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Unconventional myosin-VIIa

 MYO7A_HUMAN             Reviewed;        2215 AA.
Q13402; B9A011; F8VUN5; P78427; Q13321; Q14785; Q92821; Q92822;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 2.
07-NOV-2018, entry version 212.
RecName: Full=Unconventional myosin-VIIa;
Name=MYO7A; Synonyms=USH1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 5; 6 AND 7), DEVELOPMENTAL
STAGE, AND VARIANTS CYS-1666 AND ILE-1954.
TISSUE=Retina;
PubMed=8622919; DOI=10.1073/pnas.93.8.3232;
Weil D., Levy G., Sahly I., Levi-Acobas F., Blanchard S.,
El-Amraoui A., Crozet F., Philippe H., Abitbol M., Petit C.;
"Human myosin VIIA responsible for the Usher 1B syndrome: a predicted
membrane-associated motor protein expressed in developing sensory
epithelia.";
Proc. Natl. Acad. Sci. U.S.A. 93:3232-3237(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND VARIANTS
CYS-1666 AND ILE-1954.
TISSUE=Testis;
PubMed=8884267; DOI=10.1006/geno.1996.0489;
Chen Z.-Y., Hasson T., Kelley P.M., Schwender B.J., Schwartz M.F.,
Ramakrishnan M., Kimberling W.J., Mooseker M.S., Corey D.P.;
"Molecular cloning and domain structure of human myosin-VIIa, the gene
product defective in usher syndrome 1B.";
Genomics 36:440-448(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 166-196.
TISSUE=Epithelium, Leukocyte, and Liver;
PubMed=8022818; DOI=10.1073/pnas.91.14.6549;
Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.;
"Identification and overlapping expression of multiple unconventional
myosin genes in vertebrate cell types.";
Proc. Natl. Acad. Sci. U.S.A. 91:6549-6553(1994).
[5]
ERRATUM.
PubMed=7972138; DOI=10.1073/pnas.91.24.11767c;
Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.;
Proc. Natl. Acad. Sci. U.S.A. 91:11767-11767(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1075.
TISSUE=Testis;
PubMed=7568224; DOI=10.1073/pnas.92.21.9815;
Hasson T., Heintzelman M.B., Santos-Sacchi J., Corey D.P.,
Mooseker M.S.;
"Expression in cochlea and retina of myosin VIIa, the gene product
defective in Usher syndrome type 1B.";
Proc. Natl. Acad. Sci. U.S.A. 92:9815-9819(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-117 (ISOFORM 8).
PubMed=10737800; DOI=10.1073/pnas.97.7.3491;
Dias Neto E., Correa R.G., Verjovski-Almeida S., Briones M.R.S.,
Nagai M.A., da Silva W. Jr., Zago M.A., Bordin S., Costa F.F.,
Goldman G.H., Carvalho A.F., Matsukuma A., Baia G.S., Simpson D.H.,
Brunstein A., de Oliveira P.S.L., Bucher P., Jongeneel C.V.,
O'Hare M.J., Soares F., Brentani R.R., Reis L.F.L., de Souza S.J.,
Simpson A.J.G.;
"Shotgun sequencing of the human transcriptome with ORF expressed
sequence tags.";
Proc. Natl. Acad. Sci. U.S.A. 97:3491-3496(2000).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 96-564 (ISOFORM 1), AND VARIANTS USH1B.
TISSUE=Retina;
PubMed=7870171; DOI=10.1038/374060a0;
Weil D., Blanchard S., Kaplan J., Guilford P., Gibson F., Walsh J.,
Mburu P., Varela A., Levilliers J., Weston M.D., Kelley P.M.,
Kimberling W.J., Wagenaar M., Levi-Acobas F., Larget-Piet D.,
Munnich A., Steel K.P., Brown S.D.M., Petit C.;
"Defective myosin VIIA gene responsible for Usher syndrome type 1B.";
Nature 374:60-61(1995).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-578.
PubMed=9070921; DOI=10.1006/geno.1996.4545;
Kelley P.M., Weston M.D., Chen Z.-Y., Orten D.J., Hasson T.,
Overbeck L.D., Pinnt J., Talmadge C.B., Ing P., Mooseker M.S.,
Corey D.P., Sumegi J., Kimberling W.J.;
"The genomic structure of the gene defective in Usher syndrome type Ib
(MYO7A).";
Genomics 40:73-79(1997).
[10]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=8842737; DOI=10.1093/hmg/5.8.1171;
El-Amraoui A., Sahly I., Picaud S., Sahel J., Abitbol M., Petit C.;
"Human Usher 1B/mouse shaker-1: the retinal phenotype discrepancy
explained by the presence/absence of myosin VIIA in the photoreceptor
cells.";
Hum. Mol. Genet. 5:1171-1178(1996).
[11]
INTERACTION WITH MYRIP.
PubMed=11964381; DOI=10.1093/embo-reports/kvf090;
El-Amraoui A., Schonn J.-S., Kuessel-Andermann P., Blanchard S.,
Desnos C., Henry J.-P., Wolfrum U., Darchen F., Petit C.;
"MyRIP, a novel Rab effector, enables myosin VIIa recruitment to
retinal melanosomes.";
EMBO Rep. 3:463-470(2002).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19643958; DOI=10.1167/iovs.09-4032;
Gibbs D., Diemer T., Khanobdee K., Hu J., Bok D., Williams D.S.;
"Function of MYO7A in the human RPE and the validity of shaker1 mice
as a model for Usher syndrome 1B.";
Invest. Ophthalmol. Vis. Sci. 51:1130-1135(2010).
[13]
FUNCTION, AND ACTIVITY REGULATION.
PubMed=21687988; DOI=10.1007/s00018-011-0749-8;
Heissler S.M., Manstein D.J.;
"Functional characterization of the human myosin-7a motor domain.";
Cell. Mol. Life Sci. 69:299-311(2012).
[14]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH RPE65.
PubMed=21493626; DOI=10.1093/hmg/ddr155;
Lopes V.S., Gibbs D., Libby R.T., Aleman T.S., Welch D.L., Lillo C.,
Jacobson S.G., Radu R.A., Steel K.P., Williams D.S.;
"The Usher 1B protein, MYO7A, is required for normal localization and
function of the visual retinoid cycle enzyme, RPE65.";
Hum. Mol. Genet. 20:2560-2570(2011).
[15]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH USH1C
AND USH1G, AND TISSUE SPECIFICITY.
PubMed=21709241; DOI=10.1073/pnas.1104161108;
Grati M., Kachar B.;
"Myosin VIIa and sans localization at stereocilia upper tip-link
density implicates these Usher syndrome proteins in
mechanotransduction.";
Proc. Natl. Acad. Sci. U.S.A. 108:11476-11481(2011).
[16]
INTERACTION WITH CIB2.
PubMed=23023331; DOI=10.1038/ng.2426;
Riazuddin S., Belyantseva I.A., Giese A.P., Lee K., Indzhykulian A.A.,
Nandamuri S.P., Yousaf R., Sinha G.P., Lee S., Terrell D., Hegde R.S.,
Ali R.A., Anwar S., Andrade-Elizondo P.B., Sirmaci A., Parise L.V.,
Basit S., Wali A., Ayub M., Ansar M., Ahmad W., Khan S.N., Akram J.,
Tekin M., Riazuddin S., Cook T., Buschbeck E.K., Frolenkov G.I.,
Leal S.M., Friedman T.B., Ahmed Z.M.;
"Alterations of the CIB2 calcium- and integrin-binding protein cause
Usher syndrome type 1J and nonsyndromic deafness DFNB48.";
Nat. Genet. 44:1265-1271(2012).
[17]
SAH DOMAIN.
PubMed=25122759; DOI=10.1074/jbc.M114.585679;
Wolny M., Batchelor M., Knight P.J., Paci E., Dougan L., Peckham M.;
"Stable single alpha-helices are constant force springs in proteins.";
J. Biol. Chem. 289:27825-27835(2014).
[18]
INTERACTION WITH MYH9, AND SUBCELLULAR LOCATION.
PubMed=27331610; DOI=10.7554/eLife.15258;
Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
Groves A.K., Bellen H.J.;
"The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder
proteins in the auditory organs of Drosophila and mammals.";
Elife 5:E15258-E15258(2016).
[19]
VARIANTS USH1B CYS-212; HIS-212; HIS-302; GLN-450; GLN-468 INS AND
LEU-503.
PubMed=8900236;
Weston M.D., Kelley P.M., Overbeck L.D., Wagenaar M., Orten D.J.,
Hasson T., Chen Z.-Y., Corey D.P., Mooseker M.S., Sumegi J.,
Cremers C., Moeller C., Jacobson S.G., Gorin M.B., Kimberling W.J.;
"Myosin VIIA mutation screening in 189 Usher syndrome type 1
patients.";
Am. J. Hum. Genet. 59:1074-1083(1996).
[20]
VARIANTS USH1B ARG-214; ASP-397 AND THR-826, AND POLYMORPHISM.
PubMed=9382091; DOI=10.1086/514899;
Adato A., Weil D., Kalinski H., Pel-Or Y., Ayadi H., Petit C.,
Korostishevsky M., Bonne-Tamir B.;
"Mutation profile of all 49 exons of the human myosin VIIA gene, and
haplotype analysis, in Usher 1B families from diverse origins.";
Am. J. Hum. Genet. 61:813-821(1997).
[21]
VARIANTS USH1B ARG-25; SER-955 AND GLU-2137, AND POLYMORPHISM.
PubMed=9002678; DOI=10.1093/hmg/6.1.111;
Levy G., Levi-Acobas F., Blanchard S., Gerber S., Larget-Piet D.,
Chenal V., Liu X.-Z., Newton V., Steel K.P., Brown S.D.M., Munnich A.,
Kaplan J., Petit C., Weil D.;
"Myosin VIIA gene: heterogeneity of the mutations responsible for
Usher syndrome type IB.";
Hum. Mol. Genet. 6:111-116(1997).
[22]
VARIANT DFNB2 PRO-244.
PubMed=9171832; DOI=10.1038/ng0697-188;
Liu X.-Z., Walsh J., Mburu P., Kendrick-Jones J., Cope M.J.,
Steel K.P., Brown S.D.M.;
"Mutations in the myosin VIIA gene cause non-syndromic recessive
deafness.";
Nat. Genet. 16:188-190(1997).
[23]
VARIANT DFNB2 ILE-599.
PubMed=9171833; DOI=10.1038/ng0697-191;
Weil D., Kuessel P., Blanchard S., Levy G., Levi-Acobas F., Drira M.,
Ayadi H., Petit C.;
"The autosomal recessive isolated deafness, DFNB2, and the Usher 1B
syndrome are allelic defects of the myosin-VIIA gene.";
Nat. Genet. 16:191-193(1997).
[24]
VARIANT DFNA11 886-ALA--LYS-888 DEL.
PubMed=9354784; DOI=10.1038/ng1197-268;
Liu X.-Z., Walsh J., Tamagawa Y., Kitamura K., Nishizawa M.,
Steel K.P., Brown S.D.M.;
"Autosomal dominant non-syndromic deafness caused by a mutation in the
myosin VIIA gene.";
Nat. Genet. 17:268-269(1997).
[25]
VARIANTS USH1B PRO-651 AND GLN-1602.
PubMed=9718356; DOI=10.1086/302026;
Liu X.-Z., Hope C., Walsh J., Newton V., Ke X.M., Liang C.Y., Xu L.R.,
Zhou J.M., Trump D., Steel K.P., Bundey S., Brown S.D.M.;
"Mutations in the myosin VIIA gene cause a wide phenotypic spectrum,
including atypical Usher syndrome.";
Am. J. Hum. Genet. 63:909-912(1998).
[26]
VARIANT USH1B PRO-1087.
PubMed=10364543; DOI=10.1086/302438;
Adato A., Kalinski H., Weil D., Chaib H., Korostishevsky M.,
Bonne-Tamir B.;
"Possible interaction between USH1B and USH3 gene products as implied
by apparent digenic deafness inheritance.";
Am. J. Hum. Genet. 65:261-265(1999).
[27]
VARIANTS USH1B, AND POLYMORPHISM.
PubMed=10094549;
DOI=10.1002/(SICI)1098-1004(1999)13:2<133::AID-HUMU5>3.0.CO;2-U;
Janecke A.R., Meins M., Sadeghi M., Grundmann K., Apfelstedt-Sylla E.,
Zrenner E., Rosenberg T., Gal A.;
"Twelve novel myosin VIIA mutations in 34 patients with Usher syndrome
type I: confirmation of genetic heterogeneity.";
Hum. Mutat. 13:133-140(1999).
[28]
VARIANT USH1B LYS-1170, AND VARIANT CYS-1719.
PubMed=10447383;
DOI=10.1002/(SICI)1098-1004(1999)14:2<181::AID-HUMU11>3.0.CO;2-3;
Cuevas J.M., Espinos C., Millan J.M., Sanchez F., Trujillo M.J.,
Ayuso C., Beneyto M., Najera C.;
"Identification of three novel mutations in the MYO7A gene.";
Hum. Mutat. 14:181-181(1999).
[29]
VARIANTS USH1B GLU-26; MET-67; PRO-90; ASN-134; CYS-241; LYS-269 DEL;
VAL-457; ASP-519; ASP-968; GLN-1240; PRO-1288; PHE-1346 DEL; TRP-1743;
PRO-1858; LEU-1887 AND ASP-2187.
PubMed=10930322; DOI=10.1006/exer.2000.0863;
Bharadwaj A.K., Kasztejna J.P., Huq S., Berson E.L., Dryja T.P.;
"Evaluation of the myosin VIIA gene and visual function in patients
with Usher syndrome type I.";
Exp. Eye Res. 71:173-181(2000).
[30]
VARIANTS USH1B ASP-397; LYS-1170; LYS-1327 AND 1347-ARG--PHE-1351 DEL,
AND VARIANTS MET-1566 AND CYS-1719.
PubMed=12112664; DOI=10.1002/humu.9042;
Najera C., Beneyto M., Blanca J., Aller E., Fontcuberta A.,
Millan J.M., Ayuso C.;
"Mutations in myosin VIIA (MYO7A) and usherin (USH2A) in Spanish
patients with Usher syndrome types I and II, respectively.";
Hum. Mutat. 20:76-77(2002).
[31]
VARIANT DFNA11 ILE-458.
PubMed=15221449; DOI=10.1007/s00439-004-1137-3;
Luijendijk M.W.J., Van Wijk E., Bischoff A.M.L.C., Krieger E.,
Huygen P.L.M., Pennings R.J.E., Brunner H.G., Cremers C.W.R.J.,
Cremers F.P.M., Kremer H.;
"Identification and molecular modelling of a mutation in the motor
head domain of myosin VIIA in a family with autosomal dominant hearing
impairment (DFNA11).";
Hum. Genet. 115:149-156(2004).
[32]
VARIANT DFNA11 CYS-853, INTERACTION WITH CALM, AND CHARACTERIZATION OF
VARIANT DFNA11 CYS-853.
PubMed=15300860; DOI=10.1002/humu.9272;
Bolz H., Bolz S.-S., Schade G., Kothe C., Mohrmann G., Hess M.,
Gal A.;
"Impaired calmodulin binding of myosin-7A causes autosomal dominant
hearing loss (DFNA11).";
Hum. Mutat. 24:274-275(2004).
[33]
VARIANT DFNA11 ARG-722.
PubMed=15121790; DOI=10.1136/jmg.2003.013557;
Street V.A., Kallman J.C., Kiemele K.L.;
"Modifier controls severity of a novel dominant low-frequency
MyosinVIIA (MYO7A) auditory mutation.";
J. Med. Genet. 41:E62-E62(2004).
[34]
VARIANTS USH1B ARG-25; MET-165; TRP-756; ASP-968 AND GLN-1883, AND
VARIANT SER-16.
PubMed=15660226; DOI=10.1007/s00439-004-1227-2;
Ouyang X.M., Yan D., Du L.L., Hejtmancik J.F., Jacobson S.G.,
Nance W.E., Li A.R., Angeli S., Kaiser M., Newton V., Brown S.D.M.,
Balkany T., Liu X.Z.;
"Characterization of Usher syndrome type I gene mutations in an Usher
syndrome patient population.";
Hum. Genet. 116:292-299(2005).
[35]
VARIANTS USH1B ASP-133; ARG-163; ARG-164; MET-165; THR-198; ALA-204;
ASP-519; LYS-1170; GLN-1240; PRO-1858; TRP-1873 AND PHE-1962 DEL, AND
VARIANTS MET-1566 AND CYS-1719.
PubMed=16679490; DOI=10.1136/jmg.2006.041954;
Roux A.-F., Faugere V., Le Guedard S., Pallares-Ruiz N., Vielle A.,
Chambert S., Marlin S., Hamel C., Gilbert B., Malcolm S.,
Claustres M.;
"Survey of the frequency of USH1 gene mutations in a cohort of Usher
patients shows the importance of cadherin 23 and protocadherin 15
genes and establishes a detection rate of above 90%.";
J. Med. Genet. 43:763-768(2006).
[36]
VARIANT ILE-193.
PubMed=21901789; DOI=10.1002/humu.21587;
Wang X., Wang H., Cao M., Li Z., Chen X., Patenia C., Gore A.,
Abboud E.B., Al-Rajhi A.A., Lewis A.R., Lupski J.R., Mardon G.,
Zhang K., Muzny D., Gibbs R.A., Chen R.;
"Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A
mutations in patients with Leber congenital amaurosis.";
Hum. Mutat. 32:1450-1459(2011).
[37]
INVOLVEMENT IN USH1B, AND VARIANT USH1B LYS-1248.
PubMed=23559863;
Liu F., Li P., Liu Y., Li W., Wong F., Du R., Wang L., Li C.,
Jiang F., Tang Z., Liu M.;
"Novel compound heterozygous mutations in MYO7A in a Chinese family
with Usher syndrome type 1.";
Mol. Vis. 19:695-701(2013).
[38]
VARIANTS USH1B MET-165 AND ARG-946.
PubMed=24831256; DOI=10.1371/journal.pone.0097808;
Rong W., Chen X., Zhao K., Liu Y., Liu X., Ha S., Liu W., Kang X.,
Sheng X., Zhao C.;
"Novel and recurrent MYO7A mutations in Usher syndrome type 1 and type
2.";
PLoS ONE 9:E97808-E97808(2014).
[39]
VARIANT ARG-158.
PubMed=26720455; DOI=10.1167/iovs.15-17473;
Kastner S., Thiemann I.J., Dekomien G., Petrasch-Parwez E.,
Schreiber S., Akkad D.A., Gerding W.M., Hoffjan S., Guenes S.,
Guenes S., Bagci H., Epplen J.T.;
"Exome Sequencing Reveals AGBL5 as Novel Candidate Gene and Additional
Variants for Retinitis Pigmentosa in Five Turkish Families.";
Invest. Ophthalmol. Vis. Sci. 56:8045-8053(2015).
[40]
VARIANT USH1B LYS-1812.
PubMed=25798947; DOI=10.1371/journal.pone.0120584;
Riahi Z., Bonnet C., Zainine R., Lahbib S., Bouyacoub Y.,
Bechraoui R., Marrakchi J., Hardelin J.P., Louha M., Largueche L.,
Ben Yahia S., Kheirallah M., Elmatri L., Besbes G., Abdelhak S.,
Petit C.;
"Whole exome sequencing identifies mutations in Usher syndrome genes
in profoundly deaf Tunisian patients.";
PLoS ONE 10:E0120584-E0120584(2015).
[41]
VARIANT DFNB2 ARG-652.
PubMed=28281779; DOI=10.1089/gtmb.2016.0328;
Wang R., Han S., Khan A., Zhang X.;
"Molecular Analysis of Twelve Pakistani Families with Nonsyndromic or
Syndromic Hearing Loss.";
Genet. Test. Mol. Biomarkers 21:316-321(2017).
[42]
VARIANT GLN-1602.
PubMed=28887846; DOI=10.1002/humu.23335;
Zhou X.L., He L.X., Yu L.J., Wang Y., Wang X.J., Wang E.D., Yang T.;
"Mutations in KARS cause early-onset hearing loss and
leukoencephalopathy: Potential pathogenic mechanism.";
Hum. Mutat. 38:1740-1750(2017).
-!- FUNCTION: Myosins are actin-based motor molecules with ATPase
activity. Unconventional myosins serve in intracellular movements.
Their highly divergent tails bind to membranous compartments,
which are then moved relative to actin filaments. In the retina,
plays an important role in the renewal of the outer photoreceptor
disks. Plays an important role in the distribution and migration
of retinal pigment epithelial (RPE) melanosomes and phagosomes,
and in the regulation of opsin transport in retinal
photoreceptors. In the inner ear, plays an important role in
differentiation, morphogenesis and organization of cochlear hair
cell bundles. Involved in hair-cell vesicle trafficking of
aminoglycosides, which are known to induce ototoxicity (By
similarity). Motor protein that is a part of the functional
network formed by USH1C, USH1G, CDH23 and MYO7A that mediates
mechanotransduction in cochlear hair cells. Required for normal
hearing. {ECO:0000250, ECO:0000269|PubMed:19643958,
ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:21687988,
ECO:0000269|PubMed:21709241}.
-!- ACTIVITY REGULATION: ATP hydrolysis is inhibited by Mg(2+),
already at a concentration of 0.4 mM.
{ECO:0000269|PubMed:21687988}.
-!- SUBUNIT: Might homodimerize in a two headed molecule through the
formation of a coiled-coil rod (By similarity). Identified in a
complex with USH1C and USH1G (PubMed:21709241). Interacts with
MYRIP (PubMed:11964381). Interacts with RPE65 (PubMed:21493626).
Interacts with CIB2 (PubMed:23023331). May interact with CALM
(PubMed:15300860). Interacts with WHRN (By similarity). Interacts
with PLEKHB1 (via PH domain) (By similarity). Interacts with
PCDH15 (By similarity). Interacts with TWF2 (By similarity).
Interacts with USH1G (By similarity). Interacts with Myh9 (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P97479,
ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:15300860,
ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:21709241,
ECO:0000269|PubMed:23023331}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P97479}.
Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P97479}. Cytoplasm,
cytoskeleton {ECO:0000250|UniProtKB:P97479}. Note=In the
photoreceptor cells, mainly localized in the inner and base of
outer segments as well as in the synaptic ending region
(PubMed:8842737). In retinal pigment epithelial cells colocalizes
with a subset of melanosomes, displays predominant localization to
stress fiber-like structures and some localization to cytoplasmic
puncta (PubMed:19643958, PubMed:27331610). Detected at the tip of
cochlear hair cell stereocilia (PubMed:21709241). The complex
formed by MYO7A, USH1C and USH1G colocalizes with F-actin
(PubMed:21709241). {ECO:0000269|PubMed:19643958,
ECO:0000269|PubMed:21709241, ECO:0000269|PubMed:27331610,
ECO:0000269|PubMed:8842737}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q13402-1; Sequence=Displayed;
Name=2;
IsoId=Q13402-2; Sequence=VSP_003360, VSP_045848;
Name=3;
IsoId=Q13402-3; Sequence=VSP_003356, VSP_003357;
Name=4;
IsoId=Q13402-4; Sequence=VSP_003355, VSP_003356, VSP_003357;
Name=5;
IsoId=Q13402-5; Sequence=VSP_003353, VSP_003354;
Name=6;
IsoId=Q13402-6; Sequence=VSP_003358;
Name=7;
IsoId=Q13402-7; Sequence=VSP_003359;
Name=8;
IsoId=Q13402-8; Sequence=VSP_053793, VSP_003360;
-!- TISSUE SPECIFICITY: Expressed in the pigment epithelium and the
photoreceptor cells of the retina. Also found in kidney, liver,
testis, cochlea, lymphocytes. Not expressed in brain.
{ECO:0000269|PubMed:19643958, ECO:0000269|PubMed:21493626,
ECO:0000269|PubMed:21709241}.
-!- DEVELOPMENTAL STAGE: Detected in optic cup in 5.5 weeks-old
embryos. Expressed in retinal pigment epithelium, cochlear and
vestibular neuroepithelia, and olfactory epithelium at 8 weeks. At
19 weeks, present in both pigment epithelium and photoreceptor
cells. At 24-28 weeks, expression in pigment epithelium and
photoreceptor cells increases. Present in pigment epithelium and
photoreceptor cells in adult. {ECO:0000269|PubMed:8622919,
ECO:0000269|PubMed:8842737}.
-!- DOMAIN: The SAH (single alpha-helix) region is characterized by a
high content of charged residues which are predicted to stabilize
the alpha-helical structure by ionic bonds.
{ECO:0000305|PubMed:25122759}.
-!- DISEASE: Usher syndrome 1B (USH1B) [MIM:276900]: USH is a
genetically heterogeneous condition characterized by the
association of retinitis pigmentosa with sensorineural deafness.
Age at onset and differences in auditory and vestibular function
distinguish Usher syndrome type 1 (USH1), Usher syndrome type 2
(USH2) and Usher syndrome type 3 (USH3). USH1 is characterized by
profound congenital sensorineural deafness, absent vestibular
function and prepubertal onset of progressive retinitis pigmentosa
leading to blindness. {ECO:0000269|PubMed:10094549,
ECO:0000269|PubMed:10364543, ECO:0000269|PubMed:10447383,
ECO:0000269|PubMed:10930322, ECO:0000269|PubMed:12112664,
ECO:0000269|PubMed:15660226, ECO:0000269|PubMed:16679490,
ECO:0000269|PubMed:23559863, ECO:0000269|PubMed:24831256,
ECO:0000269|PubMed:25798947, ECO:0000269|PubMed:7870171,
ECO:0000269|PubMed:8900236, ECO:0000269|PubMed:9002678,
ECO:0000269|PubMed:9382091, ECO:0000269|PubMed:9718356}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Deafness, autosomal recessive, 2 (DFNB2) [MIM:600060]: A
form of non-syndromic sensorineural hearing loss. Sensorineural
deafness results from damage to the neural receptors of the inner
ear, the nerve pathways to the brain, or the area of the brain
that receives sound information. {ECO:0000269|PubMed:28281779,
ECO:0000269|PubMed:9171832, ECO:0000269|PubMed:9171833}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Deafness, autosomal dominant, 11 (DFNA11) [MIM:601317]: A
form of non-syndromic sensorineural hearing loss. Sensorineural
deafness results from damage to the neural receptors of the inner
ear, the nerve pathways to the brain, or the area of the brain
that receives sound information. DFNA11 is characterized by onset
after complete speech acquisition and subsequent gradual
progression. {ECO:0000269|PubMed:15121790,
ECO:0000269|PubMed:15221449, ECO:0000269|PubMed:15300860,
ECO:0000269|PubMed:9354784}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
-!- CAUTION: Represents an unconventional myosin. This protein should
not be confused with the conventional myosin-7 (MYH7).
{ECO:0000305}.
-!- CAUTION: Originally predicted to contain a coiled coil domain but
proposed to contain a stable SAH domain instead. {ECO:0000305}.
-!- WEB RESOURCE: Name=Hereditary hearing loss homepage; Note=Gene
page;
URL="http://hereditaryhearingloss.org/main.aspx?c=.HHH&n=86162";
-!- WEB RESOURCE: Name=Mutations of the MYO7A gene; Note=Retina
International's Scientific Newsletter;
URL="http://www.retina-international.org/files/sci-news/myomut.htm";
-----------------------------------------------------------------------
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EMBL; U39226; AAB03679.1; -; mRNA.
EMBL; U55208; AAC50927.1; -; mRNA.
EMBL; U55209; AAC50722.1; -; mRNA.
EMBL; AP000752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L29146; AAA20909.1; -; mRNA.
EMBL; U34227; AAC50218.1; -; mRNA.
EMBL; BF869194; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AH006665; AAC51150.1; -; Genomic_DNA.
CCDS; CCDS53683.1; -. [Q13402-1]
CCDS; CCDS53684.1; -. [Q13402-2]
PIR; A59255; A59255.
PIR; A59257; A59257.
PIR; I61697; I61697.
RefSeq; NP_000251.3; NM_000260.3. [Q13402-1]
RefSeq; NP_001120652.1; NM_001127180.1. [Q13402-2]
UniGene; Hs.370421; -.
PDB; 5MV9; X-ray; 2.60 A; A=1702-2215.
PDBsum; 5MV9; -.
ProteinModelPortal; Q13402; -.
SMR; Q13402; -.
BioGrid; 110731; 13.
CORUM; Q13402; -.
ELM; Q13402; -.
IntAct; Q13402; 3.
MINT; Q13402; -.
STRING; 9606.ENSP00000386331; -.
iPTMnet; Q13402; -.
PhosphoSitePlus; Q13402; -.
BioMuta; MYO7A; -.
DMDM; 460018219; -.
EPD; Q13402; -.
PaxDb; Q13402; -.
PeptideAtlas; Q13402; -.
PRIDE; Q13402; -.
ProteomicsDB; 59375; -.
ProteomicsDB; 59376; -. [Q13402-2]
ProteomicsDB; 59377; -. [Q13402-3]
ProteomicsDB; 59378; -. [Q13402-4]
ProteomicsDB; 59379; -. [Q13402-5]
ProteomicsDB; 59380; -. [Q13402-6]
ProteomicsDB; 59381; -. [Q13402-7]
DNASU; 4647; -.
Ensembl; ENST00000409619; ENSP00000386635; ENSG00000137474. [Q13402-8]
Ensembl; ENST00000409709; ENSP00000386331; ENSG00000137474. [Q13402-1]
Ensembl; ENST00000458637; ENSP00000392185; ENSG00000137474. [Q13402-2]
GeneID; 4647; -.
KEGG; hsa:4647; -.
UCSC; uc001oyb.3; human. [Q13402-1]
CTD; 4647; -.
DisGeNET; 4647; -.
EuPathDB; HostDB:ENSG00000137474.19; -.
GeneCards; MYO7A; -.
GeneReviews; MYO7A; -.
H-InvDB; HIX0035966; -.
HGNC; HGNC:7606; MYO7A.
HPA; CAB034059; -.
HPA; HPA028918; -.
MalaCards; MYO7A; -.
MIM; 276900; phenotype.
MIM; 276903; gene.
MIM; 600060; phenotype.
MIM; 601317; phenotype.
neXtProt; NX_Q13402; -.
OpenTargets; ENSG00000137474; -.
Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
Orphanet; 231169; Usher syndrome type 1.
Orphanet; 231178; Usher syndrome type 2.
PharmGKB; PA31411; -.
eggNOG; KOG4229; Eukaryota.
eggNOG; COG5022; LUCA.
GeneTree; ENSGT00900000140810; -.
HOGENOM; HOG000007836; -.
HOVERGEN; HBG052557; -.
InParanoid; Q13402; -.
KO; K10359; -.
OMA; FNIEEAH; -.
OrthoDB; EOG091G00BB; -.
PhylomeDB; Q13402; -.
TreeFam; TF335306; -.
Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
ChiTaRS; MYO7A; human.
GeneWiki; MYO7A; -.
GenomeRNAi; 4647; -.
PRO; PR:Q13402; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137474; Expressed in 149 organ(s), highest expression level in right adrenal gland.
CleanEx; HS_MYO7A; -.
ExpressionAtlas; Q13402; baseline and differential.
Genevisible; Q13402; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:Ensembl.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0031477; C:myosin VII complex; IEA:Ensembl.
GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
GO; GO:0032420; C:stereocilium; IEA:Ensembl.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:1990435; C:upper tip-link density; IEA:Ensembl.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0030898; F:actin-dependent ATPase activity; IEA:Ensembl.
GO; GO:0043531; F:ADP binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IMP:UniProtKB.
GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0030507; F:spectrin binding; IDA:MGI.
GO; GO:0030048; P:actin filament-based movement; IDA:UniProtKB.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
GO; GO:0050957; P:equilibrioception; IMP:HGNC.
GO; GO:0042462; P:eye photoreceptor cell development; IC:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
GO; GO:0007040; P:lysosome organization; IDA:UniProtKB.
GO; GO:0001845; P:phagolysosome assembly; IEA:Ensembl.
GO; GO:0051904; P:pigment granule transport; IEA:Ensembl.
GO; GO:0048563; P:post-embryonic animal organ morphogenesis; IEA:Ensembl.
GO; GO:0050953; P:sensory perception of light stimulus; IMP:HGNC.
GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
GO; GO:0007601; P:visual perception; IMP:UniProtKB.
CDD; cd14473; FERM_B-lobe; 2.
CDD; cd01381; MYSc_Myo7; 1.
Gene3D; 1.20.80.10; -; 2.
Gene3D; 1.25.40.530; -; 2.
Gene3D; 2.30.29.30; -; 3.
Gene3D; 2.30.30.360; -; 1.
Gene3D; 3.40.850.10; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
InterPro; IPR035963; FERM_2.
InterPro; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR008989; Myosin_S1_N.
InterPro; IPR036106; MYSc_Myo7.
InterPro; IPR000857; MyTH4_dom.
InterPro; IPR038185; MyTH4_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR029071; Ubiquitin-like_domsf.
Pfam; PF00373; FERM_M; 1.
Pfam; PF00612; IQ; 2.
Pfam; PF00063; Myosin_head; 1.
Pfam; PF00784; MyTH4; 2.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM00295; B41; 2.
SMART; SM00015; IQ; 4.
SMART; SM00242; MYSc; 1.
SMART; SM00139; MyTH4; 2.
SMART; SM00326; SH3; 1.
SUPFAM; SSF47031; SSF47031; 2.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF54236; SSF54236; 2.
PROSITE; PS50057; FERM_3; 2.
PROSITE; PS50096; IQ; 3.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
PROSITE; PS51016; MYTH4; 2.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; ATP-binding;
Calmodulin-binding; Complete proteome; Cytoplasm; Cytoskeleton;
Deafness; Disease mutation; Hearing; Leber congenital amaurosis;
Motor protein; Myosin; Non-syndromic deafness; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Retinitis pigmentosa; SH3 domain; Usher syndrome.
CHAIN 1 2215 Unconventional myosin-VIIa.
/FTId=PRO_0000123466.
DOMAIN 65 741 Myosin motor. {ECO:0000255|PROSITE-
ProRule:PRU00782}.
DOMAIN 745 765 IQ 1. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 768 788 IQ 2. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 791 811 IQ 3. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 814 834 IQ 4. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 837 857 IQ 5. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1017 1253 MyTH4 1. {ECO:0000255|PROSITE-
ProRule:PRU00359}.
DOMAIN 1258 1602 FERM 1. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 1603 1672 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 1747 1896 MyTH4 2. {ECO:0000255|PROSITE-
ProRule:PRU00359}.
DOMAIN 1902 2205 FERM 2. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
NP_BIND 158 165 ATP. {ECO:0000305}.
REGION 632 639 Actin-binding. {ECO:0000305}.
REGION 858 935 SAH. {ECO:0000305|PubMed:25122759}.
MOD_RES 1569 1569 Phosphoserine.
{ECO:0000250|UniProtKB:P97479}.
MOD_RES 1571 1571 Phosphothreonine.
{ECO:0000250|UniProtKB:P97479}.
VAR_SEQ 1 11 Missing (in isoform 8).
{ECO:0000303|PubMed:10737800}.
/FTId=VSP_053793.
VAR_SEQ 284 360 Missing (in isoform 5).
{ECO:0000303|PubMed:8622919}.
/FTId=VSP_003353.
VAR_SEQ 519 564 Missing (in isoform 5).
{ECO:0000303|PubMed:8622919}.
/FTId=VSP_003354.
VAR_SEQ 1095 1095 E -> EVLQ (in isoform 4).
{ECO:0000303|PubMed:8884267}.
/FTId=VSP_003355.
VAR_SEQ 1096 1125 Missing (in isoform 6).
{ECO:0000303|PubMed:8622919}.
/FTId=VSP_003358.
VAR_SEQ 1169 1200 DEIYCQISKQLTHNPSKSSYARGWILVSLCVG -> SVPES
LLVAEWCLCQPSKRLSQAWPGFGFAAS (in isoform 3
and isoform 4).
{ECO:0000303|PubMed:8884267}.
/FTId=VSP_003356.
VAR_SEQ 1201 2215 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:8884267}.
/FTId=VSP_003357.
VAR_SEQ 1433 1470 Missing (in isoform 7).
{ECO:0000303|PubMed:8622919}.
/FTId=VSP_003359.
VAR_SEQ 1524 1561 Missing (in isoform 2 and isoform 8).
{ECO:0000303|PubMed:10737800,
ECO:0000303|PubMed:8884267}.
/FTId=VSP_003360.
VAR_SEQ 2117 2118 Missing (in isoform 2).
{ECO:0000303|PubMed:8884267}.
/FTId=VSP_045848.
VARIANT 16 16 L -> S (in dbSNP:rs1052030).
{ECO:0000269|PubMed:15660226}.
/FTId=VAR_009315.
VARIANT 25 25 G -> R (in USH1B; dbSNP:rs782252317).
{ECO:0000269|PubMed:15660226,
ECO:0000269|PubMed:9002678}.
/FTId=VAR_009316.
VARIANT 26 26 A -> E (in USH1B; dbSNP:rs369125667).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024039.
VARIANT 67 67 V -> M (in USH1B).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024040.
VARIANT 90 90 R -> P (in USH1B).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024041.
VARIANT 133 133 H -> D (in USH1B; the deleterious effect
remains to be proven).
{ECO:0000269|PubMed:16679490}.
/FTId=VAR_027301.
VARIANT 134 134 I -> N (in USH1B; dbSNP:rs111033181).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024042.
VARIANT 158 158 G -> R (found in patients with retinitis
pigmentosa; unknown pathological
significance).
{ECO:0000269|PubMed:26720455}.
/FTId=VAR_077020.
VARIANT 163 163 G -> R (in USH1B; dbSNP:rs1472566324).
{ECO:0000269|PubMed:16679490}.
/FTId=VAR_027302.
VARIANT 164 164 K -> R (in USH1B).
{ECO:0000269|PubMed:16679490}.
/FTId=VAR_027303.
VARIANT 165 165 T -> M (in USH1B; dbSNP:rs111033174).
{ECO:0000269|PubMed:15660226,
ECO:0000269|PubMed:16679490,
ECO:0000269|PubMed:24831256}.
/FTId=VAR_024043.
VARIANT 193 193 T -> I (found in a patient with Leber
congenital amaurosis; unknown
pathological significance;
dbSNP:rs1188616455).
{ECO:0000269|PubMed:21901789}.
/FTId=VAR_066861.
VARIANT 198 198 A -> T (in USH1B; is predicted to alter
the normal splicing of exon 6).
{ECO:0000269|PubMed:16679490}.
/FTId=VAR_027304.
VARIANT 204 204 T -> A (in USH1B).
{ECO:0000269|PubMed:16679490}.
/FTId=VAR_027305.
VARIANT 205 205 I -> V (in dbSNP:rs781946292).
/FTId=VAR_009317.
VARIANT 212 212 R -> C (in USH1B; frequent mutation;
dbSNP:rs121965080).
{ECO:0000269|PubMed:8900236}.
/FTId=VAR_009318.
VARIANT 212 212 R -> H (in USH1B; frequent mutation;
dbSNP:rs28934610).
{ECO:0000269|PubMed:8900236}.
/FTId=VAR_009319.
VARIANT 214 214 G -> R (in USH1B; dbSNP:rs111033283).
{ECO:0000269|PubMed:9382091}.
/FTId=VAR_009320.
VARIANT 218 219 Missing (in USH1B).
/FTId=VAR_009321.
VARIANT 241 241 R -> C (in USH1B; dbSNP:rs782166819).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024044.
VARIANT 241 241 R -> S (in USH1B).
/FTId=VAR_009322.
VARIANT 244 244 R -> P (in DFNB2; dbSNP:rs121965081).
{ECO:0000269|PubMed:9171832}.
/FTId=VAR_009323.
VARIANT 269 269 Missing (in USH1B).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024045.
VARIANT 302 302 R -> H (in USH1B; uncertain pathological
significance; dbSNP:rs41298135).
{ECO:0000269|PubMed:8900236}.
/FTId=VAR_009324.
VARIANT 397 397 A -> D (in USH1B).
{ECO:0000269|PubMed:12112664,
ECO:0000269|PubMed:9382091}.
/FTId=VAR_009325.
VARIANT 450 450 E -> Q (in USH1B; dbSNP:rs1269622956).
{ECO:0000269|PubMed:8900236}.
/FTId=VAR_009326.
VARIANT 457 457 A -> V (in USH1B; dbSNP:rs111033286).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024046.
VARIANT 458 458 N -> I (in DFNA11; dbSNP:rs121965084).
{ECO:0000269|PubMed:15221449}.
/FTId=VAR_027306.
VARIANT 468 468 H -> HQ (in USH1B).
{ECO:0000269|PubMed:8900236}.
/FTId=VAR_009327.
VARIANT 503 503 P -> L (in USH1B).
{ECO:0000269|PubMed:8900236}.
/FTId=VAR_009328.
VARIANT 519 519 G -> D (in USH1B; unknown pathological
significance; dbSNP:rs111033206).
{ECO:0000269|PubMed:10930322,
ECO:0000269|PubMed:16679490}.
/FTId=VAR_024047.
VARIANT 597 597 V -> I (rare polymorphism).
/FTId=VAR_009329.
VARIANT 599 599 M -> I (in DFNB2; dbSNP:rs121965082).
{ECO:0000269|PubMed:9171833}.
/FTId=VAR_009330.
VARIANT 602 602 E -> K (in dbSNP:rs2276282).
/FTId=VAR_056187.
VARIANT 651 651 L -> P (in USH1B; atypical;
dbSNP:rs876657416).
{ECO:0000269|PubMed:9718356}.
/FTId=VAR_009331.
VARIANT 652 652 C -> R (in DFNB2).
{ECO:0000269|PubMed:28281779}.
/FTId=VAR_079504.
VARIANT 679 679 V -> I (in dbSNP:rs35641839).
/FTId=VAR_056188.
VARIANT 722 722 G -> R (in DFNA11).
{ECO:0000269|PubMed:15121790}.
/FTId=VAR_027307.
VARIANT 756 756 R -> W (in USH1B; dbSNP:rs782174733).
{ECO:0000269|PubMed:15660226}.
/FTId=VAR_024048.
VARIANT 826 826 A -> T (in USH1B; dbSNP:rs368341987).
{ECO:0000269|PubMed:9382091}.
/FTId=VAR_009332.
VARIANT 853 853 R -> C (in DFNA11; disturb calmodulin/
MYO7A binding).
{ECO:0000269|PubMed:15300860}.
/FTId=VAR_027308.
VARIANT 886 888 Missing (in DFNA11).
{ECO:0000269|PubMed:9354784}.
/FTId=VAR_009333.
VARIANT 946 946 M -> R (in USH1B; dbSNP:rs1296612982).
{ECO:0000269|PubMed:24831256}.
/FTId=VAR_071646.
VARIANT 955 955 G -> S (in USH1B; dbSNP:rs781988557).
{ECO:0000269|PubMed:9002678}.
/FTId=VAR_009334.
VARIANT 968 968 E -> D (in USH1B; dbSNP:rs111033233).
{ECO:0000269|PubMed:10930322,
ECO:0000269|PubMed:15660226}.
/FTId=VAR_024049.
VARIANT 1087 1087 L -> P (in USH1B; dbSNP:rs375050157).
{ECO:0000269|PubMed:10364543}.
/FTId=VAR_009335.
VARIANT 1170 1170 E -> K (in USH1B; dbSNP:rs111033214).
{ECO:0000269|PubMed:10447383,
ECO:0000269|PubMed:12112664,
ECO:0000269|PubMed:16679490}.
/FTId=VAR_009336.
VARIANT 1240 1240 R -> Q (in USH1B; dbSNP:rs111033178).
{ECO:0000269|PubMed:10930322,
ECO:0000269|PubMed:16679490}.
/FTId=VAR_009337.
VARIANT 1248 1248 E -> K (in USH1B).
{ECO:0000269|PubMed:23559863}.
/FTId=VAR_071647.
VARIANT 1288 1288 A -> P (in USH1B; dbSNP:rs749747871).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_009338.
VARIANT 1327 1327 E -> K (in USH1B; dbSNP:rs373169422).
{ECO:0000269|PubMed:12112664}.
/FTId=VAR_027309.
VARIANT 1343 1343 R -> S (in USH1B; dbSNP:rs763469001).
/FTId=VAR_009339.
VARIANT 1346 1346 Missing (in USH1B).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024050.
VARIANT 1347 1351 Missing (in USH1B).
{ECO:0000269|PubMed:12112664}.
/FTId=VAR_027310.
VARIANT 1566 1566 T -> M (in dbSNP:rs41298747).
{ECO:0000269|PubMed:12112664,
ECO:0000269|PubMed:16679490}.
/FTId=VAR_027311.
VARIANT 1602 1602 R -> Q (in USH1B; atypical;
dbSNP:rs139889944).
{ECO:0000269|PubMed:28887846,
ECO:0000269|PubMed:9718356}.
/FTId=VAR_009340.
VARIANT 1628 1628 A -> S (in USH1B).
/FTId=VAR_009341.
VARIANT 1666 1666 S -> C (in dbSNP:rs2276288).
{ECO:0000269|PubMed:8622919,
ECO:0000269|PubMed:8884267}.
/FTId=VAR_009343.
VARIANT 1666 1666 S -> G.
/FTId=VAR_027312.
VARIANT 1719 1719 Y -> C (in dbSNP:rs77625410).
{ECO:0000269|PubMed:10447383,
ECO:0000269|PubMed:12112664,
ECO:0000269|PubMed:16679490}.
/FTId=VAR_009344.
VARIANT 1740 1740 G -> S (in dbSNP:rs12275336).
/FTId=VAR_027313.
VARIANT 1743 1743 R -> W (in USH1B; dbSNP:rs111033287).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024051.
VARIANT 1812 1812 E -> K (in USH1B; dbSNP:rs377267777).
{ECO:0000269|PubMed:25798947}.
/FTId=VAR_074074.
VARIANT 1858 1858 L -> P (in USH1B; dbSNP:rs368657015).
{ECO:0000269|PubMed:10930322,
ECO:0000269|PubMed:16679490}.
/FTId=VAR_024052.
VARIANT 1873 1873 R -> W (in USH1B; dbSNP:rs397516321).
{ECO:0000269|PubMed:16679490}.
/FTId=VAR_027314.
VARIANT 1883 1883 R -> Q (in USH1B; dbSNP:rs111033215).
{ECO:0000269|PubMed:15660226}.
/FTId=VAR_024053.
VARIANT 1887 1887 P -> L (in USH1B; dbSNP:rs199606180).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024054.
VARIANT 1954 1954 L -> I (in dbSNP:rs948962).
{ECO:0000269|PubMed:8622919,
ECO:0000269|PubMed:8884267}.
/FTId=VAR_009345.
VARIANT 1962 1962 Missing (in USH1B).
{ECO:0000269|PubMed:16679490}.
/FTId=VAR_027315.
VARIANT 1992 1992 F -> I (in dbSNP:rs771906493).
/FTId=VAR_009346.
VARIANT 2137 2137 G -> E (in USH1B).
{ECO:0000269|PubMed:9002678}.
/FTId=VAR_009347.
VARIANT 2142 2142 D -> N (in dbSNP:rs1132036).
/FTId=VAR_027316.
VARIANT 2163 2163 G -> S (in USH1B; dbSNP:rs747656448).
/FTId=VAR_009348.
VARIANT 2187 2187 G -> D (in USH1B; dbSNP:rs397516332).
{ECO:0000269|PubMed:10930322}.
/FTId=VAR_024055.
CONFLICT 172 172 L -> P (in Ref. 4; AAA20909).
{ECO:0000305}.
CONFLICT 470 470 F -> L (in Ref. 2; AAC50927/AAC50722).
{ECO:0000305}.
CONFLICT 576 576 D -> N (in Ref. 9; AAC51150).
{ECO:0000305}.
CONFLICT 794 794 F -> S (in Ref. 2; AAC50927/AAC50722 and
6; AAC50218). {ECO:0000305}.
CONFLICT 873 873 R -> Q (in Ref. 2; AAC50927/AAC50722 and
6; AAC50218). {ECO:0000305}.
CONFLICT 1073 1075 KIY -> RNS (in Ref. 6; AAC50218).
{ECO:0000305}.
CONFLICT 1237 1237 N -> S (in Ref. 2; AAC50927).
{ECO:0000305}.
HELIX 1715 1721 {ECO:0000244|PDB:5MV9}.
TURN 1727 1731 {ECO:0000244|PDB:5MV9}.
HELIX 1758 1760 {ECO:0000244|PDB:5MV9}.
HELIX 1764 1780 {ECO:0000244|PDB:5MV9}.
HELIX 1794 1805 {ECO:0000244|PDB:5MV9}.
HELIX 1808 1821 {ECO:0000244|PDB:5MV9}.
HELIX 1827 1841 {ECO:0000244|PDB:5MV9}.
TURN 1848 1850 {ECO:0000244|PDB:5MV9}.
HELIX 1851 1859 {ECO:0000244|PDB:5MV9}.
TURN 1860 1863 {ECO:0000244|PDB:5MV9}.
HELIX 1867 1880 {ECO:0000244|PDB:5MV9}.
HELIX 1889 1896 {ECO:0000244|PDB:5MV9}.
STRAND 1902 1908 {ECO:0000244|PDB:5MV9}.
TURN 1909 1911 {ECO:0000244|PDB:5MV9}.
STRAND 1912 1918 {ECO:0000244|PDB:5MV9}.
HELIX 1924 1934 {ECO:0000244|PDB:5MV9}.
STRAND 1943 1951 {ECO:0000244|PDB:5MV9}.
STRAND 1953 1955 {ECO:0000244|PDB:5MV9}.
HELIX 1962 1975 {ECO:0000244|PDB:5MV9}.
STRAND 1989 1995 {ECO:0000244|PDB:5MV9}.
HELIX 2007 2012 {ECO:0000244|PDB:5MV9}.
HELIX 2014 2024 {ECO:0000244|PDB:5MV9}.
HELIX 2031 2046 {ECO:0000244|PDB:5MV9}.
HELIX 2053 2055 {ECO:0000244|PDB:5MV9}.
HELIX 2057 2059 {ECO:0000244|PDB:5MV9}.
HELIX 2060 2063 {ECO:0000244|PDB:5MV9}.
TURN 2066 2068 {ECO:0000244|PDB:5MV9}.
HELIX 2069 2071 {ECO:0000244|PDB:5MV9}.
HELIX 2074 2085 {ECO:0000244|PDB:5MV9}.
HELIX 2086 2088 {ECO:0000244|PDB:5MV9}.
HELIX 2093 2104 {ECO:0000244|PDB:5MV9}.
TURN 2108 2111 {ECO:0000244|PDB:5MV9}.
STRAND 2113 2121 {ECO:0000244|PDB:5MV9}.
STRAND 2123 2125 {ECO:0000244|PDB:5MV9}.
STRAND 2127 2134 {ECO:0000244|PDB:5MV9}.
STRAND 2137 2141 {ECO:0000244|PDB:5MV9}.
TURN 2143 2145 {ECO:0000244|PDB:5MV9}.
STRAND 2148 2152 {ECO:0000244|PDB:5MV9}.
HELIX 2154 2156 {ECO:0000244|PDB:5MV9}.
STRAND 2157 2162 {ECO:0000244|PDB:5MV9}.
STRAND 2164 2171 {ECO:0000244|PDB:5MV9}.
STRAND 2179 2183 {ECO:0000244|PDB:5MV9}.
HELIX 2187 2204 {ECO:0000244|PDB:5MV9}.
SEQUENCE 2215 AA; 254390 MW; 9F921DB43FD9BE1E CRC64;
MVILQQGDHV WMDLRLGQEF DVPIGAVVKL CDSGQVQVVD DEDNEHWISP QNATHIKPMH
PTSVHGVEDM IRLGDLNEAG ILRNLLIRYR DHLIYTYTGS ILVAVNPYQL LSIYSPEHIR
QYTNKKIGEM PPHIFAIADN CYFNMKRNSR DQCCIISGES GAGKTESTKL ILQFLAAISG
QHSWIEQQVL EATPILEAFG NAKTIRNDNS SRFGKYIDIH FNKRGAIEGA KIEQYLLEKS
RVCRQALDER NYHVFYCMLE GMSEDQKKKL GLGQASDYNY LAMGNCITCE GRVDSQEYAN
IRSAMKVLMF TDTENWEISK LLAAILHLGN LQYEARTFEN LDACEVLFSP SLATAASLLE
VNPPDLMSCL TSRTLITRGE TVSTPLSREQ ALDVRDAFVK GIYGRLFVWI VDKINAAIYK
PPSQDVKNSR RSIGLLDIFG FENFAVNSFE QLCINFANEH LQQFFVRHVF KLEQEEYDLE
SIDWLHIEFT DNQDALDMIA NKPMNIISLI DEESKFPKGT DTTMLHKLNS QHKLNANYIP
PKNNHETQFG INHFAGIVYY ETQGFLEKNR DTLHGDIIQL VHSSRNKFIK QIFQADVAMG
AETRKRSPTL SSQFKRSLEL LMRTLGACQP FFVRCIKPNE FKKPMLFDRH LCVRQLRYSG
MMETIRIRRA GYPIRYSFVE FVERYRVLLP GVKPAYKQGD LRGTCQRMAE AVLGTHDDWQ
IGKTKIFLKD HHDMLLEVER DKAITDRVIL LQKVIRGFKD RSNFLKLKNA ATLIQRHWRG
HNCRKNYGLM RLGFLRLQAL HRSRKLHQQY RLARQRIIQF QARCRAYLVR KAFRHRLWAV
LTVQAYARGM IARRLHQRLR AEYLWRLEAE KMRLAEEEKL RKEMSAKKAK EEAERKHQER
LAQLAREDAE RELKEKEAAR RKKELLEQME RARHEPVNHS DMVDKMFGFL GTSGGLPGQE
GQAPSGFEDL ERGRREMVEE DLDAALPLPD EDEEDLSEYK FAKFAATYFQ GTTTHSYTRR
PLKQPLLYHD DEGDQLAALA VWITILRFMG DLPEPKYHTA MSDGSEKIPV MTKIYETLGK
KTYKRELQAL QGEGEAQLPE GQKKSSVRHK LVHLTLKKKS KLTEEVTKRL HDGESTVQGN
SMLEDRPTSN LEKLHFIIGN GILRPALRDE IYCQISKQLT HNPSKSSYAR GWILVSLCVG
CFAPSEKFVK YLRNFIHGGP PGYAPYCEER LRRTFVNGTR TQPPSWLELQ ATKSKKPIML
PVTFMDGTTK TLLTDSATTA KELCNALADK ISLKDRFGFS LYIALFDKVS SLGSGSDHVM
DAISQCEQYA KEQGAQERNA PWRLFFRKEV FTPWHSPSED NVATNLIYQQ VVRGVKFGEY
RCEKEDDLAE LASQQYFVDY GSEMILERLL NLVPTYIPDR EITPLKTLEK WAQLAIAAHK
KGIYAQRRTD AQKVKEDVVS YARFKWPLLF SRFYEAYKFS GPSLPKNDVI VAVNWTGVYF
VDEQEQVLLE LSFPEIMAVS SSRECRVWLS LGCSDLGCAA PHSGWAGLTP AGPCSPCWSC
RGAKTTAPSF TLATIKGDEY TFTSSNAEDI RDLVVTFLEG LRKRSKYVVA LQDNPNPAGE
ESGFLSFAKG DLIILDHDTG EQVMNSGWAN GINERTKQRG DFPTDSVYVM PTVTMPPREI
VALVTMTPDQ RQDVVRLLQL RTAEPEVRAK PYTLEEFSYD YFRPPPKHTL SRVMVSKARG
KDRLWSHTRE PLKQALLKKL LGSEELSQEA CLAFIAVLKY MGDYPSKRTR SVNELTDQIF
EGPLKAEPLK DEAYVQILKQ LTDNHIRYSE ERGWELLWLC TGLFPPSNIL LPHVQRFLQS
RKHCPLAIDC LQRLQKALRN GSRKYPPHLV EVEAIQHKTT QIFHKVYFPD DTDEAFEVES
STKAKDFCQN IATRLLLKSS EGFSLFVKIA DKVLSVPEND FFFDFVRHLT DWIKKARPIK
DGIVPSLTYQ VFFMKKLWTT TVPGKDPMAD SIFHYYQELP KYLRGYHKCT REEVLQLGAL
IYRVKFEEDK SYFPSIPKLL RELVPQDLIR QVSPDDWKRS IVAYFNKHAG KSKEEAKLAF
LKLIFKWPTF GSAFFEVKQT TEPNFPEILL IAINKYGVSL IDPKTKDILT THPFTKISNW
SSGNTYFHIT IGNLVRGSKL LCETSLGYKM DDLLTSYISQ MLTAMSKQRG SRSGK


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