ID MYO6_HUMAN Reviewed; 1294 AA.
AC Q9UM54; A6H8V4; E1P540; Q5TEM5; Q5TEM6; Q5TEM7; Q9BZZ7; Q9UEG2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 4.
DT 01-MAY-2013, entry version 134.
DE RecName: Full=Unconventional myosin-VI;
DE AltName: Full=Unconventional myosin-6;
GN Name=MYO6; Synonyms=KIAA0389;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9259267; DOI=10.1093/hmg/6.8.1225;
RA Avraham K.B., Hasson T., Sobe T., Balsara B., Testa J.R.,
RA Skvorak A.B., Morton C.C., Copeland N.G., Jenkins N.A.;
RT "Characterization of unconventional MYO6, the human homologue of the
RT gene responsible for deafness in Snell's waltzer mice.";
RL Hum. Mol. Genet. 6:1225-1231(1997).
RN [2]
RP SEQUENCE REVISION.
RA Avraham K.B.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kuehn M.H., Hageman G.S.;
RT "Genomic organization of the human myosin VI gene (MYO6), a candidate
RT gene for neurosensory and storage disorders.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 2 AND 5).
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1102-1294 (ISOFORM 6).
RC TISSUE=Salivary gland;
RX PubMed=16344560; DOI=10.1101/gr.4039406;
RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T.,
RA Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
RA Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
RA Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
RA Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
RA Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
RT "Diversification of transcriptional modulation: large-scale
RT identification and characterization of putative alternative promoters
RT of human genes.";
RL Genome Res. 16:55-65(2006).
RN [9]
RP FUNCTION.
RX PubMed=10519557; DOI=10.1038/46835;
RA Wells A.L., Lin A.W., Chen L.-Q., Safer D., Cain S.M., Hasson T.,
RA Carragher B.O., Milligan R.A., Sweeney H.L.;
RT "Myosin VI is an actin-based motor that moves backwards.";
RL Nature 401:505-508(1999).
RN [10]
RP FUNCTION IN ENDOCYTOSIS, SUBCELLULAR LOCATION, AND ALTERNATIVE
RP SPLICING.
RX PubMed=11447109; DOI=10.1093/emboj/20.14.3676;
RA Buss F., Arden S.D., Lindsay M., Luzio J.P., Kendrick-Jones J.;
RT "Myosin VI isoform localized to clathrin-coated vesicles with a role
RT in clathrin-mediated endocytosis.";
RL EMBO J. 20:3676-3684(2001).
RN [11]
RP INTERACTION WITH DAB2.
RX PubMed=11967127; DOI=10.1034/j.1600-0854.2002.30503.x;
RA Morris S.M., Arden S.D., Roberts R.C., Kendrick-Jones J., Cooper J.A.,
RA Luzio J.P., Buss F.;
RT "Myosin VI binds to and localises with Dab2, potentially linking
RT receptor-mediated endocytosis and the actin cytoskeleton.";
RL Traffic 3:331-341(2002).
RN [12]
RP INTERACTION WITH CFTR.
RX PubMed=15247260; DOI=10.1074/jbc.M403141200;
RA Swiatecka-Urban A., Boyd C., Coutermarsh B., Karlson K.H., Barnaby R.,
RA Aschenbrenner L., Langford G.M., Hasson T., Stanton B.A.;
RT "Myosin VI regulates endocytosis of the cystic fibrosis transmembrane
RT conductance regulator.";
RL J. Biol. Chem. 279:38025-38031(2004).
RN [13]
RP SUBUNIT.
RX PubMed=15044955; DOI=10.1038/sj.emboj.7600180;
RA Lister I., Schmitz S., Walker M., Trinick J., Buss F., Veigel C.,
RA Kendrick-Jones J.;
RT "A monomeric myosin VI with a large working stroke.";
RL EMBO J. 23:1729-1738(2004).
RN [14]
RP FUNCTION.
RX PubMed=16949370; DOI=10.1016/j.molcel.2006.07.005;
RA Vreugde S., Ferrai C., Miluzio A., Hauben E., Marchisio P.C.,
RA Crippa M.P., Bussi M., Biffo S.;
RT "Nuclear myosin VI enhances RNA polymerase II-dependent
RT transcription.";
RL Mol. Cell 23:749-755(2006).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16507995; DOI=10.1128/MCB.26.6.2175-2186.2006;
RA Jung E.J., Liu G., Zhou W., Chen X.;
RT "Myosin VI is a mediator of the p53-dependent cell survival pathway.";
RL Mol. Cell. Biol. 26:2175-2186(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP VARIANT DFNA22 TYR-442.
RX PubMed=11468689; DOI=10.1086/323156;
RA Melchionda S., Ahituv N., Bisceglia L., Sobe T., Glaser F.,
RA Rabionet R., Arbones M.L., Notarangelo A., Di Iorio E., Carella M.,
RA Zelante L., Estivill X., Avraham K.B., Gasparini P.;
RT "MYO6, the human homologue of the gene responsible for deafness in
RT Snell's waltzer mice, is mutated in autosomal dominant nonsyndromic
RT hearing loss.";
RL Am. J. Hum. Genet. 69:635-640(2001).
RN [18]
RP VARIANT DFNB37 VAL-216.
RX PubMed=12687499; DOI=10.1086/375122;
RA Ahmed Z.M., Morell R.J., Riazuddin S., Gropman A., Shaukat S.,
RA Ahmad M.M., Mohiddin S.A., Fananapazir L., Caruso R.C., Husnain T.,
RA Khan S.N., Riazuddin S., Griffith A.J., Friedman T.B., Wilcox E.R.;
RT "Mutations of MYO6 are associated with recessive deafness, DFNB37.";
RL Am. J. Hum. Genet. 72:1315-1322(2003).
RN [19]
RP VARIANT DFNHCM ARG-246.
RX PubMed=15060111; DOI=10.1136/jmg.2003.011973;
RA Mohiddin S.A., Ahmed Z.M., Griffith A.J., Tripodi D., Friedman T.B.,
RA Fananapazir L., Morell R.J.;
RT "Novel association of hypertrophic cardiomyopathy, sensorineural
RT deafness, and a mutation in unconventional myosin VI (MYO6).";
RL J. Med. Genet. 41:309-314(2004).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase
CC activity. Unconventional myosins serve in intracellular movements.
CC Myosin 6 is a reverse-direction motor protein that moves towards
CC the minus-end of actin filaments. Has slow rate of actin-activated
CC ADP release due to weak ATP binding. Functions in a variety of
CC intracellular processes such as vesicular membrane trafficking and
CC cell migration. Required for the structural integrity of the Golgi
CC apparatus via the p53-dependent pro-survival pathway. Appears to
CC be involved in a very early step of clathrin-mediated endocytosis
CC in polarized epithelial cells. May act as a regulator of F-actin
CC dynamics. May play a role in transporting DAB2 from the plasma
CC membrane to specific cellular targets. Required for structural
CC integrity of inner ear hair cells (By similarity).
CC -!- SUBUNIT: Homodimer. Binding to calmodulin through a unique insert,
CC not found in other myosins, located in the neck region between the
CC motor domain and the IQ domain appears to contribute to the
CC directionality reversal. This interaction occurs only if the C-
CC terminal lobe of calmodulin is occupied by calcium. Interaction
CC with F-actin/ACTN1 occurs only at the apical brush border domain
CC of the proximal tubule cells (By similarity). Interacts with DAB2.
CC In vitro, the C-terminal globular tail binds a C-terminal region
CC of DAB2. Interacts with CFTR. Forms a complex with CFTR and DAB2
CC in the apical membrane of epithelial cells. Interacts with OPTN
CC (By similarity).
CC -!- INTERACTION:
CC P98082:DAB2; NbExp=3; IntAct=EBI-350606, EBI-1171238;
CC P98078:Dab2 (xeno); NbExp=4; IntAct=EBI-350606, EBI-1391846;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC membrane; Peripheral membrane protein. Golgi apparatus (By
CC similarity). Nucleus. Cytoplasm, perinuclear region. Membrane,
CC clathrin-coated pit. Cell projection, ruffle membrane; Peripheral
CC membrane protein. Note=Also present in endocyctic vesicles, and
CC membrane ruffles. Translocates from membrane ruffles, endocytic
CC vesicles and cytoplasm to Golgi apparatus, perinuclear membrane
CC and nucleus through induction by p53 and p53-induced DNA damage.
CC Recruited into membrane ruffles from cell surface by EGF-
CC stimulation. Colocalizes with DAB2 in clathrin-coated
CC pits/vesicles. Colocalizes with OPTN at the Golgi complex and in
CC vesicular structures close to the plasma membrane (By similarity).
CC -!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasmic vesicle, clathrin-
CC coated vesicle membrane.
CC -!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasmic vesicle, clathrin-
CC coated vesicle membrane. Cell projection, ruffle membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=3;
CC IsoId=Q9UM54-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9UM54-1; Sequence=VSP_022332;
CC Name=2;
CC IsoId=Q9UM54-2; Sequence=VSP_007985;
CC Name=4;
CC IsoId=Q9UM54-4; Sequence=VSP_022333;
CC Name=5;
CC IsoId=Q9UM54-5; Sequence=VSP_007985, VSP_022333;
CC Name=6;
CC IsoId=Q9UM54-6; Sequence=VSP_042208;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues examined including
CC heart, brain, placenta, pancreas, spleen, thymus, prostate,
CC testis, ovary, small intestine and colon. Highest levels in brain,
CC pancreas, testis and small intestine. Also expressed in fetal
CC brain and cochlea. Isoform 1 and isoform 2, containing the small
CC insert, and isoform 4, containing neither insert, are expressed in
CC unpolarized epithelial cells.
CC -!- DOMAIN: Divided into three regions: a N-terminal motor (head)
CC domain, followed by a neck domain consisting of a calmodulin-
CC binding linker domain and a single IQ motif, and a C-terminal tail
CC region with a coiled-coil and a unique globular domain required
CC for interaction with other proteins.
CC -!- PTM: Phosphorylation in the motor domain, induced by EGF, results
CC in translocation of MYO6 from the cell surface to membrane ruffles
CC and affects F-actin dynamics. Phosphorylated in vitro by p21-
CC activated kinase (PAK) (By similarity).
CC -!- DISEASE: Deafness, autosomal dominant, 22 (DFNA22) [MIM:606346]: A
CC form of non-syndromic sensorineural hearing loss. Sensorineural
CC deafness results from damage to the neural receptors of the inner
CC ear, the nerve pathways to the brain, or the area of the brain
CC that receives sound information. DFNA22 is progressive and
CC postlingual, with onset during childhood. By the age of
CC approximately 50 years, affected individuals invariably have
CC profound sensorineural deafness. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, autosomal recessive, 37 (DFNB37) [MIM:607821]:
CC A form of non-syndromic sensorineural hearing loss. Sensorineural
CC deafness results from damage to the neural receptors of the inner
CC ear, the nerve pathways to the brain, or the area of the brain
CC that receives sound information. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, sensorineural, with hypertrophic cardiomyopathy
CC (DFNHCM) [MIM:606346]: An autosomal dominant sensorineural
CC deafness associated with hypertrophic cardiomyopathy. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Contains 1 IQ domain.
CC -!- SIMILARITY: Contains 1 myosin head-like domain.
CC -!- CAUTION: Represents a unconventional myosin. This protein should
CC not be confused with the conventional myosin-6 (MYH6).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20843.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; U90236; AAC51654.2; -; mRNA.
DR EMBL; AF229111; AAK00229.1; -; Genomic_DNA.
DR EMBL; AF229082; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229083; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229084; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229085; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229086; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229087; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229088; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229089; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229090; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229091; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229092; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229093; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229094; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229095; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229096; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229097; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229098; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229099; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229100; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229101; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229102; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229103; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229104; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229105; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229106; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229107; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229108; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229109; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AF229110; AAK00229.1; JOINED; Genomic_DNA.
DR EMBL; AL109897; CAI19520.1; -; Genomic_DNA.
DR EMBL; AL136093; CAI19520.1; JOINED; Genomic_DNA.
DR EMBL; AL109897; CAI19521.1; -; Genomic_DNA.
DR EMBL; AL136093; CAI19521.1; JOINED; Genomic_DNA.
DR EMBL; AL109897; CAI19522.1; -; Genomic_DNA.
DR EMBL; AL136093; CAI19522.1; JOINED; Genomic_DNA.
DR EMBL; AL136093; CAI42824.1; -; Genomic_DNA.
DR EMBL; AL109897; CAI42824.1; JOINED; Genomic_DNA.
DR EMBL; AL136093; CAI42825.1; -; Genomic_DNA.
DR EMBL; AL109897; CAI42825.1; JOINED; Genomic_DNA.
DR EMBL; AL136093; CAI42826.1; -; Genomic_DNA.
DR EMBL; AL109897; CAI42826.1; JOINED; Genomic_DNA.
DR EMBL; AB002387; BAA20843.2; ALT_INIT; mRNA.
DR EMBL; CH471051; EAW48730.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48731.1; -; Genomic_DNA.
DR EMBL; BC146764; AAI46765.1; -; mRNA.
DR EMBL; BP333853; -; NOT_ANNOTATED_CDS; mRNA.
DR IPI; IPI00008455; -.
DR IPI; IPI00069126; -.
DR IPI; IPI00642722; -.
DR IPI; IPI00816452; -.
DR IPI; IPI00816461; -.
DR RefSeq; NP_004990.3; NM_004999.3.
DR UniGene; Hs.149387; -.
DR ProteinModelPortal; Q9UM54; -.
DR DIP; DIP-33123N; -.
DR IntAct; Q9UM54; 13.
DR MINT; MINT-239443; -.
DR STRING; 9606.ENSP00000358994; -.
DR PhosphoSite; Q9UM54; -.
DR DMDM; 122065628; -.
DR PaxDb; Q9UM54; -.
DR PRIDE; Q9UM54; -.
DR Ensembl; ENST00000369975; ENSP00000358992; ENSG00000196586.
DR Ensembl; ENST00000369977; ENSP00000358994; ENSG00000196586.
DR Ensembl; ENST00000369985; ENSP00000359002; ENSG00000196586.
DR GeneID; 4646; -.
DR KEGG; hsa:4646; -.
DR UCSC; uc003pig.1; human.
DR UCSC; uc003pih.1; human.
DR UCSC; uc003pii.1; human.
DR CTD; 4646; -.
DR GeneCards; GC06P076515; -.
DR HGNC; HGNC:7605; MYO6.
DR HPA; CAB010762; -.
DR MIM; 600970; gene.
DR MIM; 606346; phenotype.
DR MIM; 607821; phenotype.
DR neXtProt; NX_Q9UM54; -.
DR Orphanet; 90635; Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
DR Orphanet; 90636; Autosomal recessive nonsyndromic sensorineural deafness type DFNB.
DR Orphanet; 228012; Progressive sensorineural hearing loss - hypertrophic cardiomyopathy.
DR PharmGKB; PA31410; -.
DR eggNOG; COG5022; -.
DR HOVERGEN; HBG003523; -.
DR InParanoid; Q9UM54; -.
DR KO; K10358; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_13685; Neuronal System.
DR ChiTaRS; MYO6; human.
DR GenomeRNAi; 4646; -.
DR NextBio; 17908; -.
DR ArrayExpress; Q9UM54; -.
DR Bgee; Q9UM54; -.
DR CleanEx; HS_MYO6; -.
DR Genevestigator; Q9UM54; -.
DR GermOnline; ENSG00000196586; Homo sapiens.
DR GO; GO:0030424; C:axon; IEA:Compara.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Compara.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016461; C:unconventional myosin complex; TAS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0060001; F:minus-end directed microfilament motor activity; NAS:UniProtKB.
DR GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR GO; GO:0042491; P:auditory receptor cell differentiation; IEA:Compara.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Compara.
DR GO; GO:0016358; P:dendrite development; IEA:Compara.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0014047; P:glutamate secretion; IEA:Compara.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Compara.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IEA:Compara.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IEA:Compara.
DR GO; GO:0051046; P:regulation of secretion; IMP:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Compara.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR GO; GO:0007416; P:synapse assembly; IEA:Compara.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR PROSITE; PS50096; IQ; FALSE_NEG.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cell membrane; Cell projection; Coated pit; Coiled coil;
KW Complete proteome; Cytoplasm; Cytoplasmic vesicle; Deafness;
KW Disease mutation; Endocytosis; Golgi apparatus; Hearing; Membrane;
KW Motor protein; Myosin; Non-syndromic deafness; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1 1294 Unconventional myosin-VI.
FT /FTId=PRO_0000123464.
FT DOMAIN 1 759 Myosin head-like.
FT DOMAIN 814 834 IQ.
FT NP_BIND 151 158 ATP (Potential).
FT REGION 273 317 Responsible for slow ATPase activity (By
FT similarity).
FT REGION 665 672 Actin-binding (Potential).
FT REGION 782 810 Required for binding calmodulin (By
FT similarity).
FT REGION 1116 1118 Interaction with OPTN.
FT COILED 864 1023 Potential.
FT COMPBIAS 920 1027 Glu-rich.
FT MOD_RES 405 405 Phosphothreonine (By similarity).
FT VAR_SEQ 1037 1068 Missing (in isoform 2 and isoform 5).
FT /FTId=VSP_007985.
FT VAR_SEQ 1037 1045 Missing (in isoform 1).
FT /FTId=VSP_022332.
FT VAR_SEQ 1147 1156 DFAPFLNNSP -> A (in isoform 6).
FT /FTId=VSP_042208.
FT VAR_SEQ 1147 1155 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_022333.
FT VARIANT 216 216 E -> V (in DFNB37; dbSNP:rs28936390).
FT /FTId=VAR_016209.
FT VARIANT 246 246 H -> R (in DFNHCM; dbSNP:rs28936391).
FT /FTId=VAR_029988.
FT VARIANT 442 442 C -> Y (in DFNA22).
FT /FTId=VAR_012110.
FT CONFLICT 1156 1156 P -> A (in Ref. 5; CAI42826).
SQ SEQUENCE 1294 AA; 149691 MW; 3A8966E6864B8576 CRC64;
MEDGKPVWAP HPTDGFQMGN IVDIGPDSLT IEPLNQKGKT FLALINQVFP AEEDSKKDVE
DNCSLMYLNE ATLLHNIKVR YSKDRIYTYV ANILIAVNPY FDIPKIYSSE AIKSYQGKSL
GTRPPHVFAI ADKAFRDMKV LKMSQSIIVS GESGAGKTEN TKFVLRYLTE SYGTGQDIDD
RIVEANPLLE AFGNAKTVRN NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK
EERNYHIFYR LCAGASEDIR EKLHLSSPDN FRYLNRGCTR YFANKETDKQ ILQNRKSPEY
LKAGSMKDPL LDDHGDFIRM CTAMKKIGLD DEEKLDLFRV VAGVLHLGNI DFEEAGSTSG
GCNLKNKSAQ SLEYCAELLG LDQDDLRVSL TTRVMLTTAG GTKGTVIKVP LKVEQANNAR
DALAKTVYSH LFDHVVNRVN QCFPFETSSY FIGVLDIAGF EYFEHNSFEQ FCINYCNEKL
QQFFNERILK EEQELYQKEG LGVNEVHYVD NQDCIDLIEA KLVGILDILD EENRLPQPSD
QHFTSAVHQK HKDHFRLTIP RKSKLAVHRN IRDDEGFIIR HFAGAVCYET TQFVEKNNDA
LHMSLESLIC ESRDKFIREL FESSTNNNKD TKQKAGKLSF ISVGNKFKTQ LNLLLDKLRS
TGASFIRCIK PNLKMTSHHF EGAQILSQLQ CSGMVSVLDL MQGGYPSRAS FHELYNMYKK
YMPDKLARLD PRLFCKALFK ALGLNENDYK FGLTKVFFRP GKFAEFDQIM KSDPDHLAEL
VKRVNHWLTC SRWKKVQWCS LSVIKLKNKI KYRAEACIKM QKTIRMWLCK RRHKPRIDGL
VKVGTLKKRL DKFNEVVSVL KDGKPEMNKQ IKNLEISIDT LMAKIKSTMM TQEQIQKEYD
ALVKSSEELL SALQKKKQQE EEAERLRRIQ EEMEKERKRR EEDEKRRRKE EEERRMKLEM
EAKRKQEEEE RKKREDDEKR IQAEVEAQLA RQKEEESQQQ AVLEQERRDR ELALRIAQSE
AELISDEAQA DLALRRSLDS YPVSKNDGTR PKMTPEQMAK EMSEFLSRGP AVLATKAAAG
TKKYDLSKWK YAELRDTINT SCDIELLAAC REEFHRRLKV YHAWKSKNKK RNTETEQRAP
KSVTDYDFAP FLNNSPQQNP AAQIPARQRE IEMNRQQRFF RIPFIRPADQ YKDPQSKKKG
WWYAHFDGPW IARQMELHPD KPPILLVAGK DDMEMCELNL EETGLTRKRG AEILPRQFEE
IWERCGGIQY LQNAIESRQA RPTYATAMLQ SLLK
//
