Unconventional myosin-Va

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• actin binding Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Myosin V exhibits a high duty cycle and large unitary displacement."
    Moore J.R., Krementsova E.B., Trybus K.M., Warshaw D.M.
    J. Cell Biol. 155:625-635(2001) [PubMed] [Europe PMC] [Abstract]
  • "Myosin Va binding to neurofilaments is essential for correct myosin Va distribution and transport and neurofilament density."
    Rao M.V., Engle L.J., Mohan P.S., Yuan A., Qiu D., Cataldo A., Hassinger L., Jacobsen S., Lee V.M., Andreadis A., Julien J.P., Bridgman P.C., Nixon R.A.
    J. Cell Biol. 159:279-290(2002) [PubMed] [Europe PMC] [Abstract]
  • "The structural basis of myosin V processive movement as revealed by electron cryomicroscopy."
    Volkmann N., Liu H., Hazelwood L., Krementsova E.B., Lowey S., Trybus K.M., Hanein D.
    Mol. Cell 19:595-605(2005) [PubMed] [Europe PMC] [Abstract]
• actin filament binding Source: InterPro
• ATP binding Source: MGI
• ATP-dependent protein binding Source: MGI
• calcium-dependent protein binding Source: MGI
• calcium ion binding Source: MGIInferred from direct assayⁱ
  • "Myosin V: regulation by calcium, calmodulin, and the tail domain."
    Krementsov D.N., Krementsova E.B., Trybus K.M.
    J. Cell Biol. 164:877-886(2004) [PubMed] [Europe PMC] [Abstract]
• calmodulin binding Source: MGIInferred from direct assayⁱ
  • "Myosin V exhibits a high duty cycle and large unitary displacement."
    Moore J.R., Krementsova E.B., Trybus K.M., Warshaw D.M.
    J. Cell Biol. 155:625-635(2001) [PubMed] [Europe PMC] [Abstract]
  • "Myosin V: regulation by calcium, calmodulin, and the tail domain."
    Krementsov D.N., Krementsova E.B., Trybus K.M.
    J. Cell Biol. 164:877-886(2004) [PubMed] [Europe PMC] [Abstract]
  • "The high molecular weight neurofilament subunit plays an essential role in axonal outgrowth and stabilization."
    Lee S., Shea T.B.
    Biol Open 3:974-981(2014) [PubMed] [Europe PMC] [Abstract]
• disordered domain specific binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin."
    Geething N.C., Spudich J.A.
    J. Biol. Chem. 282:21518-21528(2007) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "The SAH domain extends the functional length of the myosin lever."
    Baboolal T.G., Sakamoto T., Forgacs E., White H.D., Jackson S.M., Takagi Y., Farrow R.E., Molloy J.E., Knight P.J., Sellers J.R., Peckham M.
    Proc. Natl. Acad. Sci. U.S.A. 106:22193-22198(2009) [PubMed] [Europe PMC] [Abstract]
  • "Influence of lever structure on myosin 5a walking."
    Oke O.A., Burgess S.A., Forgacs E., Knight P.J., Sakamoto T., Sellers J.R., White H., Trinick J.
    Proc. Natl. Acad. Sci. U.S.A. 107:2509-2514(2010) [PubMed] [Europe PMC] [Abstract]
• microfilament motor activity Source: MGIInferred from direct assayⁱ
  • "Myosin V exhibits a high duty cycle and large unitary displacement."
    Moore J.R., Krementsova E.B., Trybus K.M., Warshaw D.M.
    J. Cell Biol. 155:625-635(2001) [PubMed] [Europe PMC] [Abstract]
  • "Myosin V: regulation by calcium, calmodulin, and the tail domain."
    Krementsov D.N., Krementsova E.B., Trybus K.M.
    J. Cell Biol. 164:877-886(2004) [PubMed] [Europe PMC] [Abstract]
• motor activity Source: MGIInferred from direct assayⁱ
  • "Myosin V exhibits a high duty cycle and large unitary displacement."
    Moore J.R., Krementsova E.B., Trybus K.M., Warshaw D.M.
    J. Cell Biol. 155:625-635(2001) [PubMed] [Europe PMC] [Abstract]
• protein dimerization activity Source: MGI
• protein heterodimerization activity Source: MGI
• protein kinase binding Source: MGI
• Rab GTPase binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.11

    "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes."
    Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S., Hammer J.A., Xu T., Lippincott-Schwartz J.
    J. Cell Biol. 198:545-560(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN VESICULAR TRANSPORT, INTERACTION WITH RAB10.
• SNARE binding Source: MGI
• syntaxin-1 binding Source: MGI

GO - Biological processⁱ

• actin filament-based movement Source: MGIInferred from direct assayⁱ
  • "Myosin V: regulation by calcium, calmodulin, and the tail domain."
    Krementsov D.N., Krementsova E.B., Trybus K.M.
    J. Cell Biol. 164:877-886(2004) [PubMed] [Europe PMC] [Abstract]
• axo-dendritic protein transport Source: MGI
• cellular response to insulin stimulus Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.11

    "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes."
    Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S., Hammer J.A., Xu T., Lippincott-Schwartz J.
    J. Cell Biol. 198:545-560(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN VESICULAR TRANSPORT, INTERACTION WITH RAB10.
• chemical synaptic transmission Source: MGIInferred from mutant phenotypeⁱ
  • "Myosin Va is required for normal photoreceptor synaptic activity."
    Libby R.T., Lillo C., Kitamoto J., Williams D.S., Steel K.P.
    J. Cell. Sci. 117:4509-4515(2004) [PubMed] [Europe PMC] [Abstract]
• developmental pigmentation Source: MGIInferred from mutant phenotypeⁱ
  • "dsu functions in a MYO5A-independent pathway to suppress the coat color of dilute mice."
    O'Sullivan T.N., Wu X.S., Rachel R.A., Huang J.-D., Swing D.A., Matesic L.E., Hammer J.A. III, Copeland N.G., Jenkins N.A.
    Proc. Natl. Acad. Sci. U.S.A. 101:16831-16836(2004) [PubMed] [Europe PMC] [Abstract]
• endoplasmic reticulum localization Source: MGIInferred from mutant phenotypeⁱ
  • "The mouse neurological mutant flailer expresses a novel hybrid gene derived by exon shuffling between Gnb5 and Myo5a."
    Jones J.M., Huang J.D., Mermall V., Hamilton B.A., Mooseker M.S., Escayg A., Copeland N.G., Jenkins N.A., Meisler M.H.
    Hum. Mol. Genet. 9:821-828(2000) [PubMed] [Europe PMC] [Abstract]
  • "The dilute-lethal (dl) gene attacks a Ca2+ store in the dendritic spine of Purkinje cells in mice."
    Takagishi Y., Oda S., Hayasaka S., Dekker-Ohno K., Shikata T., Inouye M., Yamamura H.
    Neurosci. Lett. 215:169-172(1996) [PubMed] [Europe PMC] [Abstract]
• establishment of endoplasmic reticulum localization to postsynapse Source: SynGOInferred from direct assayⁱ
  • "Myosin-Va transports the endoplasmic reticulum into the dendritic spines of Purkinje neurons."
    Wagner W., Brenowitz S.D., Hammer J.A.
    Nat. Cell Biol. 13:40-48(2011) [PubMed] [Europe PMC] [Abstract]
• exocytosis Source: MGIInferred from mutant phenotypeⁱ
  • "Myosin Va transports dense core secretory vesicles in pancreatic MIN6 beta-cells."
    Varadi A., Tsuboi T., Rutter G.A.
    Mol. Biol. Cell 16:2670-2680(2005) [PubMed] [Europe PMC] [Abstract]
• hair follicle maturation Source: MGIInferred from mutant phenotypeⁱ
  • "Identification of genes important for cutaneous function revealed by a large scale reverse genetic screen in the mouse."
    DiTommaso T., Jones L.K., Cottle D.L., Gerdin A.K., Vancollie V.E., Watt F.M., Ramirez-Solis R., Bradley A., Steel K.P., Sundberg J.P., White J.K., Smyth I.M.
    PLoS Genet. 10:e1004705-e1004705(2014) [PubMed] [Europe PMC] [Abstract]
• insulin secretion Source: MGIInferred from mutant phenotypeⁱ
  • "Myosin Va transports dense core secretory vesicles in pancreatic MIN6 beta-cells."
    Varadi A., Tsuboi T., Rutter G.A.
    Mol. Biol. Cell 16:2670-2680(2005) [PubMed] [Europe PMC] [Abstract]
• locomotion involved in locomotory behavior Source: MGIInferred from mutant phenotypeⁱ
  • "Abnormal expression of tyrosine hydroxylase immunoreactivity in Purkinje cells precedes the onset of ataxia in dilute-lethal mice."
    Sawada K., Komatsu S., Haga H., Oda S., Fukui Y.
    Brain Res. 844:188-191(1999) [PubMed] [Europe PMC] [Abstract]
  • "The mouse neurological mutant flailer expresses a novel hybrid gene derived by exon shuffling between Gnb5 and Myo5a."
    Jones J.M., Huang J.D., Mermall V., Hamilton B.A., Mooseker M.S., Escayg A., Copeland N.G., Jenkins N.A., Meisler M.H.
    Hum. Mol. Genet. 9:821-828(2000) [PubMed] [Europe PMC] [Abstract]
• long-chain fatty acid biosynthetic process Source: MGIInferred from mutant phenotypeⁱ
  • "Alpha hydroxylation of lignoceric acid to cerebronic acid during brain development. Diminished hydroxylase activity in myelin-deficient mouse mutants."
    Murad S., Kishimoto Y.
    J. Biol. Chem. 250:5841-5846(1975) [PubMed] [Europe PMC] [Abstract]
• melanin biosynthetic process Source: MGIInferred from mutant phenotypeⁱ
  • "Chemical characterization of hair melanins in various coat-color mutants of mice."
    Ozeki H., Ito S., Wakamatsu K., Hirobe T.
    J. Invest. Dermatol. 105:361-366(1995) [PubMed] [Europe PMC] [Abstract]
• melanin metabolic process Source: MGIInferred from mutant phenotypeⁱ
  • "Effects of genic substitution at the agouti, brown, albino, dilute, and pink-eyed dilution loci on the proliferation and differentiation of mouse epidermal melanocytes in serum-free culture."
    Hirobe T., Wakamatsu K., Ito S.
    Eur. J. Cell Biol. 75:184-191(1998) [PubMed] [Europe PMC] [Abstract]
• melanocyte differentiation Source: MGIInferred from mutant phenotypeⁱ
  • Ref.1

    "Novel myosin heavy chain encoded by murine dilute coat colour locus."
    Mercer J.A., Seperack P.K., Strobel M.C., Copeland N.G., Jenkins N.A.
    Nature 349:709-712(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  • "Interaction of the murine dilute suppressor gene (dsu) with fourteen coat color mutations."
    Moore K.J., Swing D.A., Copeland N.G., Jenkins N.A.
    Genetics 125:421-430(1990) [PubMed] [Europe PMC] [Abstract]
  • "The murine dilute suppressor gene encodes a cell autonomous suppressor."
    Moore K.J., Swing D.A., Copeland N.G., Jenkins N.A.
    Genetics 138:491-497(1994) [PubMed] [Europe PMC] [Abstract]
• melanosome localization Source: MGIInferred from mutant phenotypeⁱ
  • "Rab27a regulates the peripheral distribution of melanosomes in melanocytes."
    Hume A.N., Collinson L.M., Rapak A., Gomes A.Q., Hopkins C.R., Seabra M.C.
    J. Cell Biol. 152:795-808(2001) [PubMed] [Europe PMC] [Abstract]
  • "Missense mutations in the globular tail of myosin-Va in dilute mice partially impair binding of Slac2-a/melanophilin."
    Fukuda M., Kuroda T.S.
    J. Cell. Sci. 117:583-591(2004) [PubMed] [Europe PMC] [Abstract]
  • "Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution."
    Provance D.W. Jr., Wei M., Ipe V., Mercer J.A.
    Proc. Natl. Acad. Sci. U.S.A. 93:14554-14558(1996) [PubMed] [Europe PMC] [Abstract]
• melanosome transport Source: MGIInferred from direct assayⁱ
  • "Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor."
    Wu X., Bowers B., Wei Q., Kocher B., Hammer J.A.
    J. Cell. Sci. 110:847-859(1997) [PubMed] [Europe PMC] [Abstract]
• myelination Source: MGIInferred from mutant phenotypeⁱ
  • "Alpha hydroxylation of lignoceric acid to cerebronic acid during brain development. Diminished hydroxylase activity in myelin-deficient mouse mutants."
    Murad S., Kishimoto Y.
    J. Biol. Chem. 250:5841-5846(1975) [PubMed] [Europe PMC] [Abstract]
• odontogenesis Source: MGIInferred from direct assayⁱ
  • "Missense mutations in the globular tail of myosin-Va in dilute mice partially impair binding of Slac2-a/melanophilin."
    Fukuda M., Kuroda T.S.
    J. Cell. Sci. 117:583-591(2004) [PubMed] [Europe PMC] [Abstract]
• pigmentation Source: MGIInferred from mutant phenotypeⁱ
  • "Effect of genic substitution on the incorporation of tyrosine into the melanin of mouse skin."
    COLEMAN D.L.
    Arch. Biochem. Biophys. 96:562-568(1962) [PubMed] [Europe PMC] [Abstract]
  • "The Effects of Genotype and Cell Environment on Melanoblast Differentiation in the House Mouse."
    Markert C.L., Silvers W.K.
    Genetics 41:429-450(1956) [PubMed] [Europe PMC] [Abstract]
  • "Interaction of the murine dilute suppressor gene (dsu) with fourteen coat color mutations."
    Moore K.J., Swing D.A., Copeland N.G., Jenkins N.A.
    Genetics 125:421-430(1990) [PubMed] [Europe PMC] [Abstract]
  • "Novel skin phenotypes revealed by a genome-wide mouse reverse genetic screen."
    Liakath-Ali K., Vancollie V.E., Heath E., Smedley D.P., Estabel J., Sunter D., Ditommaso T., White J.K., Ramirez-Solis R., Smyth I., Steel K.P., Watt F.M.
    Nat Commun 5:3540-3540(2014) [PubMed] [Europe PMC] [Abstract]
  • "Identification of genes important for cutaneous function revealed by a large scale reverse genetic screen in the mouse."
    DiTommaso T., Jones L.K., Cottle D.L., Gerdin A.K., Vancollie V.E., Watt F.M., Ramirez-Solis R., Bradley A., Steel K.P., Sundberg J.P., White J.K., Smyth I.M.
    PLoS Genet. 10:e1004705-e1004705(2014) [PubMed] [Europe PMC] [Abstract]
  • "Dilute suppressor dsu acts semidominantly to suppress the coat color phenotype of a deletion mutation, dl20J, of the murine dilute locus."
    Moore K.J., Seperack P.K., Strobel M.C., Swing D.A., Copeland N.G., Jenkins N.A.
    Proc. Natl. Acad. Sci. U.S.A. 85:8131-8135(1988) [PubMed] [Europe PMC] [Abstract]
  • "Somatic and germ-line reverse mutation rates of the retrovirus-induced dilute coat-color mutation of DBA mice."
    Seperack P.K., Strobel M.C., Corrow D.J., Jenkins N.A., Copeland N.G.
    Proc. Natl. Acad. Sci. U.S.A. 85:189-192(1988) [PubMed] [Europe PMC] [Abstract]
  • "Dilute-coat-color locus of mice: nucleotide sequence analysis of the d+2J and d+Ha revertant alleles."
    Hutchison K.W., Copeland N.G., Jenkins N.A.
    Mol. Cell. Biol. 4:2899-2904(1984) [PubMed] [Europe PMC] [Abstract]
  • "Excision of the DBA ecotropic provirus in dilute coat-color revertants of mice occurs by homologous recombination involving the viral LTRs."
    Copeland N.G., Hutchison K.W., Jenkins N.A.
    Cell 33:379-387(1983) [PubMed] [Europe PMC] [Abstract]
  • "Retroviral sequences located within an intron of the dilute gene alter dilute expression in a tissue-specific manner."
    Seperack P.K., Mercer J.A., Strobel M.C., Copeland N.G., Jenkins N.A.
    EMBO J. 14:2326-2332(1995) [PubMed] [Europe PMC] [Abstract]
  • "The murine dilute suppressor gene encodes a cell autonomous suppressor."
    Moore K.J., Swing D.A., Copeland N.G., Jenkins N.A.
    Genetics 138:491-497(1994) [PubMed] [Europe PMC] [Abstract]
  • "Molecular genetic dissection of mouse unconventional myosin-VA: head region mutations."
    Huang J.D., Cope M.J., Mermall V., Strobel M.C., Kendrick-Jones J., Russell L.B., Mooseker M.S., Copeland N.G., Jenkins N.A.
    Genetics 148:1951-1961(1998) [PubMed] [Europe PMC] [Abstract]
  • "Molecular genetic dissection of mouse unconventional myosin-VA: tail region mutations."
    Huang J.D., Mermall V., Strobel M.C., Russell L.B., Mooseker M.S., Copeland N.G., Jenkins N.A.
    Genetics 148:1963-1972(1998) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cellular response to insulin stimulus Source: MGI
• positive regulation of protein localization to plasma membrane Source: MGI
• positive regulation of vascular associated smooth muscle cell migration Source: MGI
• post-Golgi vesicle-mediated transport Source: MGI
• protein localization to plasma membrane Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.11

    "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes."
    Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S., Hammer J.A., Xu T., Lippincott-Schwartz J.
    J. Cell Biol. 198:545-560(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN VESICULAR TRANSPORT, INTERACTION WITH RAB10.
• regulation of exocytosis Source: MGI
• regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: MGIInferred from mutant phenotypeⁱ
  • "Local calcium release in dendritic spines required for long-term synaptic depression."
    Miyata M., Finch E.A., Khiroug L., Hashimoto K., Hayasaka S., Oda S.I., Inouye M., Takagishi Y., Augustine G.J., Kano M.
    Neuron 28:233-244(2000) [PubMed] [Europe PMC] [Abstract]
• regulation of postsynaptic cytosolic calcium ion concentration Source: SynGOInferred from direct assayⁱ
  • "Myosin-Va transports the endoplasmic reticulum into the dendritic spines of Purkinje neurons."
    Wagner W., Brenowitz S.D., Hammer J.A.
    Nat. Cell Biol. 13:40-48(2011) [PubMed] [Europe PMC] [Abstract]
• secretory granule localization Source: MGIInferred from mutant phenotypeⁱ
  • "Myosin Va transports dense core secretory vesicles in pancreatic MIN6 beta-cells."
    Varadi A., Tsuboi T., Rutter G.A.
    Mol. Biol. Cell 16:2670-2680(2005) [PubMed] [Europe PMC] [Abstract]
• synapse organization Source: MGIInferred from mutant phenotypeⁱ
  • "Myosin Va is required for normal photoreceptor synaptic activity."
    Libby R.T., Lillo C., Kitamoto J., Williams D.S., Steel K.P.
    J. Cell. Sci. 117:4509-4515(2004) [PubMed] [Europe PMC] [Abstract]
• vesicle-mediated transport Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.11

    "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes."
    Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S., Hammer J.A., Xu T., Lippincott-Schwartz J.
    J. Cell Biol. 198:545-560(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN VESICULAR TRANSPORT, INTERACTION WITH RAB10.
• vesicle transport along actin filament Source: MGI
• visual perception Source: MGIInferred from mutant phenotypeⁱ
  • "Myosin Va is required for normal photoreceptor synaptic activity."
    Libby R.T., Lillo C., Kitamoto J., Williams D.S., Steel K.P.
    J. Cell. Sci. 117:4509-4515(2004) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• actin binding Source: MGIInferred from direct assayⁱ
  • "Myosin V exhibits a high duty cycle and large unitary displacement."
    Moore J.R., Krementsova E.B., Trybus K.M., Warshaw D.M.
    J. Cell Biol. 155:625-635(2001) [PubMed] [Europe PMC] [Abstract]
  • "Myosin Va binding to neurofilaments is essential for correct myosin Va distribution and transport and neurofilament density."
    Rao M.V., Engle L.J., Mohan P.S., Yuan A., Qiu D., Cataldo A., Hassinger L., Jacobsen S., Lee V.M., Andreadis A., Julien J.P., Bridgman P.C., Nixon R.A.
    J. Cell Biol. 159:279-290(2002) [PubMed] [Europe PMC] [Abstract]
  • "The structural basis of myosin V processive movement as revealed by electron cryomicroscopy."
    Volkmann N., Liu H., Hazelwood L., Krementsova E.B., Lowey S., Trybus K.M., Hanein D.
    Mol. Cell 19:595-605(2005) [PubMed] [Europe PMC] [Abstract]
• actin filament binding Source: InterPro
• ATP-dependent protein binding Source: MGI
• calcium-dependent protein binding Source: MGI
• calmodulin binding Source: MGIInferred from direct assayⁱ
  • "Myosin V exhibits a high duty cycle and large unitary displacement."
    Moore J.R., Krementsova E.B., Trybus K.M., Warshaw D.M.
    J. Cell Biol. 155:625-635(2001) [PubMed] [Europe PMC] [Abstract]
  • "Myosin V: regulation by calcium, calmodulin, and the tail domain."
    Krementsov D.N., Krementsova E.B., Trybus K.M.
    J. Cell Biol. 164:877-886(2004) [PubMed] [Europe PMC] [Abstract]
  • "The high molecular weight neurofilament subunit plays an essential role in axonal outgrowth and stabilization."
    Lee S., Shea T.B.
    Biol Open 3:974-981(2014) [PubMed] [Europe PMC] [Abstract]
• disordered domain specific binding Source: CAFAInferred from physical interactionⁱ
  • "Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin."
    Geething N.C., Spudich J.A.
    J. Biol. Chem. 282:21518-21528(2007) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "The SAH domain extends the functional length of the myosin lever."
    Baboolal T.G., Sakamoto T., Forgacs E., White H.D., Jackson S.M., Takagi Y., Farrow R.E., Molloy J.E., Knight P.J., Sellers J.R., Peckham M.
    Proc. Natl. Acad. Sci. U.S.A. 106:22193-22198(2009) [PubMed] [Europe PMC] [Abstract]
  • "Influence of lever structure on myosin 5a walking."
    Oke O.A., Burgess S.A., Forgacs E., Knight P.J., Sakamoto T., Sellers J.R., White H., Trinick J.
    Proc. Natl. Acad. Sci. U.S.A. 107:2509-2514(2010) [PubMed] [Europe PMC] [Abstract]
• protein dimerization activity Source: MGI
• protein heterodimerization activity Source: MGI
• protein kinase binding Source: MGI
• Rab GTPase binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.11

    "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes."
    Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S., Hammer J.A., Xu T., Lippincott-Schwartz J.
    J. Cell Biol. 198:545-560(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN VESICULAR TRANSPORT, INTERACTION WITH RAB10.
• SNARE binding Source: MGI
• syntaxin-1 binding Source: MGI

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Coiled coil

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY 
        60         70         80         90        100
RLDPKTGELP HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY 
       110        120        130        140        150
TYCGIVLVAI NPYEQLPIYG EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM 
       160        170        180        190        200
ARDERNQSII VSGESGAGKT VSAKYAMRYF ATVSGSASEA NVEEKVLASN 
       210        220        230        240        250
PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR TYLLEKSRVV 
       260        270        280        290        300
FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADSFHYTKQ GGSPMIEGVD 
       310        320        330        340        350
DAKEMAHTRQ ACTLLGISES YQMGIFRILA GILHLGNVGF ASRDSDSCTI 
       360        370        380        390        400
PPKHEPLTIF CDLMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR 
       410        420        430        440        450
DALAKHIYAK LFNWIVDHVN QALHSAVKQH SFIGVLDIYG FETFEINSFE 
       460        470        480        490        500
QFCINYANEK LQQQFNMHVF KLEQEEYMKE QIPWTLIDFY DNQPCINLIE 
       510        520        530        540        550
SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK PRMSNKAFII 
       560        570        580        590        600
KHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS 
       610        620        630        640        650
PTSATSSGRT PLTRVPVKPT KGRPGQTAKE HKKTVGHQFR NSLHLLMETL 
       660        670        680        690        700
NATTPHYVRC IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR 
       710        720        730        740        750
WTYQEFFSRY RVLMKQKDVL GDRKQTCKNV LEKLILDKDK YQFGKTKIFF 
       760        770        780        790        800
RAGQVAYLEK LRADKLRAAC IRIQKTIRGW LLRKRYLCMQ RAAITVQRYV 
       810        820        830        840        850
RGYQARCYAK FLRRTKAATT IQKYWRMYVV RRRYKIRRAA TIVIQSYLRG 
       860        870        880        890        900
YLTRNRYRKI LREYKAVIIQ KRVRGWLART HYKRTMKAIV YLQCCFRRMM 
       910        920        930        940        950
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLMEKL 
       960        970        980        990       1000
TNLEGVYNSE TEKLRNDVER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE 
      1010       1020       1030       1040       1050
QTRSEKKSIE ERADKYKQET DQLVSNLKEE NTLLKQEKET LNHRIVEQAK 
      1060       1070       1080       1090       1100
EMTETMERKL VEETKQLELD LNDERLRYQN LLNEFSRLEE RYDDLKEEMT 
      1110       1120       1130       1140       1150
LMLNVPKPGH KRTDSTHSSN ESEYTFSSEF AETEDIAPRT EEPIEKKVPL 
      1160       1170       1180       1190       1200
DMSLFLKLQK RVTELEQEKQ LMQDELDRKE EQVFRSKAKE EERPQIRGAE 
      1210       1220       1230       1240       1250
LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME 
      1260       1270       1280       1290       1300
QLTSVSEELD VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ 
      1310       1320       1330       1340       1350
KMKDKGEIAQ AYIGLKETNR LLESQLQSQK RSHENEAEAL RGEIQSLKEE 
      1360       1370       1380       1390       1400
NNRQQQLLAQ NLQLPPEARI EASLQHEITR LTNENLYFEE LYADDPKKYQ 
      1410       1420       1430       1440       1450
SYRISLYKRM IDLMEQLEKQ DKTVRKLKKQ LKVFAKKIGE LEVGQMENIS 
      1460       1470       1480       1490       1500
PGQIIDEPIR PVNIPRKEKD FQGMLEYKRE DEQKLVKNLI LELKPRGVAV 
      1510       1520       1530       1540       1550
NLIPGLPAYI LFMCVRHADY LNDDQKVRSL LTSTINSIKK VLKKRGDDFE 
      1560       1570       1580       1590       1600
TVSFWLSNTC RFLHCLKQYS GEEGFMKHNT SRQNEHCLTN FDLAEYRQVL 
      1610       1620       1630       1640       1650
SDLAIQIYQQ LVRVLENILQ PMIVSGMLEH ETIQGVSGVK PTGLRKRTSS 
      1660       1670       1680       1690       1700
IADEGTYTLD SILRQLNSFH SVMCQHGMDP ELIKQVVKQM FYIVGAITLN 
      1710       1720       1730       1740       1750
NLLLRKDMCS WSKGMQIRYN VSQLEEWLRD KNLMNSGAKE TLEPLIQAAQ 
      1760       1770       1780       1790       1800
LLQVKKKTDD DAEAICSMCN ALTTAQIVKV LNLYTPVNEF EERVSVSFIR 
      1810       1820       1830       1840       1850
TIQMRLRDRK DSPQLLMDAK HIFPVTFPFN PSSLALETIQ IPASLGLGFI 

ARV                                                    

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families
3. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot