Q5SUA5 · MYO1G_MOUSE

  • Protein
    Unconventional myosin-Ig
  • Gene
    Myo1g
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Caution

It is uncertain whether Met-1 or Met-7 is the initiator.
Represents an unconventional myosin. This protein should not be confused with the conventional myosin-1 (MYH1).

Features

Showing features for binding site.

110241002003004005006007008009001,000
TypeIDPosition(s)Description
Binding site108-115ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentfilopodium
Cellular Componentlamellipodium
Cellular Componentleading edge membrane
Cellular Componentmicrovillus
Cellular Componentmyosin complex
Cellular Componentnucleoplasm
Cellular Componentphagocytic cup
Cellular Componentplasma membrane
Molecular Functionactin binding
Molecular FunctionATP binding
Molecular Functioncalmodulin binding
Molecular Functioncytoskeletal motor activity
Molecular Functionphosphatidylinositol-3,4,5-trisphosphate binding
Molecular Functionphosphatidylinositol-3,4-bisphosphate binding
Molecular Functionphosphatidylinositol-4,5-bisphosphate binding
Biological Processcell gliding
Biological Processcell-substrate adhesion
Biological Processestablishment of localization in cell
Biological Processexocytosis
Biological ProcessFc-gamma receptor signaling pathway involved in phagocytosis
Biological Processphagocytosis
Biological ProcessT cell meandering migration
Biological ProcessT cell mediated immunity

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Unconventional myosin-Ig

Gene names

    • Name
      Myo1g

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • NOD
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q5SUA5
  • Secondary accessions
    • Q8BIT8
    • Q8BJ17
    • Q8BJ65
    • Q8R019
    • Q91ZI1

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Peripheral membrane protein
Note: Recruited to Fc-gamma receptor (Fc-gamma-R) phagocytic cup (PubMed:23038771).
In T-cells, transiently accumulates in discrete areas at the plasma membrane of migrating cells or when membranes are deformed (PubMed:25083865).

Keywords

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.

TypeIDPosition(s)Description
Mutagenesis111Does not affect localization to the plasma membrane.
Mutagenesis167Does not affect localization to the plasma membrane.
Mutagenesis883Abolishes localization to phagocytic cups; when associated with A-893.
Mutagenesis893Abolishes localization to phagocytic cups; when associated with A-883.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003403181-1024Unconventional myosin-Ig

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

Interaction

Subunit

Interacts with calmodulin; via its IQ motifs.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain15-713Myosin motor
Region590-612Actin-binding
Domain716-745IQ
Domain830-1023TH1
Region999-1024Disordered
Compositional bias1008-1024Polar residues

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,024
  • Mass (Da)
    117,227
  • Last updated
    2004-12-21 v1
  • Checksum
    F24181A6D37EE9EA
MLAVGRMEDEEGPEYGKPDFVLLDQLTMEDFMKNLELRFEKGRIYTYIGEVLVSVNPYQELPLYGPEAIAKYQGRELYERPPHLYAVANAAYKAMKRRSRDTCIVISGESGAGKTEASKHIMQYIAAVTNPSQRAEVERVKNVLLKSTCVLEAFGNARTNRNHNSSRFGKYMDINFDFKGDPVGGHIHSYLLEKSRVLKQHVGERNFHAFYQLLRGSEDQELQGLHLERNPAVYNFTRQGAGLNMGVHNALDSDEKSHQGVMEAMRIIGFSPDEVESIHRILAAILHLGNIEFVETEENGPQKGGLEVADEALVGYVAKLTATPRDLVLRTLLARTVASGGREVIEKSHTVAEASYARDACAKAMYQRLFEWVVNKINSIMEPRNRDPRCDGKDTVIGVLDIYGFEVFPVNSFEQFCINYCNEKLQQLFIQLILKQEQEEYEREGIAWQTIEYFNNATIVELVEQPHRGILAVLDEACSTAGPITDRIFLQTLDTHHRHHPHYSSRQLCPTDKTMEFGRDFQIKHYAGDVTYSVEGFIDKNRDSLFQDFKRLLYNSVDPTLRAMWPDGQQDITEVTKRPLTAGTLFKNSMVALVENLASKEPFYVRCIKPNEDKVAGRLDEAHCRHQVEYLGLLENVRVRRAGFASRQPYPRFLLRYKMTCEYTWPNHLLGSDRDAVSALLEQHGLQGDVAFGHSKLFIRSPRTLVTLEQSRARLIPIIVLLLQKAWRGTLARWHCRRLRAIYTIMRWFRRHKVRAHLIELQRRFQAARQPPLYGRDLVWPTPPAVLQPFQDTCRVLFSRWRARQLVKNIPPSDMIQIKAKVAAMGALQGLRQDWGCQRAWARDYLSSDTDNPTASHLFAEQLKALREKDGFGSVLFSSHVRKVNRFRKSRDRALLLTDRYLYKLEPGRQYRVMRAVPLEAVTGLSVTSGRDQLVVLHAQGYDDLVVCLHRSQPPLDNRIGELVGMLAAHCQGEGRTLEVRVSDCIPLSQRGARRLISVEPRPEQPEPDFQSSRSTFTLLWPSH

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A8Y5I5A8Y5I5_MOUSEMyo1g99
D6RHL4D6RHL4_MOUSEMyo1g65
D6RGA2D6RGA2_MOUSEMyo1g73

Sequence caution

The sequence BAC31139.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict425in Ref. 1; BAC27149
Sequence conflict467in Ref. 1; BAC40093
Sequence conflict816in Ref. 1; BAC40093
Compositional bias1008-1024Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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