V5NBV4 · TPM_MACRS
- ProteinTropomyosin Mac r 1.0101
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids284 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Tropomyosin, in association with the troponin complex, plays a central role in the calcium dependent regulation of muscle contraction.
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 | actin filament | |
Molecular Function | actin filament binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | actin filament organization | |
Biological Process | locomotion | |
Biological Process | muscle contraction | |
Biological Process | muscle system process | |
Biological Process | regulation of muscle contraction |
Keywords
- Molecular function
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTropomyosin Mac r 1.0101
- Alternative names
- Allergen nameMac r 1.0101
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Crustacea > Multicrustacea > Malacostraca > Eumalacostraca > Eucarida > Decapoda > Pleocyemata > Caridea > Palaemonoidea > Palaemonidae > Macrobrachium
Accessions
- Primary accessionV5NBV4
- Secondary accessions
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Allergenic properties
Causes an allergic reaction in human. Natural protein binds to IgE in patients allergic to giant fresh water prawn (M.rosenbergii) (PubMed:23569834, PubMed:27001653, PubMed:34255496).
Recombinant protein binds to IgE in 77% of the 13 Thai children tested allergic to both seawater prawn P.monodon and freshwater prawn M.rosenbergii. Cross-reacts with P.monodon tropomyosin allergen Pen m 1 (PubMed:27001653).
Cross-reacts with tropomyosins of freshwater crustaceans M.lanchesteri, C.quadricarinatus and P.clarkii (PubMed:34255496).
Recombinant protein binds to IgE in 77% of the 13 Thai children tested allergic to both seawater prawn P.monodon and freshwater prawn M.rosenbergii. Cross-reacts with P.monodon tropomyosin allergen Pen m 1 (PubMed:27001653).
Cross-reacts with tropomyosins of freshwater crustaceans M.lanchesteri, C.quadricarinatus and P.clarkii (PubMed:34255496).
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 44-45 | |||||
Sequence: FS → HN |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Protein family/group databases
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000455697 | 1-284 | Tropomyosin Mac r 1.0101 | |||
Sequence: MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANNRAEKSEEEVFSLQKRMQQLENDLDSVQEALLKANQHLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDELDQTFSELSGY |
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-42 | Disordered | ||||
Sequence: MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANNRAEKSEEE | ||||||
Coiled coil | 1-273 | |||||
Sequence: MDAIKKKMQAMKLEKDNAMDRADTLEQQNKEANNRAEKSEEEVFSLQKRMQQLENDLDSVQEALLKANQHLEEKDKALSNAEGEVAALNRRIQLLEEDLERSEERLNTATTKLAEASQAADESERMRKVLENRSLSDEERMDALENQLKEARFLAEEADRKYDEVARKLAMVEADLERAEERAETGESKIVELEEELRVVGNNLKSLEVSEEKANQREEAYKEQIKTLTNKLKAAEARAEFAERSVQKLQKEVDRLEDELVNEKEKYKSITDE |
Domain
The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.
Sequence similarities
Belongs to the tropomyosin family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length284
- Mass (Da)32,829
- Last updated2014-02-19 v1
- Checksum8ACA4C565D73B144
Keywords
- Technical term