ID MYO7A_MOUSE Reviewed; 2215 AA. AC P97479; E9QLP7; Q5MJ57; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 27-MAR-2024, entry version 206. DE RecName: Full=Unconventional myosin-VIIa; GN Name=Myo7a; Synonyms=Myo7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISEASE. RX PubMed=7870172; DOI=10.1038/374062a0; RA Gibson F., Walsh J., Mburu P., Varela A., Brown K.A., Antonio M., RA Beisel K.W., Steel K.P., Brown S.D.M.; RT "A type VII myosin encoded by the mouse deafness gene shaker-1."; RL Nature 374:62-64(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9680294; DOI=10.1046/j.1365-4624.1997.00020.x; RA Mburu P., Liu X.-Z., Walsh J., Saw D. Jr., Cope M.J., Gibson F., RA Kendrick-Jones J., Steel K.P., Brown S.D.M.; RT "Mutation analysis of the mouse myosin VIIA deafness gene."; RL Genes Funct. 1:191-203(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-2215 (ISOFORM 2), AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; TISSUE=Inner ear; RX PubMed=15654330; DOI=10.1038/ncb1219; RA Belyantseva I.A., Boger E.T., Naz S., Frolenkov G.I., Sellers J.R., RA Ahmed Z.M., Griffith A.J., Friedman T.B.; RT "Myosin-XVa is required for tip localization of whirlin and differential RT elongation of hair-cell stereocilia."; RL Nat. Cell Biol. 7:148-156(2005). RN [5] RP INTERACTION WITH MYRIP. RX PubMed=12221080; DOI=10.1074/jbc.m203862200; RA Fukuda M., Kuroda T.S.; RT "Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a RT novel linker protein that interacts with Rab27, myosin Va/VIIa, and RT actin."; RL J. Biol. Chem. 277:43096-43103(2002). RN [6] RP INTERACTION WITH WHRN. RX PubMed=15590698; DOI=10.1093/hmg/ddi036; RA Delprat B., Michel V., Goodyear R., Yamasaki Y., Michalski N., RA El-Amraoui A., Perfettini I., Legrain P., Richardson G., Hardelin J.-P., RA Petit C.; RT "Myosin XVa and whirlin, two deafness gene products required for hair RT bundle growth, are located at the stereocilia tips and interact directly."; RL Hum. Mol. Genet. 14:401-410(2005). RN [7] RP INTERACTION WITH PLEKHB1. RX PubMed=15976448; DOI=10.1242/jcs.02424; RA Etournay R., El-Amraoui A., Bahloul A., Blanchard S., Roux I., Pezeron G., RA Michalski N., Daviet L., Hardelin J.-P., Legrain P., Petit C.; RT "PHR1, an integral membrane protein of the inner ear sensory cells, RT directly interacts with myosin 1c and myosin VIIa."; RL J. Cell Sci. 118:2891-2899(2005). RN [8] RP INTERACTION WITH PCDH15. RX PubMed=16481439; DOI=10.1523/jneurosci.4251-05.2006; RA Senften M., Schwander M., Kazmierczak P., Lillo C., Shin J.B., Hasson T., RA Geleoc G.S., Gillespie P.G., Williams D., Holt J.R., Muller U.; RT "Physical and functional interaction between protocadherin 15 and myosin RT VIIa in mechanosensory hair cells."; RL J. Neurosci. 26:2060-2071(2006). RN [9] RP INTERACTION WITH ADGRV1 AND USH2A. RX PubMed=17567809; DOI=10.1523/jneurosci.0342-07.2007; RA Michalski N., Michel V., Bahloul A., Lefevre G., Barral J., Yagi H., RA Chardenoux S., Weil D., Martin P., Hardelin J.P., Sato M., Petit C.; RT "Molecular characterization of the ankle-link complex in cochlear hair RT cells and its role in the hair bundle functioning."; RL J. Neurosci. 27:6478-6488(2007). RN [10] RP INTERACTION WITH TWF2. RC STRAIN=C3Heb/FeJ; TISSUE=Inner ear; RX PubMed=19774077; DOI=10.1371/journal.pone.0007097; RA Rzadzinska A.K., Nevalainen E.M., Prosser H.M., Lappalainen P., Steel K.P.; RT "MyosinVIIa interacts with Twinfilin-2 at the tips of mechanosensory RT stereocilia in the inner ear."; RL PLoS ONE 4:E7097-E7097(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1563; SER-1569 AND THR-1571, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [12] 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 [13] RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. 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 [14] RP INTERACTION WITH PDZD7, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=27525485; DOI=10.7554/elife.18312; RA Morgan C.P., Krey J.F., Grati M., Zhao B., Fallen S., Kannan-Sundhari A., RA Liu X.Z., Choi D., Mueller U., Barr-Gillespie P.G.; RT "PDZD7-MYO7A complex identified in enriched stereocilia membranes."; RL Elife 5:0-0(2016). RN [15] RP INTERACTION WITH MYH9. 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 [16] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 965-1687 IN COMPLEX WITH USH1G, RP INTERACTION WITH USH1G, AND MUTAGENESIS OF ALA-1189 AND PHE-1473. RX PubMed=21311020; DOI=10.1126/science.1198848; RA Wu L., Pan L., Wei Z., Zhang M.; RT "Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo."; RL Science 331:757-760(2011). 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. Mediates intracellular transport of RPE65 in CC the retina pigment epithelium. In the inner ear, plays an important CC role in differentiation, morphogenesis and organization of cochlear CC hair cell bundles. Motor protein that is a part of the functional CC network formed by USH1C, USH1G, CDH23 and MYO7A that mediates CC mechanotransduction in cochlear hair cells. Required for normal CC hearing. Involved in hair-cell vesicle trafficking of aminoglycosides, CC which are known to induce ototoxicity. {ECO:0000269|PubMed:21493626, CC ECO:0000269|PubMed:21709241, ECO:0000269|PubMed:27525485}. 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 (By similarity). Interacts with MYRIP CC (PubMed:12221080). Interacts with RPE65 (PubMed:21493626). Interacts CC with CIB2 (By similarity). May interact with CALM (By similarity). CC Interacts with WHRN (PubMed:15590698). Interacts with PLEKHB1 (via PH CC domain) (PubMed:15976448). Interacts with PCDH15 (PubMed:16481439). CC Interacts with TWF2 (PubMed:19774077). Interacts with USH1G CC (PubMed:21311020). Interacts with MYH9 (PubMed:27331610). Interacts CC (via MyTH4-FERM domains) with cytoplasmic regions of ADGRV1 and USH2A CC (PubMed:17567809). Interacts with PDZD7 (via MyTH4-FERM domains) CC (PubMed:27525485). Interacts with CALML4 (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:Q13402, ECO:0000269|PubMed:12221080, CC ECO:0000269|PubMed:15590698, ECO:0000269|PubMed:15976448, CC ECO:0000269|PubMed:16481439, ECO:0000269|PubMed:17567809, CC ECO:0000269|PubMed:19774077, ECO:0000269|PubMed:21311020, CC ECO:0000269|PubMed:21493626, ECO:0000269|PubMed:27331610, CC ECO:0000269|PubMed:27525485}. CC -!- INTERACTION: CC P97479; O70309: Itgb5; NbExp=3; IntAct=EBI-1149557, EBI-8401821; CC P97479; Q91ZQ5: Rpe65; NbExp=3; IntAct=EBI-1149557, EBI-11682496; CC P97479; Q80T11: Ush1g; NbExp=4; IntAct=EBI-1149557, EBI-7418889; CC P97479; P18084: ITGB5; Xeno; NbExp=8; IntAct=EBI-1149557, EBI-1223434; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21709241}. CC Cytoplasm, cell cortex {ECO:0000269|PubMed:21709241}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:21709241}. Synapse CC {ECO:0000250|UniProtKB:Q13402}. 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 (By similarity). 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 (By similarity). Detected at the tip of cochlear CC hair cell stereocilia (PubMed:27525485). The complex formed by MYO7A, CC USH1C and USH1G colocalizes with F-actin (By similarity). CC {ECO:0000250|UniProtKB:Q13402, ECO:0000269|PubMed:27525485}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P97479-1; Sequence=Displayed; CC Name=2; CC IsoId=P97479-2; Sequence=VSP_042238; CC -!- TISSUE SPECIFICITY: Detected in mechanosensory stereocilia of cochlea CC hair cells (at protein level). Expressed in the retina, cochlea, kidney CC and liver. {ECO:0000269|PubMed:15654330, ECO:0000269|PubMed:21493626, CC ECO:0000269|PubMed:21709241}. CC -!- DEVELOPMENTAL STAGE: In the inner ear of the 16.5 day old embryo, CC expressed only in the cochlear and vestibular sensory hair cells. In CC addition, expression also occurs in the epithelial cells of the small CC intestine, hepatocytes, and choroidal plexus. 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:0000250|UniProtKB:Q13402}. CC -!- DISEASE: Note=Defects in Myo7a are the cause of the shaker-1 (sh-1) CC phenotype which affects only the inner ear. Sh-1 homozygote mutants CC show hyperactivity, head tossing and circling due to vestibular CC dysfunction, together with typical neuroepithelial-type cochlear CC defects involving dysfunction and progressive degeneration of the organ CC of Corti. {ECO:0000269|PubMed:7870172}. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U81453; AAB40708.1; -; mRNA. DR EMBL; AC115022; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC119880; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC157792; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY821853; AAV87212.1; -; mRNA. DR CCDS; CCDS40026.1; -. [P97479-2] DR CCDS; CCDS57565.1; -. [P97479-1] DR PIR; T30870; T30870. DR RefSeq; NP_001243010.1; NM_001256081.1. [P97479-1] DR RefSeq; NP_001243012.1; NM_001256083.1. DR RefSeq; NP_032689.2; NM_008663.2. [P97479-2] DR RefSeq; XP_011239993.1; XM_011241691.1. DR PDB; 3PVL; X-ray; 2.80 A; A=965-1687. DR PDB; 5WST; X-ray; 2.10 A; A/B=866-932. DR PDB; 5WSU; X-ray; 3.00 A; C/D=834-935. DR PDB; 5WSV; X-ray; 2.33 A; B/D=828-870. DR PDBsum; 3PVL; -. DR PDBsum; 5WST; -. DR PDBsum; 5WSU; -. DR PDBsum; 5WSV; -. DR AlphaFoldDB; P97479; -. DR SMR; P97479; -. DR BioGRID; 201669; 9. DR IntAct; P97479; 5. DR MINT; P97479; -. DR STRING; 10090.ENSMUSP00000102745; -. DR iPTMnet; P97479; -. DR PhosphoSitePlus; P97479; -. DR SwissPalm; P97479; -. DR jPOST; P97479; -. DR MaxQB; P97479; -. DR PaxDb; 10090-ENSMUSP00000102745; -. DR PeptideAtlas; P97479; -. DR ProteomicsDB; 287590; -. [P97479-1] DR ProteomicsDB; 287591; -. [P97479-2] DR Pumba; P97479; -. DR ABCD; P97479; 18 sequenced antibodies. DR Antibodypedia; 31226; 240 antibodies from 31 providers. DR DNASU; 17921; -. DR Ensembl; ENSMUST00000107127.8; ENSMUSP00000102744.2; ENSMUSG00000030761.17. [P97479-2] DR Ensembl; ENSMUST00000107128.8; ENSMUSP00000102745.2; ENSMUSG00000030761.17. [P97479-1] DR GeneID; 17921; -. DR KEGG; mmu:17921; -. DR UCSC; uc009ijy.2; mouse. [P97479-2] DR UCSC; uc009ijz.2; mouse. [P97479-1] DR AGR; MGI:104510; -. DR CTD; 4647; -. DR MGI; MGI:104510; Myo7a. DR VEuPathDB; HostDB:ENSMUSG00000030761; -. DR eggNOG; KOG4229; Eukaryota. DR GeneTree; ENSGT00940000155350; -. DR InParanoid; P97479; -. DR OMA; GFQGRCR; -. DR OrthoDB; 1094820at2759; -. DR PhylomeDB; P97479; -. DR TreeFam; TF335306; -. DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision). DR BioGRID-ORCS; 17921; 0 hits in 79 CRISPR screens. DR ChiTaRS; Myo7a; mouse. DR PRO; PR:P97479; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; P97479; Protein. DR Bgee; ENSMUSG00000030761; Expressed in fourth ventricle and 173 other cell types or tissues. DR ExpressionAtlas; P97479; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB. DR GO; GO:0042470; C:melanosome; IDA:MGI. DR GO; GO:0005902; C:microvillus; ISO:MGI. DR GO; GO:0016459; C:myosin complex; ISO:MGI. DR GO; GO:0031477; C:myosin VII complex; ISO:MGI. DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI. DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB. DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB. DR GO; GO:0032420; C:stereocilium; IDA:UniProtKB. DR GO; GO:0120044; C:stereocilium base; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IDA:UniProtKB. DR GO; GO:1990435; C:upper tip-link density; ISO:MGI. DR GO; GO:0031982; C:vesicle; IBA:GO_Central. DR GO; GO:0003779; F:actin binding; ISO:MGI. DR GO; GO:0051015; F:actin filament binding; ISO:MGI. DR GO; GO:0043531; F:ADP binding; ISO:MGI. DR GO; GO:0005524; F:ATP binding; ISO:MGI. DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB. DR GO; GO:0003774; F:cytoskeletal motor activity; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0000146; F:microfilament motor activity; ISO:MGI. DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0030507; F:spectrin binding; ISO:MGI. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0030048; P:actin filament-based movement; ISO:MGI. DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI. DR GO; GO:0030030; P:cell projection organization; IMP:MGI. DR GO; GO:0090102; P:cochlea development; IMP:MGI. DR GO; GO:0050957; P:equilibrioception; ISO:MGI. DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI. DR GO; GO:0048839; P:inner ear development; IMP:MGI. DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI. DR GO; GO:0060113; P:inner ear receptor cell differentiation; IMP:MGI. DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI. DR GO; GO:0006886; P:intracellular protein transport; IMP:MGI. DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB. DR GO; GO:0042490; P:mechanoreceptor differentiation; IMP:MGI. DR GO; GO:0006909; P:phagocytosis; IMP:MGI. DR GO; GO:0001845; P:phagolysosome assembly; IMP:MGI. DR GO; GO:0051875; P:pigment granule localization; IMP:MGI. DR GO; GO:0051904; P:pigment granule transport; IMP:MGI. DR GO; GO:0008104; P:protein localization; IDA:UniProtKB. DR GO; GO:0007423; P:sensory organ development; IBA:GO_Central. DR GO; GO:0007600; P:sensory perception; IMP:MGI. DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:MGI. DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI. DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central. DR GO; GO:0007601; P:visual perception; IMP:MGI. DR CDD; cd17092; FERM1_F1_Myosin-VII; 1. DR CDD; cd17093; FERM2_F1_Myosin-VII; 1. 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 CDD; cd11881; SH3_MYO7A; 1. DR CDD; cd22249; UDM1_RNF168_RNF169-like; 1. DR Gene3D; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.190; -; 1. DR Gene3D; 1.20.58.530; -; 1. DR Gene3D; 1.20.80.10; -; 2. DR Gene3D; 6.20.240.20; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1. DR Gene3D; 1.25.40.530; MyTH4 domain; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2. DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR22692; MYOSIN VII, XV; 1. DR PANTHER; PTHR22692:SF34; MYOSIN VIIA; 1. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF00612; IQ; 3. 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF47031; Second domain of FERM; 2. DR SUPFAM; SSF50044; SH3-domain; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 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. DR Genevisible; P97479; MM. 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; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; SH3 domain; Synapse; Transport. FT CHAIN 1..2215 FT /note="Unconventional myosin-VIIa" FT /id="PRO_0000123467" 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:0000250|UniProtKB:Q13402" FT BINDING 158..165 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305" FT MOD_RES 1563 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1569 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1571 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 1523..1560 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15654330" FT /id="VSP_042238" FT VARIANT 241 FT /note="R -> P (in sh-1)" FT VARIANT 502 FT /note="R -> P (in sh-1)" FT MUTAGEN 1189 FT /note="A->E: Strongly reduced affinity for USH1G." FT /evidence="ECO:0000269|PubMed:21311020" FT MUTAGEN 1473 FT /note="F->Q: Reduced affinity for USH1G." FT /evidence="ECO:0000269|PubMed:21311020" FT CONFLICT 85 FT /note="L -> R (in Ref. 1; AAB40708)" FT /evidence="ECO:0000305" FT CONFLICT 238 FT /note="E -> S (in Ref. 1; AAB40708)" FT /evidence="ECO:0000305" FT CONFLICT 589 FT /note="I -> V (in Ref. 1; AAB40708)" FT /evidence="ECO:0000305" FT CONFLICT 682 FT /note="V -> G (in Ref. 1; AAB40708)" FT /evidence="ECO:0000305" FT CONFLICT 1156 FT /note="F -> L (in Ref. 1; AAB40708)" FT /evidence="ECO:0000305" FT HELIX 828..853 FT /evidence="ECO:0007829|PDB:5WSV" FT HELIX 866..929 FT /evidence="ECO:0007829|PDB:5WST" FT HELIX 1001..1008 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1032..1048 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1070..1075 FT /evidence="ECO:0007829|PDB:3PVL" FT TURN 1076..1079 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1084..1088 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1150..1163 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1165..1167 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1168..1178 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1185..1201 FT /evidence="ECO:0007829|PDB:3PVL" FT TURN 1206..1208 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1209..1217 FT /evidence="ECO:0007829|PDB:3PVL" FT TURN 1221..1223 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1224..1237 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1246..1254 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1258..1264 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1269..1274 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1280..1290 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1299..1305 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1308..1313 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1319..1331 FT /evidence="ECO:0007829|PDB:3PVL" FT TURN 1332..1334 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1337..1339 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1343..1348 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1357..1359 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1361..1376 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1385..1400 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1406..1416 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1419..1421 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1424..1426 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1428..1444 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1451..1465 FT /evidence="ECO:0007829|PDB:3PVL" FT TURN 1467..1469 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1472..1482 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1487..1494 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1497..1501 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1507..1512 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1513..1515 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1516..1522 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1564..1566 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1569..1574 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1579..1583 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1587..1604 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1607..1612 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1632..1634 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1640..1645 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1646..1653 FT /evidence="ECO:0007829|PDB:3PVL" FT TURN 1654..1656 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1659..1663 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1664..1666 FT /evidence="ECO:0007829|PDB:3PVL" FT STRAND 1667..1669 FT /evidence="ECO:0007829|PDB:3PVL" FT HELIX 1678..1684 FT /evidence="ECO:0007829|PDB:3PVL" SQ SEQUENCE 2215 AA; 254939 MW; D942FC7674B75EC7 CRC64; MVILQKGDYV WMDLKSGQEF DVPIGAVVKL CDSGQIQVVD DEDNEHWISP QNATHIKPMH PTSVHGVEDM IRLGDLNEAG ILRNLLIRYR DHLIYTYTGS ILVAVNPYQL LSIYSPEHIR QYTNKKIGEM PPHIFAIADN CYFNMKRNNR DQCCIISGES GAGKTESTKL ILQFLAAISG QHSWIEQQVL EATPILEAFG NAKTIRNDNS SRFGKYIDIH FNKRGAIEGA KIEQYLLEKS RVCRQAPDER NYHVFYCMLE GMNEEEKKKL GLGQAADYNY LAMGNCITCE GRVDSQEYAN IRSAMKVLMF TDTENWEISK LLAAILHMGN LQYEARTFEN LDACEVLFSP SLATAASLLE VNPPDLMSCL TSRTLITRGE TVSTPLSREQ ALDVRDAFVK GIYGRLFVWI VEKINAAIYK PPPLEVKNSR RSIGLLDIFG FENFTVNSFE QLCINFANEH LQQFFVRHVF KLEQEEYDLE SIDWLHIEFT DNQEALDMIA NRPMNVISLI DEESKFPKGT DATMLHKLNS QHKLNANYVP PKNSHETQFG INHFAGVVYY ESQGFLEKNR DTLHGDIIQL VHSSRNKFIK QIFQADVAMG AETRKRSPTL SSQFKRSLEL LMRTLGACQP FFVRCIKPNE FKKPMLFDRH LCVRQLRYSG MMETIRIRHA GYPIRYSFVE FVERYRVLLP GVKPAYKQGD LRGTCQRMAE AVLGTHDDWQ IGKTKIFLKD HHDMLLEVER DKAITDRVIL LQKVIRGFKD RSNFLRLKSA ATLIQRHWRG HHCRKNYELI RLGFLRLQAL HRSRKLHKQY RLARQRIIEF QARCRAYLVR KAFRHRLWAV ITVQAYARGM IARRLHRRLR VEYQRRLEAE RMRLAEEEKL RKEMSAKKAK EEAERKHQER LAQLAREDAE RELKEKEEAR RKKELLEQME KARHEPINHS DMVDKMFGFL GTSGSLPGQE GQAPSGFEDL ERGRREMVEE DVDAALPLPD EDEEDLSEYK FAKFAATYFQ GTTTHSYTRR PLKQPLLYHD DEGDQLAALA VWITILRFMG DLPEPKYHTA MSDGSEKIPV MTKIYETLGK KTYKRELQAL QGEGETQLPE GQKKTSVRHK LVHLTLKKKS KLTEEVTKRL NDGESTVQGN SMLEDRPTSN LEKLHFIIGN GILRPALRDE IYCQISKQLT HNPSKSSYAR GWILVSLCVG CFAPSEKFVK YLRNFIHGGP PGYAPYCEER LRRTFVNGTR TQPPSWLELQ ATKSKKPIML PVTFMDGTTK TLLTDSATTA RELCNALADK ISLKDRFGFS LYIALFDKVS SLGSGSDHVM DAISQCEQYA KEQGAQERNA PWRLFFRKEV FTPWHNPSED NVATNLIYQQ VVRGVKFGEY RCEKEDDLAE LASQQYFVDY GSEMILERLL SLVPTYIPDR EITPLKNLEK WAQLAIAAHK KGIYAQRRTD SQKVKEDVVN YARFKWPLLF SRFYEAYKFS GPPLPKSDVI VAVNWTGVYF VDEQEQVLLE LSFPEIMAVS SSRECRVLLS LGCSDLGCAT CQSGRAGLTP AGPCSPCWSC RGTKMMAPSF TLATIKGDEY TFTSSNAEDI RDLVVTFLEG LRKRSKYVVA LQDNPNPAGE ESGFLSFAKG DLIILDHDTG EQVMNSGWAN GINERTKQRG DFPTDCVYVM PTVTLPPREI VALVTMTPDQ RQDVVRLLQL RTAEPEVRAK PYTLEEFSYD YFRPPPKHTL SRVMVSKARG KDRLWSHTRE PLKQALLKKI LGSEELSQEA CMAFVAVLKY MGDYPSKRMR SVNELTDQIF EWALKAEPLK DEAYVQILKQ LTDNHIRYSE ERGWELLWLC TGLFPPSNIL LPHVQRFLQS RKHCPLAIDC LQRLQKALRN GSRKYPPHLV EVEAIQHKTT QIFHKVYFPD DTDEAFEVES STKAKDFCQN IASRLLLKSS EGFSLFVKIA DKVISVPEND FFFDFVRHLT DWIKKARPIK DGIVPSLTYQ VFFMKKLWTT TVPGKDPMAD SIFHYYQELP KYLRGYHKCT REEVLQLGAL IYRVKFEEDK SYFPSIPKLL RELVPQDLIR QVSPDDWKRS IVAYFNKHAG KSKEEAKLAF LKLIFKWPTF GSAFFEVKQT TEPNFPEILL IAINKYGVSL IDPRTKDILT THPFTKISNW SSGNTYFHIT IGNLVRGSKL LCETSLGYKM DDLLTSYISQ MLTAMSKQRN SRSGR //