MYO7A_MOUSE
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 03-AUG-2022, entry version 197.
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). {ECO:0000250, ECO:0000250|UniProtKB:Q13402,
CC ECO:0000269|PubMed:12221080, ECO:0000269|PubMed:15590698,
CC ECO:0000269|PubMed:15976448, ECO:0000269|PubMed:16481439,
CC ECO:0000269|PubMed:17567809, ECO:0000269|PubMed:19774077,
CC ECO:0000269|PubMed:21311020, ECO:0000269|PubMed:21493626,
CC ECO:0000269|PubMed:27331610, 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}.
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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; 8.
DR IntAct; P97479; 5.
DR MINT; P97479; -.
DR STRING; 10090.ENSMUSP00000102745; -.
DR iPTMnet; P97479; -.
DR PhosphoSitePlus; P97479; -.
DR jPOST; P97479; -.
DR MaxQB; P97479; -.
DR PaxDb; P97479; -.
DR PeptideAtlas; P97479; -.
DR PRIDE; P97479; -.
DR ProteomicsDB; 287590; -. [P97479-1]
DR ProteomicsDB; 287591; -. [P97479-2]
DR ABCD; P97479; 32 sequenced antibodies.
DR Antibodypedia; 31226; 198 antibodies from 31 providers.
DR DNASU; 17921; -.
DR Ensembl; ENSMUST00000107127; ENSMUSP00000102744; ENSMUSG00000030761. [P97479-2]
DR Ensembl; ENSMUST00000107128; ENSMUSP00000102745; ENSMUSG00000030761. [P97479-1]
DR GeneID; 17921; -.
DR KEGG; mmu:17921; -.
DR UCSC; uc009ijy.2; mouse. [P97479-2]
DR UCSC; uc009ijz.2; mouse. [P97479-1]
DR CTD; 4647; -.
DR MGI; MGI:104510; Myo7a.
DR VEuPathDB; HostDB:ENSMUSG00000030761; -.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155350; -.
DR InParanoid; P97479; -.
DR OMA; LHRGNKH; -.
DR OrthoDB; 527681at2759; -.
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 74 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 169 other tissues.
DR ExpressionAtlas; P97479; baseline and differential.
DR Genevisible; P97479; MM.
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; 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: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:0047485; F:protein N-terminus binding; ISO: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: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:0048563; P:post-embryonic animal organ morphogenesis; 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; 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; 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; 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; 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
