LOCUS       NP_032689               2177 aa            linear   ROD 04-MAR-2025
DEFINITION  unconventional myosin-VIIa isoform 2 [Mus musculus].
ACCESSION   NP_032689
VERSION     NP_032689.2
DBSOURCE    REFSEQ: accession NM_008663.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 2177)
  AUTHORS   Sun,Y., Ren,M., Zhang,Y., Li,S., Luo,Z., Sun,S., He,S., Wang,G.,
            Zhang,D., Mansour,S.L., Song,L. and Liu,Z.
  TITLE     Casz1 is required for both inner hair cell fate stabilization and
            outer hair cell survival
  JOURNAL   Science, eado4930 (2025) In press
   PUBMED   39883789
  REMARK    Publication Status: Available-Online prior to print
REFERENCE   2  (residues 1 to 2177)
  AUTHORS   Wu,M., Jia,G., Liu,Y., Lou,Y., Li,Y., Xia,M., Li,H. and Li,W.
  TITLE     PKM2 controls cochlear development through lactate-dependent
            transcriptional regulation
  JOURNAL   Proc Natl Acad Sci U S A 122 (2), e2410829122 (2025)
   PUBMED   39773029
REFERENCE   3  (residues 1 to 2177)
  AUTHORS   Underhill,A., Webb,S., Grandi,F.C., Jeng,J.Y., de Monvel,J.B.,
            Plion,B., Carlton,A.J., Amariutei,A.E., Voulgari,N., De Faveri,F.,
            Ceriani,F., Mustapha,M., Johnson,S.L., Safieddine,S., Kros,C.J. and
            Marcotti,W.
  TITLE     MYO7A is required for the functional integrity of the
            mechanoelectrical transduction complex in hair cells of the adult
            cochlea
  JOURNAL   Proc Natl Acad Sci U S A 122 (1), e2414707122 (2025)
   PUBMED   39746042
REFERENCE   4  (residues 1 to 2177)
  AUTHORS   O'Connor,A.P., Amariutei,A.E., Zanella,A., Hool,S.A., Carlton,A.J.,
            Kong,F., Saenz-Roldan,M., Jeng,J.Y., Lecomte,M.J., Johnson,S.L.,
            Safieddine,S. and Marcotti,W.
  TITLE     In vivo AAV9-Myo7a gene rescue restores hearing and cholinergic
            efferent innervation in inner hair cells
  JOURNAL   JCI Insight 9 (23), e182138 (2024)
   PUBMED   39641274
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2177)
  AUTHORS   Fritzsch,B., Weng,X., Yamoah,E.N., Qin,T., Hui,C.C.,
            Lebron-Mora,L., Pavlinkova,G. and Sham,M.H.
  TITLE     Irx3/5 Null Deletion in Mice Blocks Cochlea-Saccule Segregation and
            Disrupts the Auditory Tonotopic Map
  JOURNAL   J Comp Neurol 532 (12), e70008 (2024)
   PUBMED   39655644
REFERENCE   6  (residues 1 to 2177)
  AUTHORS   Brown,K.A., Sutcliffe,M.J., Steel,K.P. and Brown,S.D.
  TITLE     Close linkage of the olfactory marker protein gene to the mouse
            deafness mutation shaker-1
  JOURNAL   Genomics 13 (1), 189-193 (1992)
   PUBMED   1349573
REFERENCE   7  (residues 1 to 2177)
  AUTHORS   Rinchik,E.M., Johnson,D.K., Margolis,F.L., Jackson,I.J.,
            Russell,L.B. and Carpenter,D.A.
  TITLE     Reverse genetics in the mouse and its application to the study of
            deafness
  JOURNAL   Ann N Y Acad Sci 630, 80-92 (1991)
   PUBMED   1952626
REFERENCE   8  (residues 1 to 2177)
  AUTHORS   MacSwiney,F.J. and Wallace,M.E.
  TITLE     Genetics of warfarin-resistance in house mice of three separate
            localities
  JOURNAL   J Hyg (Lond) 80 (1), 69-75 (1978)
   PUBMED   621381
REFERENCE   9  (residues 1 to 2177)
  AUTHORS   Eicher,E.M. and Coleman,D.I.
  TITLE     Influence of gene duplication and X-inactivation on mouse
            mitochondrial malic enzyme activity and electrophoretic patterns
  JOURNAL   Genetics 85 (4), 647-658 (1977)
   PUBMED   863237
REFERENCE   10 (residues 1 to 2177)
  AUTHORS   Wallace,M.E. and MacSwiney,F.J.
  TITLE     A major gene controlling warfarin-resistance in the house mouse
  JOURNAL   J Hyg (Lond) 76 (2), 173-181 (1976)
   PUBMED   1063212
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC115022.11, AY821853.1 and AC157792.4.
            
            On Oct 4, 2006 this sequence version replaced NP_032689.1.
            
            Transcript Variant: This variant (2) lacks an in-frame segment in
            the coding region, compared to variant 1. The resulting isoform (2)
            is shorter than isoform 1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed/partial sample support SAMN00849374,
                              SAMN00849375 [ECO:0000350]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2177
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 53.57 cM"
     Protein         1..2177
                     /product="unconventional myosin-VIIa isoform 2"
                     /note="myosin-VIIa; motor protein; shaker 1;
                     unconventional myosin-VIIa"
                     /calculated_mol_wt=250967
     Region          79..729
                     /region_name="MYSc_Myo7"
                     /note="class VII myosin, motor domain; cd01381"
                     /db_xref="CDD:276832"
     Site            order(106..114,158..165,202..212,437..442)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:276832"
     Site            106..114
                     /site_type="other"
                     /note="purine-binding loop"
                     /db_xref="CDD:276832"
     Site            158..165
                     /site_type="other"
                     /note="P-loop"
                     /db_xref="CDD:276832"
     Site            202..212
                     /site_type="other"
                     /note="switch I region"
                     /db_xref="CDD:276832"
     Site            437..442
                     /site_type="other"
                     /note="switch II region"
                     /db_xref="CDD:276832"
     Site            466..489
                     /site_type="other"
                     /note="relay loop"
                     /db_xref="CDD:276832"
     Region          632..639
                     /region_name="Actin-binding. /evidence=ECO:0000305"
                     /note="propagated from UniProtKB/Swiss-Prot (P97479.2)"
     Site            660..669
                     /site_type="other"
                     /note="SH1 helix"
                     /db_xref="CDD:276832"
     Site            order(672..697,717..729)
                     /site_type="other"
                     /note="converter subdomain"
                     /db_xref="CDD:276832"
     Region          766..787
                     /region_name="IQ"
                     /note="Calmodulin-binding motif; smart00015"
                     /db_xref="CDD:197470"
     Region          <803..>975
                     /region_name="PTZ00121"
                     /note="MAEBL; Provisional"
                     /db_xref="CDD:173412"
     Region          <857..>935
                     /region_name="MAP7"
                     /note="MAP7 (E-MAP-115) family; pfam05672"
                     /db_xref="CDD:461709"
     Region          858..935
                     /region_name="SAH. /evidence=ECO:0000250|UniProtKB:Q13402"
                     /note="propagated from UniProtKB/Swiss-Prot (P97479.2)"
     Region          1017..1253
                     /region_name="MyTH4"
                     /note="Domain in Myosin and Kinesin Tails; smart00139"
                     /db_xref="CDD:214535"
     Region          1257..1355
                     /region_name="FERM1_F1_Myosin-VII"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain 1, F1 sub-domain, found in Myosin-VIIa,
                     Myosin-VIIb, and similar proteins; cd17092"
                     /db_xref="CDD:340612"
     Region          1259..1474
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Site            order(1307..1312,1317,1325,1347)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:340612"
     Region          1468..1566
                     /region_name="FERM_C1_MyoVII"
                     /note="FERM domain C-lobe, repeat 1, of Myosin VII
                     (MyoVII/Myo7); cd13198"
                     /db_xref="CDD:270019"
     Site            order(1468..1469,1473,1475,1490,1505)
                     /site_type="other"
                     /note="CEN1 peptide binding site [polypeptide binding]"
                     /db_xref="CDD:270019"
     Site            order(1478,1500,1502,1509)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270019"
     Site            1525
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P97479.2)"
     Site            1531
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P97479.2)"
     Site            1533
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P97479.2)"
     Site            1553..1564
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270019"
     Region          1567..1631
                     /region_name="SH3_MYO7A"
                     /note="Src Homology 3 domain of Myosin VIIa and similar
                     proteins; cd11881"
                     /db_xref="CDD:212814"
     Site            order(1574,1576,1579,1586,1609..1610,1625,1627..1628)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212814"
     Region          1709..1858
                     /region_name="MyTH4"
                     /note="Domain in Myosin and Kinesin Tails; smart00139"
                     /db_xref="CDD:214535"
     Region          1863..1960
                     /region_name="FERM2_F1_Myosin-VII"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain 2, F1 sub-domain, found in Myosin-VIIa,
                     Myosin-VIIb, and similar proteins; cd17093"
                     /db_xref="CDD:340613"
     Region          1865..2077
                     /region_name="B41"
                     /note="Band 4.1 homologues; smart00295"
                     /db_xref="CDD:214604"
     Region          2073..2168
                     /region_name="FERM_C2_MyoVII"
                     /note="FERM domain C-lobe, repeat 2, of Myosin VII
                     (MyoVII, Myo7); cd13199"
                     /db_xref="CDD:270020"
     Site            order(2081,2102,2104,2110)
                     /site_type="other"
                     /note="putative phosphoinositide binding site [chemical
                     binding]"
                     /db_xref="CDD:270020"
     Site            order(2114,2118..2121,2156,2160,2163..2164)
                     /site_type="other"
                     /note="putative peptide binding site [polypeptide
                     binding]"
                     /db_xref="CDD:270020"
     Site            2156..2167
                     /site_type="other"
                     /note="putative actin binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:270020"
     CDS             1..2177
                     /gene="Myo7a"
                     /gene_synonym="Hdb; Myo7; nmf371; polka; sh-1; sh1; USH1B"
                     /coded_by="NM_008663.2:261..6794"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS40026.1"
                     /db_xref="GeneID:17921"
                     /db_xref="MGI:MGI:104510"
ORIGIN      
        1 mvilqkgdyv wmdlksgqef dvpigavvkl cdsgqiqvvd dednehwisp qnathikpmh
       61 ptsvhgvedm irlgdlneag ilrnlliryr dhliytytgs ilvavnpyql lsiyspehir
      121 qytnkkigem pphifaiadn cyfnmkrnnr dqcciisges gagktestkl ilqflaaisg
      181 qhswieqqvl eatpileafg naktirndns srfgkyidih fnkrgaiega kieqylleks
      241 rvcrqapder nyhvfycmle gmneeekkkl glgqaadyny lamgncitce grvdsqeyan
      301 irsamkvlmf tdtenweisk llaailhmgn lqyeartfen ldacevlfsp slataaslle
      361 vnppdlmscl tsrtlitrge tvstplsreq aldvrdafvk giygrlfvwi vekinaaiyk
      421 ppplevknsr rsiglldifg fenftvnsfe qlcinfaneh lqqffvrhvf kleqeeydle
      481 sidwlhieft dnqealdmia nrpmnvisli deeskfpkgt datmlhklns qhklnanyvp
      541 pknshetqfg inhfagvvyy esqgfleknr dtlhgdiiql vhssrnkfik qifqadvamg
      601 aetrkrsptl ssqfkrslel lmrtlgacqp ffvrcikpne fkkpmlfdrh lcvrqlrysg
      661 mmetirirha gypirysfve fveryrvllp gvkpaykqgd lrgtcqrmae avlgthddwq
      721 igktkiflkd hhdmllever dkaitdrvil lqkvirgfkd rsnflrlksa atliqrhwrg
      781 hhcrknyeli rlgflrlqal hrsrklhkqy rlarqriief qarcraylvr kafrhrlwav
      841 itvqayargm iarrlhrrlr veyqrrleae rmrlaeeekl rkemsakkak eeaerkhqer
      901 laqlaredae relkekeear rkkelleqme karhepinhs dmvdkmfgfl gtsgslpgqe
      961 gqapsgfedl ergrremvee dvdaalplpd edeedlseyk fakfaatyfq gttthsytrr
     1021 plkqpllyhd degdqlaala vwitilrfmg dlpepkyhta msdgsekipv mtkiyetlgk
     1081 ktykrelqal qgegetqlpe gqkktsvrhk lvhltlkkks klteevtkrl ndgestvqgn
     1141 smledrptsn leklhfiign gilrpalrde iycqiskqlt hnpskssyar gwilvslcvg
     1201 cfapsekfvk ylrnfihggp pgyapyceer lrrtfvngtr tqppswlelq atkskkpiml
     1261 pvtfmdgttk tlltdsatta relcnaladk islkdrfgfs lyialfdkvs slgsgsdhvm
     1321 daisqceqya keqgaqerna pwrlffrkev ftpwhnpsed nvatnliyqq vvrgvkfgey
     1381 rcekeddlae lasqqyfvdy gsemilerll slvptyipdr eitplknlek waqlaiaahk
     1441 kgiyaqrrtd sqkvkedvvn yarfkwpllf srfyeaykfs gpplpksdvi vavnwtgvyf
     1501 vdeqeqvlle lsfpeimavs ssrgtkmmap sftlatikgd eytftssnae dirdlvvtfl
     1561 eglrkrskyv valqdnpnpa geesgflsfa kgdliildhd tgeqvmnsgw anginertkq
     1621 rgdfptdcvy vmptvtlppr eivalvtmtp dqrqdvvrll qlrtaepevr akpytleefs
     1681 ydyfrpppkh tlsrvmvska rgkdrlwsht replkqallk kilgseelsq eacmafvavl
     1741 kymgdypskr mrsvneltdq ifewalkaep lkdeayvqil kqltdnhiry seergwellw
     1801 lctglfppsn illphvqrfl qsrkhcplai dclqrlqkal rngsrkypph lveveaiqhk
     1861 ttqifhkvyf pddtdeafev esstkakdfc qniasrlllk ssegfslfvk iadkvisvpe
     1921 ndfffdfvrh ltdwikkarp ikdgivpslt yqvffmkklw tttvpgkdpm adsifhyyqe
     1981 lpkylrgyhk ctreevlqlg aliyrvkfee dksyfpsipk llrelvpqdl irqvspddwk
     2041 rsivayfnkh agkskeeakl aflklifkwp tfgsaffevk qttepnfpei lliainkygv
     2101 slidprtkdi ltthpftkis nwssgntyfh itignlvrgs kllcetslgy kmddlltsyi
     2161 sqmltamskq rnsrsgr
//
