIEAERATRAKTEKQRSDYARELEELSERLEEAGGVTSTQIELNKKREAEFLKLRRDLEEATLQHEAMVAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLEIDDLSSSMESVSKSKANLEKICRTLEDQLSEARGKNEEIQRSLSELTTQKSRLQTEAGELSRQLEEKESIVSQLSRSKQAFTQQTEELKRQLEEENKAKNALAHALQSSRHDCDLLREQYEEEQEGKAELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDSEEQVEAVNAKCASLEKTKQRLQGEVEDLMVDVERANSLAAALDKKQRNFDKVLAEWKTKCEESQAELEASLKESRSLSTELFKLKNAYEEALDQLETVKRENKNLEQEIADLTEQIAENGKTIHELEKSRKQIELEKADIQLALEEAEAALEHEEAKILRIQLELTQVKSEIDRKIAEKDEEIEQLKRNYQRTVETMQSALDAEVRSRNEAIRLKKKMEGDLNEIEIQLSHANRQAAETLKHLRSVQGQLKDTQLHLDDALRGQEDLKEQLAIVERRANLLQAEVEELRATLEQTERARKLAEQELLDSNERVQLLHTQNTSLIHTKKKLETDLMQLQSEVEDASRDARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLETRIRELEFELEGEQKKNTESVKGLRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQVKVKSYKRQAEEADEQANAHLTKFRKAQHELEEAEERADIAESQVNKLRAKTRDFTSSRM |
Domain
The rodlike tail sequence is highly repetitive, showing cycles of a 28-residue repeat pattern composed of 4 heptapeptides, characteristic for alpha-helical coiled coils.
Limited proteolysis of myosin heavy chain produces 1 light meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment (S2).
Sequence similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,940
- Mass (Da)223,905
- Last updated2009-07-07 v3
- ChecksumB7D6AF219E88E5C8
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 327 | in Ref. 1; CAA32167 | ||||
Sequence: A → R | ||||||
Sequence conflict | 732 | in Ref. 1; CAA32167 | ||||
Sequence: P → L | ||||||
Sequence conflict | 1331 | in Ref. 4; CAA35942 | ||||
Sequence: A → G | ||||||
Sequence conflict | 1391-1392 | in Ref. 1; CAA32167 and 3; CAA31492 | ||||
Sequence: KK → QE | ||||||
Sequence conflict | 1608-1609 | in Ref. 4; CAA35942 | ||||
Sequence: SR → RA | ||||||
Sequence conflict | 1663-1664 | in Ref. 3; CAA31492 | ||||
Sequence: RG → QT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X13988 EMBL· GenBank· DDBJ | CAA32167.1 EMBL· GenBank· DDBJ | mRNA | ||
AC002347 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
X13100 EMBL· GenBank· DDBJ | CAA31492.1 EMBL· GenBank· DDBJ | mRNA | ||
X51593 EMBL· GenBank· DDBJ | CAA35942.1 EMBL· GenBank· DDBJ | mRNA | ||
X15696 EMBL· GenBank· DDBJ | CAA33731.1 EMBL· GenBank· DDBJ | mRNA |