P12845 · MYO2_CAEEL
- ProteinMyosin-2
- Genemyo-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1947 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Muscle contraction.
Miscellaneous
There are four different myosin heavy chains in C.elegans.
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 | 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 | microfilament motor activity | |
Biological Process | muscle contraction | |
Biological Process | sarcomere organization |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMyosin-2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionP12845
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Thick filaments of the myofibrils.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000123381 | 1-1947 | Myosin-2 | |||
Sequence: MDYENDPGWKYLRRSREEMLQDQSRAYDSKKNVWIPDSEDGYIEGVITKTAGDNVTVSIGQGAEKTVKKDVVQEMNPPKFEKTEDMSNLTFLNDASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGESGAGKTENTKKVISYFAAVGAAQQETFGAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPKGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHALIVEVWQDYTTQEEAAAAAAKGTAGAKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLAADESIIGKTDAKKGSALMLARLVKEKKLEEENFRVGLTKVFFKAGIVAHLEDLRDQSLAQLITGLQAQIRWYYQTIERKRRVEKITALKIIQRNIRSWAELRTWVWFKLYGKVKPLVNSGKIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETEGLIGADEFDEVKKRQNQKTSEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTRANAEQK | ||||||
Modified residue | 125 | N6,N6,N6-trimethyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-77 | Myosin N-terminal SH3-like | ||||
Sequence: DSKKNVWIPDSEDGYIEGVITKTAGDNVTVSIGQGAEKTVKKDVVQEMNP | ||||||
Domain | 81-794 | Myosin motor | ||||
Sequence: EKTEDMSNLTFLNDASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGESGAGKTENTKKVISYFAAVGAAQQETFGAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQAELIIDGINDKEEHQLTDEAFDILKFTPTEKMECYRLVAAMMHMGNMKFKQRPREEQAEPDGTDDAERAAKCFGIDSEEFLKALTRPRVKVGNEWVNKGQNIEQVNWAVGAMAKGLYSRIFNWLVKKCNQTLDQKGISRDHFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIIAMLDEECIVPKATDLTLAQKLIDQHLGKHPNFEKPKPPKGKQAEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVTVMKASKEHALIVEVWQDYTTQEEAAAAAAKGTAGAKKKGKSGSFMTVSMLYRESLNKLMTMLHSTHPHFIRCIIPNEKKASGVIDAGLVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYALLAADESIIGKTDAKKGSALMLARLVKEKKLEEENFRVGLTKVFFKAGIVAHLEDLRD | ||||||
Region | 668-690 | Actin-binding | ||||
Sequence: LNKLMTMLHSTHPHFIRCIIPNE | ||||||
Region | 773-787 | Actin-binding | ||||
Sequence: RVGLTKVFFKAGIVA | ||||||
Region | 856-1947 | Rodlike tail (S2 and LMM domains) | ||||
Sequence: VNSGKIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETEGLIGADEFDEVKKRQNQKTSEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTRANAEQK | ||||||
Coiled coil | 856-1947 | |||||
Sequence: VNSGKIEAQYEKLQETVATLKDTVVQEEEKKRQLQEGAERLNKETADLLAQLEASKGSTREVEERMTAMNEQKVALEGKLADASKKLEVEEARAVEINKQKKLVEAECADLKKNCQDVDLSLRKVEAEKNAKEHQIRALQDEMRQQDENISKLNKERKNQEEQNKKLTEDLQAAEEQNLAANKLKAKLMQSLEDSEQTMEREKRNRADMDKNKRKAEGELKIAQETLEELNKSKSDAENALRRKETELHTLGMKLEDEQAAVAKLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDELTEQLEDQARATAAQIELGKKKDAELTKLRRDLEESGLKFGEQLTVLKKKGSDAIQELSDQIEQLQKQKGRIEKEKGHMQREFDESSAALDQEAKLRADQERIAKGYEVRLLELRLKADEQSRQLQDFVSSKGRLNSENSDLARQVEELEAKIQAANRLKLQFSNELDHAKRQAEEESRERQNLSNLSKNLARELEQLKESIEDEVAGKNEASRQLSKASVELDQWRTKFETEGLIGADEFDEVKKRQNQKTSEIQDALDACNAKIVALENARSRLTAEADANRLEAEHHAQAVSSLEKKQKAFDKVIDEWKKKVDDLYLELDGAQRDARQLSGEAHKLRGQHDTLADQVEGLRRENKSLSDETRDLTESLSEGGRATHALSKNLRRLEMEKEELQRGLDEAEAALESEESKALRCQIEVSQIRAEIEKRIAEKEEEFENHRKVHQQTIDSIQATLDSETKAKSELFRVKKKLEADINELEIALDHANKANEDAQKNIRRYLDQIRELQQTVDEEQKRREEFREHLLAAERKLAVAKQEQEELIVKLEALERARRVVESSVKEHQEHNNELNSQNVALAAAKSQLDNEIALLNSDIAEAHTELSASEDRGRRAASDAAKLAEDLRHEQEQSQQLERFKKQLESAVKDLQERADAAEAAVMKGGAKAIQKAEQRLKAFQSDLETESRRAGEASKTLARADRKVREFEFQVAEDKKNYDKLQELVEKLTAKLKLQKKQLEEAEEQANSHLSKYRTVQLSLETAEERADSAEQCLVRIRSRTRANAEQK | ||||||
Region | 1047-1075 | Disordered | ||||
Sequence: LEDSEQTMEREKRNRADMDKNKRKAEGEL | ||||||
Compositional bias | 1049-1075 | Basic and acidic residues | ||||
Sequence: DSEQTMEREKRNRADMDKNKRKAEGEL | ||||||
Region | 1119-1161 | Disordered | ||||
Sequence: KLQKGIQQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDE | ||||||
Compositional bias | 1125-1161 | Basic and acidic residues | ||||
Sequence: QQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDE | ||||||
Region | 1231-1253 | Disordered | ||||
Sequence: GRIEKEKGHMQREFDESSAALDQ | ||||||
Compositional bias | 1516-1533 | Basic and acidic residues | ||||
Sequence: RENKSLSDETRDLTESLS | ||||||
Region | 1516-1537 | Disordered | ||||
Sequence: RENKSLSDETRDLTESLSEGGR |
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
- Length1,947
- Mass (Da)223,048
- Last updated2004-11-09 v2
- Checksum09024B39E16DEA78
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 132 | in Ref. 1; CAA30855 | ||||
Sequence: D → E | ||||||
Sequence conflict | 137 | in Ref. 3; AAA28121 | ||||
Sequence: M → I | ||||||
Sequence conflict | 286 | in Ref. 1; CAA30855 and 3; AAA28121 | ||||
Sequence: C → S | ||||||
Sequence conflict | 420 | in Ref. 1; CAA30855 | ||||
Sequence: N → K | ||||||
Compositional bias | 1049-1075 | Basic and acidic residues | ||||
Sequence: DSEQTMEREKRNRADMDKNKRKAEGEL | ||||||
Compositional bias | 1125-1161 | Basic and acidic residues | ||||
Sequence: QQDEARVKDLHDQLADEKDARQRADRSRADQQAEYDE | ||||||
Sequence conflict | 1248 | in Ref. 1; CAA30855 | ||||
Sequence: S → C | ||||||
Sequence conflict | 1271-1273 | in Ref. 1; CAA30855 | ||||
Sequence: RLL → QTS | ||||||
Compositional bias | 1516-1533 | Basic and acidic residues | ||||
Sequence: RENKSLSDETRDLTESLS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X08066 EMBL· GenBank· DDBJ | CAA30855.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z68119 EMBL· GenBank· DDBJ | CAA92197.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z68117 EMBL· GenBank· DDBJ | CAA92197.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M37233 EMBL· GenBank· DDBJ | AAA28121.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M37235 EMBL· GenBank· DDBJ | AAA28122.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M37236 EMBL· GenBank· DDBJ | AAA28123.1 EMBL· GenBank· DDBJ | Genomic DNA |