Q5SUA5 · MYO1G_MOUSE
- ProteinUnconventional myosin-Ig
- GeneMyo1g
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1024 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Unconventional myosin required during immune response for detection of rare antigen-presenting cells by regulating T-cell migration (PubMed:25083865).
Unconventional myosins are actin-based motor molecules with ATPase activity and serve in intracellular movements. Acts as a regulator of T-cell migration by generating membrane tension, enforcing cell-intrinsic meandering search, thereby enhancing detection of rare antigens during lymph-node surveillance, enabling pathogen eradication (PubMed:25083865).
Also required in B-cells, where it regulates different membrane/cytoskeleton-dependent processes (PubMed:24310084).
Involved in Fc-gamma receptor (Fc-gamma-R) phagocytosis (PubMed:23038771).
Unconventional myosins are actin-based motor molecules with ATPase activity and serve in intracellular movements. Acts as a regulator of T-cell migration by generating membrane tension, enforcing cell-intrinsic meandering search, thereby enhancing detection of rare antigens during lymph-node surveillance, enabling pathogen eradication (PubMed:25083865).
Also required in B-cells, where it regulates different membrane/cytoskeleton-dependent processes (PubMed:24310084).
Involved in Fc-gamma receptor (Fc-gamma-R) phagocytosis (PubMed:23038771).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | filopodium | |
Cellular Component | lamellipodium | |
Cellular Component | leading edge membrane | |
Cellular Component | microvillus | |
Cellular Component | myosin complex | |
Cellular Component | nucleoplasm | |
Cellular Component | phagocytic cup | |
Cellular Component | plasma membrane | |
Molecular Function | actin binding | |
Molecular Function | ATP binding | |
Molecular Function | calmodulin binding | |
Molecular Function | cytoskeletal motor activity | |
Molecular Function | phosphatidylinositol-3,4,5-trisphosphate binding | |
Molecular Function | phosphatidylinositol-3,4-bisphosphate binding | |
Molecular Function | phosphatidylinositol-4,5-bisphosphate binding | |
Biological Process | cell gliding | |
Biological Process | cell-substrate adhesion | |
Biological Process | establishment of localization in cell | |
Biological Process | exocytosis | |
Biological Process | Fc-gamma receptor signaling pathway involved in phagocytosis | |
Biological Process | phagocytosis | |
Biological Process | T cell meandering migration | |
Biological Process | T cell mediated immunity |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameUnconventional myosin-Ig
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ5SUA5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
T-cells display impaired migration patterns and are less efficient in scanning and evaluating antigen-presenting cells. T-cells show global reduction in membrane tension, while their homeostatic tissue distribution and responsiveness to T-cell receptor (TCR) engagement are unaffected. However, T-cells move faster and straighter, leading to defects in detection of antigen-presenting cells, specifically for detection of rare antigens.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 111 | Does not affect localization to the plasma membrane. | ||||
Sequence: G → R | ||||||
Mutagenesis | 167 | Does not affect localization to the plasma membrane. | ||||
Sequence: R → C | ||||||
Mutagenesis | 883 | Abolishes localization to phagocytic cups; when associated with A-893. | ||||
Sequence: K → A | ||||||
Mutagenesis | 893 | Abolishes localization to phagocytic cups; when associated with A-883. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 57 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000340318 | 1-1024 | Unconventional myosin-Ig | |||
Sequence: MLAVGRMEDEEGPEYGKPDFVLLDQLTMEDFMKNLELRFEKGRIYTYIGEVLVSVNPYQELPLYGPEAIAKYQGRELYERPPHLYAVANAAYKAMKRRSRDTCIVISGESGAGKTEASKHIMQYIAAVTNPSQRAEVERVKNVLLKSTCVLEAFGNARTNRNHNSSRFGKYMDINFDFKGDPVGGHIHSYLLEKSRVLKQHVGERNFHAFYQLLRGSEDQELQGLHLERNPAVYNFTRQGAGLNMGVHNALDSDEKSHQGVMEAMRIIGFSPDEVESIHRILAAILHLGNIEFVETEENGPQKGGLEVADEALVGYVAKLTATPRDLVLRTLLARTVASGGREVIEKSHTVAEASYARDACAKAMYQRLFEWVVNKINSIMEPRNRDPRCDGKDTVIGVLDIYGFEVFPVNSFEQFCINYCNEKLQQLFIQLILKQEQEEYEREGIAWQTIEYFNNATIVELVEQPHRGILAVLDEACSTAGPITDRIFLQTLDTHHRHHPHYSSRQLCPTDKTMEFGRDFQIKHYAGDVTYSVEGFIDKNRDSLFQDFKRLLYNSVDPTLRAMWPDGQQDITEVTKRPLTAGTLFKNSMVALVENLASKEPFYVRCIKPNEDKVAGRLDEAHCRHQVEYLGLLENVRVRRAGFASRQPYPRFLLRYKMTCEYTWPNHLLGSDRDAVSALLEQHGLQGDVAFGHSKLFIRSPRTLVTLEQSRARLIPIIVLLLQKAWRGTLARWHCRRLRAIYTIMRWFRRHKVRAHLIELQRRFQAARQPPLYGRDLVWPTPPAVLQPFQDTCRVLFSRWRARQLVKNIPPSDMIQIKAKVAAMGALQGLRQDWGCQRAWARDYLSSDTDNPTASHLFAEQLKALREKDGFGSVLFSSHVRKVNRFRKSRDRALLLTDRYLYKLEPGRQYRVMRAVPLEAVTGLSVTSGRDQLVVLHAQGYDDLVVCLHRSQPPLDNRIGELVGMLAAHCQGEGRTLEVRVSDCIPLSQRGARRLISVEPRPEQPEPDFQSSRSTFTLLWPSH |
Proteomic databases
PTM databases
Expression
Tissue specificity
Specifically expressed in hematopoietic cells. Detected in adult tissues of the immune system such as thymus, lymph nodes and spleen, but not in brain, lung, heart, liver, small intestine, testis and kidney (at protein level). Highly expressed in T-lymphocytes; constitutes the most highly expressed class I myosin in naive CD4 and CD8 T-cells. Also present in B-lymphocytes.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 15-713 | Myosin motor | ||||
Sequence: YGKPDFVLLDQLTMEDFMKNLELRFEKGRIYTYIGEVLVSVNPYQELPLYGPEAIAKYQGRELYERPPHLYAVANAAYKAMKRRSRDTCIVISGESGAGKTEASKHIMQYIAAVTNPSQRAEVERVKNVLLKSTCVLEAFGNARTNRNHNSSRFGKYMDINFDFKGDPVGGHIHSYLLEKSRVLKQHVGERNFHAFYQLLRGSEDQELQGLHLERNPAVYNFTRQGAGLNMGVHNALDSDEKSHQGVMEAMRIIGFSPDEVESIHRILAAILHLGNIEFVETEENGPQKGGLEVADEALVGYVAKLTATPRDLVLRTLLARTVASGGREVIEKSHTVAEASYARDACAKAMYQRLFEWVVNKINSIMEPRNRDPRCDGKDTVIGVLDIYGFEVFPVNSFEQFCINYCNEKLQQLFIQLILKQEQEEYEREGIAWQTIEYFNNATIVELVEQPHRGILAVLDEACSTAGPITDRIFLQTLDTHHRHHPHYSSRQLCPTDKTMEFGRDFQIKHYAGDVTYSVEGFIDKNRDSLFQDFKRLLYNSVDPTLRAMWPDGQQDITEVTKRPLTAGTLFKNSMVALVENLASKEPFYVRCIKPNEDKVAGRLDEAHCRHQVEYLGLLENVRVRRAGFASRQPYPRFLLRYKMTCEYTWPNHLLGSDRDAVSALLEQHGLQGDVAFGHSKLFIRSPRTLVTLEQSRA | ||||||
Region | 590-612 | Actin-binding | ||||
Sequence: MVALVENLASKEPFYVRCIKPNE | ||||||
Domain | 716-745 | IQ | ||||
Sequence: IPIIVLLLQKAWRGTLARWHCRRLRAIYTI | ||||||
Domain | 830-1023 | TH1 | ||||
Sequence: GLRQDWGCQRAWARDYLSSDTDNPTASHLFAEQLKALREKDGFGSVLFSSHVRKVNRFRKSRDRALLLTDRYLYKLEPGRQYRVMRAVPLEAVTGLSVTSGRDQLVVLHAQGYDDLVVCLHRSQPPLDNRIGELVGMLAAHCQGEGRTLEVRVSDCIPLSQRGARRLISVEPRPEQPEPDFQSSRSTFTLLWPS | ||||||
Region | 999-1024 | Disordered | ||||
Sequence: VEPRPEQPEPDFQSSRSTFTLLWPSH | ||||||
Compositional bias | 1008-1024 | Polar residues | ||||
Sequence: PDFQSSRSTFTLLWPSH |
Domain
The myosin tail domain mediates binding to phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2), phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) and binds to membranous compartments. It is required for recruitment to Fc-gamma receptor (Fc-gamma-R) phagocytic cups.
Sequence similarities
Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,024
- Mass (Da)117,227
- Last updated2004-12-21 v1
- ChecksumF24181A6D37EE9EA
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 425 | in Ref. 1; BAC27149 | ||||
Sequence: L → Q | ||||||
Sequence conflict | 467 | in Ref. 1; BAC40093 | ||||
Sequence: H → R | ||||||
Sequence conflict | 816 | in Ref. 1; BAC40093 | ||||
Sequence: I → T | ||||||
Compositional bias | 1008-1024 | Polar residues | ||||
Sequence: PDFQSSRSTFTLLWPSH |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK030825 EMBL· GenBank· DDBJ | BAC27149.1 EMBL· GenBank· DDBJ | mRNA | ||
AK042033 EMBL· GenBank· DDBJ | BAC31139.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK088011 EMBL· GenBank· DDBJ | BAC40093.1 EMBL· GenBank· DDBJ | mRNA | ||
AL646047 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC028661 EMBL· GenBank· DDBJ | AAH28661.1 EMBL· GenBank· DDBJ | mRNA | ||
AF426468 EMBL· GenBank· DDBJ | AAL26548.1 EMBL· GenBank· DDBJ | mRNA |