MYO7A_HUMAN
ID MYO7A_HUMAN Reviewed; 2215 AA.
AC Q13402; B9A011; F8VUN5; P78427; Q13321; Q14785; Q92821; Q92822;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 2.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=Unconventional myosin-VIIa;
GN Name=MYO7A; Synonyms=USH1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 5; 6 AND 7), DEVELOPMENTAL STAGE,
RP AND VARIANTS CYS-1666 AND ILE-1954.
RC TISSUE=Retina;
RX PubMed=8622919; DOI=10.1073/pnas.93.8.3232;
RA Weil D., Levy G., Sahly I., Levi-Acobas F., Blanchard S., El-Amraoui A.,
RA Crozet F., Philippe H., Abitbol M., Petit C.;
RT "Human myosin VIIA responsible for the Usher 1B syndrome: a predicted
RT membrane-associated motor protein expressed in developing sensory
RT epithelia.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3232-3237(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND VARIANTS CYS-1666 AND
RP ILE-1954.
RC TISSUE=Testis;
RX PubMed=8884267; DOI=10.1006/geno.1996.0489;
RA Chen Z.-Y., Hasson T., Kelley P.M., Schwender B.J., Schwartz M.F.,
RA Ramakrishnan M., Kimberling W.J., Mooseker M.S., Corey D.P.;
RT "Molecular cloning and domain structure of human myosin-VIIa, the gene
RT product defective in usher syndrome 1B.";
RL Genomics 36:440-448(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-196.
RC TISSUE=Epithelium, Leukocyte, and Liver;
RX PubMed=8022818; DOI=10.1073/pnas.91.14.6549;
RA Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.;
RT "Identification and overlapping expression of multiple unconventional
RT myosin genes in vertebrate cell types.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6549-6553(1994).
RN [5]
RP ERRATUM OF PUBMED:8022818.
RX PubMed=7972138; DOI=10.1073/pnas.91.24.11767-c;
RA Bement W.M., Hasson T., Wirth J.A., Cheney R.E., Mooseker M.S.;
RL Proc. Natl. Acad. Sci. U.S.A. 91:11767-11767(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1075.
RC TISSUE=Testis;
RX PubMed=7568224; DOI=10.1073/pnas.92.21.9815;
RA Hasson T., Heintzelman M.B., Santos-Sacchi J., Corey D.P., Mooseker M.S.;
RT "Expression in cochlea and retina of myosin VIIa, the gene product
RT defective in Usher syndrome type 1B.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9815-9819(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-117 (ISOFORM 8).
RX PubMed=10737800; DOI=10.1073/pnas.97.7.3491;
RA Dias Neto E., Correa R.G., Verjovski-Almeida S., Briones M.R.S.,
RA Nagai M.A., da Silva W. Jr., Zago M.A., Bordin S., Costa F.F.,
RA Goldman G.H., Carvalho A.F., Matsukuma A., Baia G.S., Simpson D.H.,
RA Brunstein A., de Oliveira P.S.L., Bucher P., Jongeneel C.V., O'Hare M.J.,
RA Soares F., Brentani R.R., Reis L.F.L., de Souza S.J., Simpson A.J.G.;
RT "Shotgun sequencing of the human transcriptome with ORF expressed sequence
RT tags.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3491-3496(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 96-564 (ISOFORM 1), AND VARIANTS USH1B.
RC TISSUE=Retina;
RX PubMed=7870171; DOI=10.1038/374060a0;
RA Weil D., Blanchard S., Kaplan J., Guilford P., Gibson F., Walsh J.,
RA Mburu P., Varela A., Levilliers J., Weston M.D., Kelley P.M.,
RA Kimberling W.J., Wagenaar M., Levi-Acobas F., Larget-Piet D., Munnich A.,
RA Steel K.P., Brown S.D.M., Petit C.;
RT "Defective myosin VIIA gene responsible for Usher syndrome type 1B.";
RL Nature 374:60-61(1995).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-578.
RX PubMed=9070921; DOI=10.1006/geno.1996.4545;
RA Kelley P.M., Weston M.D., Chen Z.-Y., Orten D.J., Hasson T., Overbeck L.D.,
RA Pinnt J., Talmadge C.B., Ing P., Mooseker M.S., Corey D.P., Sumegi J.,
RA Kimberling W.J.;
RT "The genomic structure of the gene defective in Usher syndrome type Ib
RT (MYO7A).";
RL Genomics 40:73-79(1997).
RN [10]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=8842737; DOI=10.1093/hmg/5.8.1171;
RA El-Amraoui A., Sahly I., Picaud S., Sahel J., Abitbol M., Petit C.;
RT "Human Usher 1B/mouse shaker-1: the retinal phenotype discrepancy explained
RT by the presence/absence of myosin VIIA in the photoreceptor cells.";
RL Hum. Mol. Genet. 5:1171-1178(1996).
RN [11]
RP INTERACTION WITH MYRIP.
RX PubMed=11964381; DOI=10.1093/embo-reports/kvf090;
RA El-Amraoui A., Schonn J.-S., Kuessel-Andermann P., Blanchard S., Desnos C.,
RA Henry J.-P., Wolfrum U., Darchen F., Petit C.;
RT "MyRIP, a novel Rab effector, enables myosin VIIa recruitment to retinal
RT melanosomes.";
RL EMBO Rep. 3:463-470(2002).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19643958; DOI=10.1167/iovs.09-4032;
RA Gibbs D., Diemer T., Khanobdee K., Hu J., Bok D., Williams D.S.;
RT "Function of MYO7A in the human RPE and the validity of shaker1 mice as a
RT model for Usher syndrome 1B.";
RL Invest. Ophthalmol. Vis. Sci. 51:1130-1135(2010).
RN [13]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=21687988; DOI=10.1007/s00018-011-0749-8;
RA Heissler S.M., Manstein D.J.;
RT "Functional characterization of the human myosin-7a motor domain.";
RL Cell. Mol. Life Sci. 69:299-311(2012).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH RPE65.
RX PubMed=21493626; DOI=10.1093/hmg/ddr155;
RA Lopes V.S., Gibbs D., Libby R.T., Aleman T.S., Welch D.L., Lillo C.,
RA Jacobson S.G., Radu R.A., Steel K.P., Williams D.S.;
RT "The Usher 1B protein, MYO7A, is required for normal localization and
RT function of the visual retinoid cycle enzyme, RPE65.";
RL Hum. Mol. Genet. 20:2560-2570(2011).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH USH1C AND
RP USH1G, AND TISSUE SPECIFICITY.
RX PubMed=21709241; DOI=10.1073/pnas.1104161108;
RA Grati M., Kachar B.;
RT "Myosin VIIa and sans localization at stereocilia upper tip-link density
RT implicates these Usher syndrome proteins in mechanotransduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11476-11481(2011).
RN [16]
RP INTERACTION WITH CIB2.
RX PubMed=23023331; DOI=10.1038/ng.2426;
RA Riazuddin S., Belyantseva I.A., Giese A.P., Lee K., Indzhykulian A.A.,
RA Nandamuri S.P., Yousaf R., Sinha G.P., Lee S., Terrell D., Hegde R.S.,
RA Ali R.A., Anwar S., Andrade-Elizondo P.B., Sirmaci A., Parise L.V.,
RA Basit S., Wali A., Ayub M., Ansar M., Ahmad W., Khan S.N., Akram J.,
RA Tekin M., Riazuddin S., Cook T., Buschbeck E.K., Frolenkov G.I., Leal S.M.,
RA Friedman T.B., Ahmed Z.M.;
RT "Alterations of the CIB2 calcium- and integrin-binding protein cause Usher
RT syndrome type 1J and nonsyndromic deafness DFNB48.";
RL Nat. Genet. 44:1265-1271(2012).
RN [17]
RP SAH DOMAIN.
RX PubMed=25122759; DOI=10.1074/jbc.m114.585679;
RA Wolny M., Batchelor M., Knight P.J., Paci E., Dougan L., Peckham M.;
RT "Stable single alpha-helices are constant force springs in proteins.";
RL J. Biol. Chem. 289:27825-27835(2014).
RN [18]
RP INTERACTION WITH MYH9, AND SUBCELLULAR LOCATION.
RX PubMed=27331610; DOI=10.7554/elife.15258;
RA Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
RA Groves A.K., Bellen H.J.;
RT "The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in
RT the auditory organs of Drosophila and mammals.";
RL Elife 5:E15258-E15258(2016).
RN [19]
RP VARIANTS USH1B CYS-212; HIS-212; GLN-450; GLN-468 INS AND LEU-503, AND
RP VARIANT HIS-302.
RX PubMed=8900236;
RA Weston M.D., Kelley P.M., Overbeck L.D., Wagenaar M., Orten D.J.,
RA Hasson T., Chen Z.-Y., Corey D.P., Mooseker M.S., Sumegi J., Cremers C.,
RA Moeller C., Jacobson S.G., Gorin M.B., Kimberling W.J.;
RT "Myosin VIIA mutation screening in 189 Usher syndrome type 1 patients.";
RL Am. J. Hum. Genet. 59:1074-1083(1996).
RN [20]
RP VARIANTS USH1B ARG-214; ASP-397 AND THR-826, AND POLYMORPHISM.
RX PubMed=9382091; DOI=10.1086/514899;
RA Adato A., Weil D., Kalinski H., Pel-Or Y., Ayadi H., Petit C.,
RA Korostishevsky M., Bonne-Tamir B.;
RT "Mutation profile of all 49 exons of the human myosin VIIA gene, and
RT haplotype analysis, in Usher 1B families from diverse origins.";
RL Am. J. Hum. Genet. 61:813-821(1997).
RN [21]
RP VARIANTS USH1B ARG-25; SER-955 AND GLU-2137, AND POLYMORPHISM.
RX PubMed=9002678; DOI=10.1093/hmg/6.1.111;
RA Levy G., Levi-Acobas F., Blanchard S., Gerber S., Larget-Piet D.,
RA Chenal V., Liu X.-Z., Newton V., Steel K.P., Brown S.D.M., Munnich A.,
RA Kaplan J., Petit C., Weil D.;
RT "Myosin VIIA gene: heterogeneity of the mutations responsible for Usher
RT syndrome type IB.";
RL Hum. Mol. Genet. 6:111-116(1997).
RN [22]
RP VARIANT DFNB2 PRO-244.
RX PubMed=9171832; DOI=10.1038/ng0697-188;
RA Liu X.-Z., Walsh J., Mburu P., Kendrick-Jones J., Cope M.J., Steel K.P.,
RA Brown S.D.M.;
RT "Mutations in the myosin VIIA gene cause non-syndromic recessive
RT deafness.";
RL Nat. Genet. 16:188-190(1997).
RN [23]
RP VARIANT DFNB2 ILE-599.
RX PubMed=9171833; DOI=10.1038/ng0697-191;
RA Weil D., Kuessel P., Blanchard S., Levy G., Levi-Acobas F., Drira M.,
RA Ayadi H., Petit C.;
RT "The autosomal recessive isolated deafness, DFNB2, and the Usher 1B
RT syndrome are allelic defects of the myosin-VIIA gene.";
RL Nat. Genet. 16:191-193(1997).
RN [24]
RP VARIANT DFNA11 886-ALA--LYS-888 DEL.
RX PubMed=9354784; DOI=10.1038/ng1197-268;
RA Liu X.-Z., Walsh J., Tamagawa Y., Kitamura K., Nishizawa M., Steel K.P.,
RA Brown S.D.M.;
RT "Autosomal dominant non-syndromic deafness caused by a mutation in the
RT myosin VIIA gene.";
RL Nat. Genet. 17:268-269(1997).
RN [25]
RP VARIANTS USH1B PRO-651 AND GLN-1602.
RX PubMed=9718356; DOI=10.1086/302026;
RA Liu X.-Z., Hope C., Walsh J., Newton V., Ke X.M., Liang C.Y., Xu L.R.,
RA Zhou J.M., Trump D., Steel K.P., Bundey S., Brown S.D.M.;
RT "Mutations in the myosin VIIA gene cause a wide phenotypic spectrum,
RT including atypical Usher syndrome.";
RL Am. J. Hum. Genet. 63:909-912(1998).
RN [26]
RP VARIANT USH1B PRO-1087.
RX PubMed=10364543; DOI=10.1086/302438;
RA Adato A., Kalinski H., Weil D., Chaib H., Korostishevsky M.,
RA Bonne-Tamir B.;
RT "Possible interaction between USH1B and USH3 gene products as implied by
RT apparent digenic deafness inheritance.";
RL Am. J. Hum. Genet. 65:261-265(1999).
RN [27]
RP VARIANTS USH1B, AND POLYMORPHISM.
RX PubMed=10094549;
RX DOI=10.1002/(sici)1098-1004(1999)13:2<133::aid-humu5>3.0.co;2-u;
RA Janecke A.R., Meins M., Sadeghi M., Grundmann K., Apfelstedt-Sylla E.,
RA Zrenner E., Rosenberg T., Gal A.;
RT "Twelve novel myosin VIIA mutations in 34 patients with Usher syndrome type
RT I: confirmation of genetic heterogeneity.";
RL Hum. Mutat. 13:133-140(1999).
RN [28]
RP VARIANT USH1B LYS-1170, AND VARIANT CYS-1719.
RX PubMed=10447383;
RX DOI=10.1002/(sici)1098-1004(1999)14:2<181::aid-humu11>3.0.co;2-3;
RA Cuevas J.M., Espinos C., Millan J.M., Sanchez F., Trujillo M.J., Ayuso C.,
RA Beneyto M., Najera C.;
RT "Identification of three novel mutations in the MYO7A gene.";
RL Hum. Mutat. 14:181-181(1999).
RN [29]
RP VARIANTS USH1B GLU-26; MET-67; PRO-90; ASN-134; CYS-241; LYS-269 DEL;
RP VAL-457; ASP-519; ASP-968; GLN-1240; PRO-1288; PHE-1346 DEL; TRP-1743;
RP PRO-1858; LEU-1887 AND ASP-2187.
RX PubMed=10930322; DOI=10.1006/exer.2000.0863;
RA Bharadwaj A.K., Kasztejna J.P., Huq S., Berson E.L., Dryja T.P.;
RT "Evaluation of the myosin VIIA gene and visual function in patients with
RT Usher syndrome type I.";
RL Exp. Eye Res. 71:173-181(2000).
RN [30]
RP VARIANTS USH1B ASP-397; LYS-1170; LYS-1327 AND 1347-ARG--PHE-1351 DEL, AND
RP VARIANTS MET-1566 AND CYS-1719.
RX PubMed=12112664; DOI=10.1002/humu.9042;
RA Najera C., Beneyto M., Blanca J., Aller E., Fontcuberta A., Millan J.M.,
RA Ayuso C.;
RT "Mutations in myosin VIIA (MYO7A) and usherin (USH2A) in Spanish patients
RT with Usher syndrome types I and II, respectively.";
RL Hum. Mutat. 20:76-77(2002).
RN [31]
RP VARIANT DFNA11 ILE-458.
RX PubMed=15221449; DOI=10.1007/s00439-004-1137-3;
RA Luijendijk M.W.J., Van Wijk E., Bischoff A.M.L.C., Krieger E.,
RA Huygen P.L.M., Pennings R.J.E., Brunner H.G., Cremers C.W.R.J.,
RA Cremers F.P.M., Kremer H.;
RT "Identification and molecular modelling of a mutation in the motor head
RT domain of myosin VIIA in a family with autosomal dominant hearing
RT impairment (DFNA11).";
RL Hum. Genet. 115:149-156(2004).
RN [32]
RP VARIANT DFNA11 CYS-853, INTERACTION WITH CALM, AND CHARACTERIZATION OF
RP VARIANT DFNA11 CYS-853.
RX PubMed=15300860; DOI=10.1002/humu.9272;
RA Bolz H., Bolz S.-S., Schade G., Kothe C., Mohrmann G., Hess M., Gal A.;
RT "Impaired calmodulin binding of myosin-7A causes autosomal dominant hearing
RT loss (DFNA11).";
RL Hum. Mutat. 24:274-275(2004).
RN [33]
RP VARIANT DFNA11 ARG-722.
RX PubMed=15121790; DOI=10.1136/jmg.2003.013557;
RA Street V.A., Kallman J.C., Kiemele K.L.;
RT "Modifier controls severity of a novel dominant low-frequency MyosinVIIA
RT (MYO7A) auditory mutation.";
RL J. Med. Genet. 41:E62-E62(2004).
RN [34]
RP VARIANTS USH1B ARG-25; MET-165; TRP-756; ASP-968 AND GLN-1883, AND VARIANT
RP SER-16.
RX PubMed=15660226; DOI=10.1007/s00439-004-1227-2;
RA Ouyang X.M., Yan D., Du L.L., Hejtmancik J.F., Jacobson S.G., Nance W.E.,
RA Li A.R., Angeli S., Kaiser M., Newton V., Brown S.D.M., Balkany T.,
RA Liu X.Z.;
RT "Characterization of Usher syndrome type I gene mutations in an Usher
RT syndrome patient population.";
RL Hum. Genet. 116:292-299(2005).
RN [35]
RP VARIANTS USH1B ASP-133; ARG-163; ARG-164; MET-165; THR-198; ALA-204;
RP ASP-519; LYS-1170; GLN-1240; PRO-1858; TRP-1873 AND PHE-1962 DEL, AND
RP VARIANTS MET-1566 AND CYS-1719.
RX PubMed=16679490; DOI=10.1136/jmg.2006.041954;
RA Roux A.-F., Faugere V., Le Guedard S., Pallares-Ruiz N., Vielle A.,
RA Chambert S., Marlin S., Hamel C., Gilbert B., Malcolm S., Claustres M.;
RT "Survey of the frequency of USH1 gene mutations in a cohort of Usher
RT patients shows the importance of cadherin 23 and protocadherin 15 genes and
RT establishes a detection rate of above 90%.";
RL J. Med. Genet. 43:763-768(2006).
RN [36]
RP VARIANT ILE-193.
RX PubMed=21901789; DOI=10.1002/humu.21587;
RA Wang X., Wang H., Cao M., Li Z., Chen X., Patenia C., Gore A., Abboud E.B.,
RA Al-Rajhi A.A., Lewis A.R., Lupski J.R., Mardon G., Zhang K., Muzny D.,
RA Gibbs R.A., Chen R.;
RT "Whole-exome sequencing identifies ALMS1, IQCB1, CNGA3, and MYO7A mutations
RT in patients with Leber congenital amaurosis.";
RL Hum. Mutat. 32:1450-1459(2011).
RN [37]
RP INVOLVEMENT IN USH1B, AND VARIANT USH1B LYS-1248.
RX PubMed=23559863;
RA Liu F., Li P., Liu Y., Li W., Wong F., Du R., Wang L., Li C., Jiang F.,
RA Tang Z., Liu M.;
RT "Novel compound heterozygous mutations in MYO7A in a Chinese family with
RT Usher syndrome type 1.";
RL Mol. Vis. 19:695-701(2013).
RN [38]
RP VARIANTS USH1B MET-165 AND ARG-946.
RX PubMed=24831256; DOI=10.1371/journal.pone.0097808;
RA Rong W., Chen X., Zhao K., Liu Y., Liu X., Ha S., Liu W., Kang X.,
RA Sheng X., Zhao C.;
RT "Novel and recurrent MYO7A mutations in Usher syndrome type 1 and type 2.";
RL PLoS ONE 9:E97808-E97808(2014).
RN [39]
RP VARIANT ARG-158.
RX PubMed=26720455; DOI=10.1167/iovs.15-17473;
RA Kastner S., Thiemann I.J., Dekomien G., Petrasch-Parwez E., Schreiber S.,
RA Akkad D.A., Gerding W.M., Hoffjan S., Guenes S., Guenes S., Bagci H.,
RA Epplen J.T.;
RT "Exome Sequencing Reveals AGBL5 as Novel Candidate Gene and Additional
RT Variants for Retinitis Pigmentosa in Five Turkish Families.";
RL Invest. Ophthalmol. Vis. Sci. 56:8045-8053(2015).
RN [40]
RP VARIANT USH1B LYS-1812.
RX PubMed=25798947; DOI=10.1371/journal.pone.0120584;
RA Riahi Z., Bonnet C., Zainine R., Lahbib S., Bouyacoub Y., Bechraoui R.,
RA Marrakchi J., Hardelin J.P., Louha M., Largueche L., Ben Yahia S.,
RA Kheirallah M., Elmatri L., Besbes G., Abdelhak S., Petit C.;
RT "Whole exome sequencing identifies mutations in Usher syndrome genes in
RT profoundly deaf Tunisian patients.";
RL PLoS ONE 10:E0120584-E0120584(2015).
RN [41]
RP VARIANT DFNB2 ARG-652.
RX PubMed=28281779; DOI=10.1089/gtmb.2016.0328;
RA Wang R., Han S., Khan A., Zhang X.;
RT "Molecular Analysis of Twelve Pakistani Families with Nonsyndromic or
RT Syndromic Hearing Loss.";
RL Genet. Test. Mol. Biomarkers 21:316-321(2017).
RN [42]
RP VARIANT GLN-1602.
RX PubMed=28887846; DOI=10.1002/humu.23335;
RA Zhou X.L., He L.X., Yu L.J., Wang Y., Wang X.J., Wang E.D., Yang T.;
RT "Mutations in KARS cause early-onset hearing loss and leukoencephalopathy:
RT Potential pathogenic mechanism.";
RL Hum. Mutat. 38:1740-1750(2017).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails bind to membranous compartments, which are then moved
CC relative to actin filaments. In the retina, plays an important role in
CC the renewal of the outer photoreceptor disks. Plays an important role
CC in the distribution and migration of retinal pigment epithelial (RPE)
CC melanosomes and phagosomes, and in the regulation of opsin transport in
CC retinal photoreceptors. In the inner ear, plays an important role in
CC differentiation, morphogenesis and organization of cochlear hair cell
CC bundles. Involved in hair-cell vesicle trafficking of aminoglycosides,
CC which are known to induce ototoxicity (By similarity). Motor protein
CC that is a part of the functional network formed by USH1C, USH1G, CDH23
CC and MYO7A that mediates mechanotransduction in cochlear hair cells.
CC Required for normal hearing. {ECO:0000250, ECO:0000269|PubMed:19643958,
CC ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:21687988,
CC ECO:0000269|PubMed:21709241}.
CC -!- ACTIVITY REGULATION: ATP hydrolysis is inhibited by Mg(2+), already at
CC a concentration of 0.4 mM. {ECO:0000269|PubMed:21687988}.
CC -!- SUBUNIT: Might homodimerize in a two headed molecule through the
CC formation of a coiled-coil rod (By similarity). Identified in a complex
CC with USH1C and USH1G (PubMed:21709241). Interacts with MYRIP
CC (PubMed:11964381). Interacts with RPE65 (PubMed:21493626). Interacts
CC with CIB2 (PubMed:23023331). May interact with CALM (PubMed:15300860).
CC Interacts with WHRN (By similarity). Interacts with PLEKHB1 (via PH
CC domain) (By similarity). Interacts with PCDH15 (By similarity).
CC Interacts with TWF2 (By similarity). Interacts with USH1G (By
CC similarity). Interacts with MYH9 (By similarity). Interacts (via MyTH4-
CC FERM domains) with cytoplasmic regions of ADGRV1 and USH2A. Interacts
CC with PDZD7 (via MyTH4-FERM domains) (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P97479, ECO:0000269|PubMed:11964381,
CC ECO:0000269|PubMed:15300860, ECO:0000269|PubMed:21493626,
CC ECO:0000269|PubMed:21709241, ECO:0000269|PubMed:23023331}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P97479}.
CC Cytoplasm, cell cortex {ECO:0000250|UniProtKB:P97479}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:P97479}. Synapse
CC {ECO:0000269|PubMed:8842737}. Note=In the photoreceptor cells, mainly
CC localized in the inner and base of outer segments as well as in the
CC synaptic ending region (PubMed:8842737). In retinal pigment epithelial
CC cells colocalizes with a subset of melanosomes, displays predominant
CC localization to stress fiber-like structures and some localization to
CC cytoplasmic puncta (PubMed:19643958, PubMed:27331610). Detected at the
CC tip of cochlear hair cell stereocilia (PubMed:21709241). The complex
CC formed by MYO7A, USH1C and USH1G colocalizes with F-actin
CC (PubMed:21709241). {ECO:0000269|PubMed:19643958,
CC ECO:0000269|PubMed:21709241, ECO:0000269|PubMed:27331610,
CC ECO:0000269|PubMed:8842737}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q13402-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13402-2; Sequence=VSP_003360, VSP_045848;
CC Name=3;
CC IsoId=Q13402-3; Sequence=VSP_003356, VSP_003357;
CC Name=4;
CC IsoId=Q13402-4; Sequence=VSP_003355, VSP_003356, VSP_003357;
CC Name=5;
CC IsoId=Q13402-5; Sequence=VSP_003353, VSP_003354;
CC Name=6;
CC IsoId=Q13402-6; Sequence=VSP_003358;
CC Name=7;
CC IsoId=Q13402-7; Sequence=VSP_003359;
CC Name=8;
CC IsoId=Q13402-8; Sequence=VSP_053793, VSP_003360;
CC -!- TISSUE SPECIFICITY: Expressed in the pigment epithelium and the
CC photoreceptor cells of the retina. Also found in kidney, liver, testis,
CC cochlea, lymphocytes. Not expressed in brain.
CC {ECO:0000269|PubMed:19643958, ECO:0000269|PubMed:21493626,
CC ECO:0000269|PubMed:21709241}.
CC -!- DEVELOPMENTAL STAGE: Detected in optic cup in 5.5 weeks-old embryos.
CC Expressed in retinal pigment epithelium, cochlear and vestibular
CC neuroepithelia, and olfactory epithelium at 8 weeks. At 19 weeks,
CC present in both pigment epithelium and photoreceptor cells. At 24-28
CC weeks, expression in pigment epithelium and photoreceptor cells
CC increases. Present in pigment epithelium and photoreceptor cells in
CC adult. {ECO:0000269|PubMed:8622919, ECO:0000269|PubMed:8842737}.
CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high
CC content of charged residues which are predicted to stabilize the alpha-
CC helical structure by ionic bonds. {ECO:0000305|PubMed:25122759}.
CC -!- DISEASE: Usher syndrome 1B (USH1B) [MIM:276900]: USH is a genetically
CC heterogeneous condition characterized by the association of retinitis
CC pigmentosa with sensorineural deafness. Age at onset and differences in
CC auditory and vestibular function distinguish Usher syndrome type 1
CC (USH1), Usher syndrome type 2 (USH2) and Usher syndrome type 3 (USH3).
CC USH1 is characterized by profound congenital sensorineural deafness,
CC absent vestibular function and prepubertal onset of progressive
CC retinitis pigmentosa leading to blindness.
CC {ECO:0000269|PubMed:10094549, ECO:0000269|PubMed:10364543,
CC ECO:0000269|PubMed:10447383, ECO:0000269|PubMed:10930322,
CC ECO:0000269|PubMed:12112664, ECO:0000269|PubMed:15660226,
CC ECO:0000269|PubMed:16679490, ECO:0000269|PubMed:23559863,
CC ECO:0000269|PubMed:24831256, ECO:0000269|PubMed:25798947,
CC ECO:0000269|PubMed:7870171, ECO:0000269|PubMed:8900236,
CC ECO:0000269|PubMed:9002678, ECO:0000269|PubMed:9382091,
CC ECO:0000269|PubMed:9718356}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, autosomal recessive, 2 (DFNB2) [MIM:600060]: A form
CC of non-syndromic sensorineural hearing loss. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. {ECO:0000269|PubMed:28281779, ECO:0000269|PubMed:9171832,
CC ECO:0000269|PubMed:9171833}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Deafness, autosomal dominant, 11 (DFNA11) [MIM:601317]: A form
CC of non-syndromic sensorineural hearing loss. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. DFNA11 is characterized by onset after complete speech
CC acquisition and subsequent gradual progression.
CC {ECO:0000269|PubMed:15121790, ECO:0000269|PubMed:15221449,
CC ECO:0000269|PubMed:15300860, ECO:0000269|PubMed:9354784}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-7 (MYH7). {ECO:0000305}.
CC -!- CAUTION: Originally predicted to contain a coiled coil domain but
CC proposed to contain a stable SAH domain instead. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Hereditary hearing loss homepage; Note=Gene page;
CC URL="https://hereditaryhearingloss.org/dominant-genes";
CC -!- WEB RESOURCE: Name=Mutations of the MYO7A gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/myomut.htm";
CC ---------------------------------------------------------------------------
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DR EMBL; U39226; AAB03679.1; -; mRNA.
DR EMBL; U55208; AAC50927.1; -; mRNA.
DR EMBL; U55209; AAC50722.1; -; mRNA.
DR EMBL; AP000752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L29146; AAA20909.1; -; mRNA.
DR EMBL; U34227; AAC50218.1; -; mRNA.
DR EMBL; BF869194; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AH006665; AAC51150.1; -; Genomic_DNA.
DR CCDS; CCDS53683.1; -. [Q13402-1]
DR CCDS; CCDS53684.1; -. [Q13402-2]
DR PIR; A59255; A59255.
DR PIR; A59257; A59257.
DR PIR; I61697; I61697.
DR RefSeq; NP_000251.3; NM_000260.3. [Q13402-1]
DR RefSeq; NP_001120652.1; NM_001127180.1. [Q13402-2]
DR PDB; 5MV9; X-ray; 2.60 A; A=1702-2215.
DR PDBsum; 5MV9; -.
DR AlphaFoldDB; Q13402; -.
DR SMR; Q13402; -.
DR BioGRID; 110731; 19.
DR CORUM; Q13402; -.
DR ELM; Q13402; -.
DR IntAct; Q13402; 6.
DR MINT; Q13402; -.
DR STRING; 9606.ENSP00000386331; -.
DR GlyGen; Q13402; 1 site.
DR iPTMnet; Q13402; -.
DR PhosphoSitePlus; Q13402; -.
DR BioMuta; MYO7A; -.
DR DMDM; 460018219; -.
DR EPD; Q13402; -.
DR jPOST; Q13402; -.
DR MassIVE; Q13402; -.
DR MaxQB; Q13402; -.
DR PaxDb; Q13402; -.
DR PeptideAtlas; Q13402; -.
DR PRIDE; Q13402; -.
DR ProteomicsDB; 28745; -.
DR ProteomicsDB; 59375; -. [Q13402-1]
DR ProteomicsDB; 59376; -. [Q13402-2]
DR ProteomicsDB; 59377; -. [Q13402-3]
DR ProteomicsDB; 59378; -. [Q13402-4]
DR ProteomicsDB; 59379; -. [Q13402-5]
DR ProteomicsDB; 59380; -. [Q13402-6]
DR ProteomicsDB; 59381; -. [Q13402-7]
DR ProteomicsDB; 7477; -.
DR Antibodypedia; 31226; 198 antibodies from 31 providers.
DR DNASU; 4647; -.
DR Ensembl; ENST00000409619.6; ENSP00000386635.2; ENSG00000137474.23. [Q13402-8]
DR Ensembl; ENST00000409709.9; ENSP00000386331.3; ENSG00000137474.23. [Q13402-1]
DR Ensembl; ENST00000458637.6; ENSP00000392185.2; ENSG00000137474.23. [Q13402-2]
DR GeneID; 4647; -.
DR KEGG; hsa:4647; -.
DR MANE-Select; ENST00000409709.9; ENSP00000386331.3; NM_000260.4; NP_000251.3.
DR UCSC; uc001oyb.3; human. [Q13402-1]
DR CTD; 4647; -.
DR DisGeNET; 4647; -.
DR GeneCards; MYO7A; -.
DR GeneReviews; MYO7A; -.
DR HGNC; HGNC:7606; MYO7A.
DR HPA; ENSG00000137474; Tissue enhanced (adrenal gland, choroid plexus).
DR MalaCards; MYO7A; -.
DR MIM; 276900; phenotype.
DR MIM; 276903; gene.
DR MIM; 600060; phenotype.
DR MIM; 601317; phenotype.
DR neXtProt; NX_Q13402; -.
DR OpenTargets; ENSG00000137474; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR Orphanet; 90636; Autosomal recessive non-syndromic sensorineural deafness type DFNB.
DR Orphanet; 231169; Usher syndrome type 1.
DR Orphanet; 231178; Usher syndrome type 2.
DR PharmGKB; PA31411; -.
DR VEuPathDB; HostDB:ENSG00000137474; -.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155350; -.
DR HOGENOM; CLU_000192_14_1_1; -.
DR InParanoid; Q13402; -.
DR OMA; LHRGNKH; -.
DR OrthoDB; 527681at2759; -.
DR PhylomeDB; Q13402; -.
DR TreeFam; TF335306; -.
DR PathwayCommons; Q13402; -.
DR Reactome; R-HSA-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-9662361; Sensory processing of sound by outer hair cells of the cochlea.
DR SignaLink; Q13402; -.
DR SIGNOR; Q13402; -.
DR BioGRID-ORCS; 4647; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; MYO7A; human.
DR GeneWiki; MYO7A; -.
DR GenomeRNAi; 4647; -.
DR Pharos; Q13402; Tbio.
DR PRO; PR:Q13402; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13402; protein.
DR Bgee; ENSG00000137474; Expressed in right adrenal gland cortex and 125 other tissues.
DR ExpressionAtlas; Q13402; baseline and differential.
DR Genevisible; Q13402; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
DR GO; GO:0120044; C:stereocilium base; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IMP:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; IDA:UniProtKB.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
DR GO; GO:0050957; P:equilibrioception; IMP:HGNC-UCL.
DR GO; GO:0042462; P:eye photoreceptor cell development; IC:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
DR GO; GO:0007040; P:lysosome organization; IDA:UniProtKB.
DR GO; GO:0042490; P:mechanoreceptor differentiation; ISS:UniProtKB.
DR GO; GO:0001845; P:phagolysosome assembly; IEA:Ensembl.
DR GO; GO:0051904; P:pigment granule transport; IEA:Ensembl.
DR GO; GO:0048563; P:post-embryonic animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0007423; P:sensory organ development; IBA:GO_Central.
DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:HGNC-UCL.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 2.
DR CDD; cd13198; FERM_C1_MyoVII; 1.
DR CDD; cd13199; FERM_C2_MyoVII; 1.
DR CDD; cd01381; MYSc_Myo7; 1.
DR Gene3D; 1.20.80.10; -; 2.
DR Gene3D; 1.25.40.530; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041793; MyoVII_FERM_C1.
DR InterPro; IPR041794; MyoVII_FERM_C2.
DR InterPro; IPR036106; MYSc_Myo7.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 2.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47031; SSF47031; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50057; FERM_3; 2.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Cytoplasm; Cytoskeleton; Deafness; Disease variant;
KW Hearing; Leber congenital amaurosis; Motor protein; Myosin;
KW Non-syndromic deafness; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Retinitis pigmentosa; SH3 domain; Synapse;
KW Usher syndrome.
FT CHAIN 1..2215
FT /note="Unconventional myosin-VIIa"
FT /id="PRO_0000123466"
FT DOMAIN 65..741
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 745..765
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 768..788
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 791..811
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 814..834
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 837..857
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1017..1253
FT /note="MyTH4 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1258..1602
FT /note="FERM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 1603..1672
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1747..1896
FT /note="MyTH4 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1902..2205
FT /note="FERM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 632..639
FT /note="Actin-binding"
FT /evidence="ECO:0000305"
FT REGION 858..935
FT /note="SAH"
FT /evidence="ECO:0000305|PubMed:25122759"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 1569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97479"
FT MOD_RES 1571
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97479"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:10737800"
FT /id="VSP_053793"
FT VAR_SEQ 284..360
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:8622919"
FT /id="VSP_003353"
FT VAR_SEQ 519..564
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:8622919"
FT /id="VSP_003354"
FT VAR_SEQ 1095
FT /note="E -> EVLQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8884267"
FT /id="VSP_003355"
FT VAR_SEQ 1096..1125
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:8622919"
FT /id="VSP_003358"
FT VAR_SEQ 1169..1200
FT /note="DEIYCQISKQLTHNPSKSSYARGWILVSLCVG -> SVPESLLVAEWCLCQP
FT SKRLSQAWPGFGFAAS (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8884267"
FT /id="VSP_003356"
FT VAR_SEQ 1201..2215
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8884267"
FT /id="VSP_003357"
FT VAR_SEQ 1433..1470
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:8622919"
FT /id="VSP_003359"
FT VAR_SEQ 1524..1561
FT /note="Missing (in isoform 2 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:10737800,
FT ECO:0000303|PubMed:8884267"
FT /id="VSP_003360"
FT VAR_SEQ 2117..2118
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8884267"
FT /id="VSP_045848"
FT VARIANT 16
FT /note="L -> S (in dbSNP:rs1052030)"
FT /evidence="ECO:0000269|PubMed:15660226"
FT /id="VAR_009315"
FT VARIANT 25
FT /note="G -> R (in USH1B; dbSNP:rs782252317)"
FT /evidence="ECO:0000269|PubMed:15660226,
FT ECO:0000269|PubMed:9002678"
FT /id="VAR_009316"
FT VARIANT 26
FT /note="A -> E (in USH1B; dbSNP:rs369125667)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024039"
FT VARIANT 67
FT /note="V -> M (in USH1B; dbSNP:rs1555054747)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024040"
FT VARIANT 90
FT /note="R -> P (in USH1B)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024041"
FT VARIANT 133
FT /note="H -> D (in USH1B; unknown pathological significance;
FT dbSNP:rs111033403)"
FT /evidence="ECO:0000269|PubMed:16679490"
FT /id="VAR_027301"
FT VARIANT 134
FT /note="I -> N (in USH1B; dbSNP:rs111033181)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024042"
FT VARIANT 158
FT /note="G -> R (found in patients with retinitis pigmentosa;
FT unknown pathological significance; dbSNP:rs1555062409)"
FT /evidence="ECO:0000269|PubMed:26720455"
FT /id="VAR_077020"
FT VARIANT 163
FT /note="G -> R (in USH1B; dbSNP:rs1472566324)"
FT /evidence="ECO:0000269|PubMed:16679490"
FT /id="VAR_027302"
FT VARIANT 164
FT /note="K -> R (in USH1B)"
FT /evidence="ECO:0000269|PubMed:16679490"
FT /id="VAR_027303"
FT VARIANT 165
FT /note="T -> M (in USH1B; dbSNP:rs111033174)"
FT /evidence="ECO:0000269|PubMed:15660226,
FT ECO:0000269|PubMed:16679490, ECO:0000269|PubMed:24831256"
FT /id="VAR_024043"
FT VARIANT 193
FT /note="T -> I (found in a patient with Leber congenital
FT amaurosis; unknown pathological significance;
FT dbSNP:rs1188616455)"
FT /evidence="ECO:0000269|PubMed:21901789"
FT /id="VAR_066861"
FT VARIANT 198
FT /note="A -> T (in USH1B; is predicted to alter the normal
FT splicing of exon 6)"
FT /evidence="ECO:0000269|PubMed:16679490"
FT /id="VAR_027304"
FT VARIANT 204
FT /note="T -> A (in USH1B)"
FT /evidence="ECO:0000269|PubMed:16679490"
FT /id="VAR_027305"
FT VARIANT 205
FT /note="I -> V (in dbSNP:rs781946292)"
FT /id="VAR_009317"
FT VARIANT 212
FT /note="R -> C (in USH1B; dbSNP:rs121965080)"
FT /evidence="ECO:0000269|PubMed:8900236"
FT /id="VAR_009318"
FT VARIANT 212
FT /note="R -> H (in USH1B; dbSNP:rs28934610)"
FT /evidence="ECO:0000269|PubMed:8900236"
FT /id="VAR_009319"
FT VARIANT 214
FT /note="G -> R (in USH1B; dbSNP:rs111033283)"
FT /evidence="ECO:0000269|PubMed:9382091"
FT /id="VAR_009320"
FT VARIANT 218..219
FT /note="Missing (in USH1B)"
FT /id="VAR_009321"
FT VARIANT 241
FT /note="R -> C (in USH1B; dbSNP:rs782166819)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024044"
FT VARIANT 241
FT /note="R -> S (in USH1B)"
FT /id="VAR_009322"
FT VARIANT 244
FT /note="R -> P (in DFNB2; dbSNP:rs121965081)"
FT /evidence="ECO:0000269|PubMed:9171832"
FT /id="VAR_009323"
FT VARIANT 269
FT /note="Missing (in USH1B; dbSNP:rs781896482)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024045"
FT VARIANT 302
FT /note="R -> H (in dbSNP:rs41298135)"
FT /evidence="ECO:0000269|PubMed:8900236"
FT /id="VAR_009324"
FT VARIANT 397
FT /note="A -> D (in USH1B; dbSNP:rs1555067667)"
FT /evidence="ECO:0000269|PubMed:12112664,
FT ECO:0000269|PubMed:9382091"
FT /id="VAR_009325"
FT VARIANT 450
FT /note="E -> Q (in USH1B; dbSNP:rs1269622956)"
FT /evidence="ECO:0000269|PubMed:8900236"
FT /id="VAR_009326"
FT VARIANT 457
FT /note="A -> V (in USH1B; dbSNP:rs111033286)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024046"
FT VARIANT 458
FT /note="N -> I (in DFNA11; dbSNP:rs121965084)"
FT /evidence="ECO:0000269|PubMed:15221449"
FT /id="VAR_027306"
FT VARIANT 468
FT /note="H -> HQ (in USH1B)"
FT /evidence="ECO:0000269|PubMed:8900236"
FT /id="VAR_009327"
FT VARIANT 503
FT /note="P -> L (in USH1B)"
FT /evidence="ECO:0000269|PubMed:8900236"
FT /id="VAR_009328"
FT VARIANT 519
FT /note="G -> D (in USH1B; dbSNP:rs111033206)"
FT /evidence="ECO:0000269|PubMed:10930322,
FT ECO:0000269|PubMed:16679490"
FT /id="VAR_024047"
FT VARIANT 597
FT /note="V -> I"
FT /id="VAR_009329"
FT VARIANT 599
FT /note="M -> I (in DFNB2; dbSNP:rs121965082)"
FT /evidence="ECO:0000269|PubMed:9171833"
FT /id="VAR_009330"
FT VARIANT 602
FT /note="E -> K (in dbSNP:rs2276282)"
FT /id="VAR_056187"
FT VARIANT 651
FT /note="L -> P (in USH1B; atypical; dbSNP:rs876657416)"
FT /evidence="ECO:0000269|PubMed:9718356"
FT /id="VAR_009331"
FT VARIANT 652
FT /note="C -> R (in DFNB2)"
FT /evidence="ECO:0000269|PubMed:28281779"
FT /id="VAR_079504"
FT VARIANT 679
FT /note="V -> I (in dbSNP:rs35641839)"
FT /id="VAR_056188"
FT VARIANT 722
FT /note="G -> R (in DFNA11)"
FT /evidence="ECO:0000269|PubMed:15121790"
FT /id="VAR_027307"
FT VARIANT 756
FT /note="R -> W (in USH1B; dbSNP:rs782174733)"
FT /evidence="ECO:0000269|PubMed:15660226"
FT /id="VAR_024048"
FT VARIANT 826
FT /note="A -> T (in USH1B; dbSNP:rs368341987)"
FT /evidence="ECO:0000269|PubMed:9382091"
FT /id="VAR_009332"
FT VARIANT 853
FT /note="R -> C (in DFNA11; disturb calmodulin/MYO7A
FT binding)"
FT /evidence="ECO:0000269|PubMed:15300860"
FT /id="VAR_027308"
FT VARIANT 886..888
FT /note="Missing (in DFNA11)"
FT /evidence="ECO:0000269|PubMed:9354784"
FT /id="VAR_009333"
FT VARIANT 946
FT /note="M -> R (in USH1B; dbSNP:rs1296612982)"
FT /evidence="ECO:0000269|PubMed:24831256"
FT /id="VAR_071646"
FT VARIANT 955
FT /note="G -> S (in USH1B; dbSNP:rs781988557)"
FT /evidence="ECO:0000269|PubMed:9002678"
FT /id="VAR_009334"
FT VARIANT 968
FT /note="E -> D (in USH1B; dbSNP:rs111033233)"
FT /evidence="ECO:0000269|PubMed:10930322,
FT ECO:0000269|PubMed:15660226"
FT /id="VAR_024049"
FT VARIANT 1087
FT /note="L -> P (in USH1B; dbSNP:rs375050157)"
FT /evidence="ECO:0000269|PubMed:10364543"
FT /id="VAR_009335"
FT VARIANT 1170
FT /note="E -> K (in USH1B; dbSNP:rs111033214)"
FT /evidence="ECO:0000269|PubMed:10447383,
FT ECO:0000269|PubMed:12112664, ECO:0000269|PubMed:16679490"
FT /id="VAR_009336"
FT VARIANT 1240
FT /note="R -> Q (in USH1B; dbSNP:rs111033178)"
FT /evidence="ECO:0000269|PubMed:10930322,
FT ECO:0000269|PubMed:16679490"
FT /id="VAR_009337"
FT VARIANT 1248
FT /note="E -> K (in USH1B)"
FT /evidence="ECO:0000269|PubMed:23559863"
FT /id="VAR_071647"
FT VARIANT 1288
FT /note="A -> P (in USH1B; dbSNP:rs749747871)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_009338"
FT VARIANT 1327
FT /note="E -> K (in USH1B; dbSNP:rs373169422)"
FT /evidence="ECO:0000269|PubMed:12112664"
FT /id="VAR_027309"
FT VARIANT 1343
FT /note="R -> S (in USH1B; dbSNP:rs763469001)"
FT /id="VAR_009339"
FT VARIANT 1346
FT /note="Missing (in USH1B; dbSNP:rs1437625274)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024050"
FT VARIANT 1347..1351
FT /note="Missing (in USH1B)"
FT /evidence="ECO:0000269|PubMed:12112664"
FT /id="VAR_027310"
FT VARIANT 1566
FT /note="T -> M (in dbSNP:rs41298747)"
FT /evidence="ECO:0000269|PubMed:12112664,
FT ECO:0000269|PubMed:16679490"
FT /id="VAR_027311"
FT VARIANT 1602
FT /note="R -> Q (in USH1B; atypical; dbSNP:rs139889944)"
FT /evidence="ECO:0000269|PubMed:28887846,
FT ECO:0000269|PubMed:9718356"
FT /id="VAR_009340"
FT VARIANT 1628
FT /note="A -> S (in USH1B)"
FT /id="VAR_009341"
FT VARIANT 1666
FT /note="S -> C (in dbSNP:rs2276288)"
FT /evidence="ECO:0000269|PubMed:8622919,
FT ECO:0000269|PubMed:8884267"
FT /id="VAR_009343"
FT VARIANT 1666
FT /note="S -> G"
FT /id="VAR_027312"
FT VARIANT 1719
FT /note="Y -> C (in dbSNP:rs77625410)"
FT /evidence="ECO:0000269|PubMed:10447383,
FT ECO:0000269|PubMed:12112664, ECO:0000269|PubMed:16679490"
FT /id="VAR_009344"
FT VARIANT 1740
FT /note="G -> S (in dbSNP:rs12275336)"
FT /id="VAR_027313"
FT VARIANT 1743
FT /note="R -> W (in USH1B; dbSNP:rs111033287)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024051"
FT VARIANT 1812
FT /note="E -> K (in USH1B; dbSNP:rs377267777)"
FT /evidence="ECO:0000269|PubMed:25798947"
FT /id="VAR_074074"
FT VARIANT 1858
FT /note="L -> P (in USH1B; dbSNP:rs368657015)"
FT /evidence="ECO:0000269|PubMed:10930322,
FT ECO:0000269|PubMed:16679490"
FT /id="VAR_024052"
FT VARIANT 1873
FT /note="R -> W (in USH1B; dbSNP:rs397516321)"
FT /evidence="ECO:0000269|PubMed:16679490"
FT /id="VAR_027314"
FT VARIANT 1883
FT /note="R -> Q (in USH1B; dbSNP:rs111033215)"
FT /evidence="ECO:0000269|PubMed:15660226"
FT /id="VAR_024053"
FT VARIANT 1887
FT /note="P -> L (in USH1B; dbSNP:rs199606180)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024054"
FT VARIANT 1954
FT /note="L -> I (in dbSNP:rs948962)"
FT /evidence="ECO:0000269|PubMed:8622919,
FT ECO:0000269|PubMed:8884267"
FT /id="VAR_009345"
FT VARIANT 1962
FT /note="Missing (in USH1B)"
FT /evidence="ECO:0000269|PubMed:16679490"
FT /id="VAR_027315"
FT VARIANT 1992
FT /note="F -> I (in dbSNP:rs771906493)"
FT /id="VAR_009346"
FT VARIANT 2137
FT /note="G -> E (in USH1B; dbSNP:rs1191025888)"
FT /evidence="ECO:0000269|PubMed:9002678"
FT /id="VAR_009347"
FT VARIANT 2142
FT /note="D -> N (in dbSNP:rs1132036)"
FT /id="VAR_027316"
FT VARIANT 2163
FT /note="G -> S (in USH1B; dbSNP:rs747656448)"
FT /id="VAR_009348"
FT VARIANT 2187
FT /note="G -> D (in USH1B; dbSNP:rs397516332)"
FT /evidence="ECO:0000269|PubMed:10930322"
FT /id="VAR_024055"
FT CONFLICT 172
FT /note="L -> P (in Ref. 4; AAA20909)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="F -> L (in Ref. 2; AAC50927/AAC50722)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="D -> N (in Ref. 9; AAC51150)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="F -> S (in Ref. 2; AAC50927/AAC50722 and 6;
FT AAC50218)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="R -> Q (in Ref. 2; AAC50927/AAC50722 and 6;
FT AAC50218)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073..1075
FT /note="KIY -> RNS (in Ref. 6; AAC50218)"
FT /evidence="ECO:0000305"
FT CONFLICT 1237
FT /note="N -> S (in Ref. 2; AAC50927)"
FT /evidence="ECO:0000305"
FT HELIX 1715..1721
FT /evidence="ECO:0007829|PDB:5MV9"
FT TURN 1727..1731
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 1758..1760
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 1764..1780
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 1794..1805
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 1808..1821
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 1827..1841
FT /evidence="ECO:0007829|PDB:5MV9"
FT TURN 1848..1850
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 1851..1859
FT /evidence="ECO:0007829|PDB:5MV9"
FT TURN 1860..1863
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 1867..1880
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 1889..1896
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 1902..1908
FT /evidence="ECO:0007829|PDB:5MV9"
FT TURN 1909..1911
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 1912..1918
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 1924..1934
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 1943..1951
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 1953..1955
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 1962..1975
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 1989..1995
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2007..2012
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2014..2024
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2031..2046
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2053..2055
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2057..2059
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2060..2063
FT /evidence="ECO:0007829|PDB:5MV9"
FT TURN 2066..2068
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2069..2071
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2074..2085
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2086..2088
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2093..2104
FT /evidence="ECO:0007829|PDB:5MV9"
FT TURN 2108..2111
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 2113..2121
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 2123..2125
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 2127..2134
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 2137..2141
FT /evidence="ECO:0007829|PDB:5MV9"
FT TURN 2143..2145
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 2148..2152
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2154..2156
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 2157..2162
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 2164..2171
FT /evidence="ECO:0007829|PDB:5MV9"
FT STRAND 2179..2183
FT /evidence="ECO:0007829|PDB:5MV9"
FT HELIX 2187..2204
FT /evidence="ECO:0007829|PDB:5MV9"
SQ 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
