ID   MYO7A_PIG               Reviewed;         566 AA.
AC   Q28970; Q29064;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Unconventional myosin-VIIa;
DE   Flags: Fragment;
GN   Name=MYO7A;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney proximal tubule;
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 168-198.
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   [3]
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).
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. Motor protein that is a part of the functional network formed
CC       by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in
CC       cochlear hair cells. Required for normal hearing. Involved in hair-cell
CC       vesicle trafficking of aminoglycosides, which are known to induce
CC       ototoxicity (By similarity). {ECO:0000250}.
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 (By
CC       similarity). Interacts with RPE65 (By similarity). Interacts with CIB2
CC       (By similarity). May interact with CALM (By similarity). Interacts with
CC       WHRN (By similarity). Interacts with PLEKHB1 (via PH domain) (By
CC       similarity). Interacts with PCDH15 (By similarity). Interacts with TWF2
CC       (By similarity). Interacts with USH1G (By similarity). Interacts with
CC       MYH9 (By similarity). Interacts (via MyTH4-FERM domains) with
CC       cytoplasmic regions of ADGRV1 and USH2A. Interacts with PDZD7 (via
CC       MyTH4-FERM domains) (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P97479, ECO:0000250|UniProtKB:Q13402}.
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: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 (By similarity). The complex formed by MYO7A,
CC       USH1C and USH1G colocalizes with F-actin (By similarity).
CC       {ECO:0000250|UniProtKB:P97479, ECO:0000250|UniProtKB:Q13402}.
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}.
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DR   EMBL; U34226; AAC48476.1; -; mRNA.
DR   EMBL; L29133; AAA20918.1; -; mRNA.
DR   PIR; A59285; A59285.
DR   AlphaFoldDB; Q28970; -.
DR   SMR; Q28970; -.
DR   STRING; 9823.ENSSSCP00000015796; -.
DR   PaxDb; Q28970; -.
DR   PeptideAtlas; Q28970; -.
DR   PRIDE; Q28970; -.
DR   eggNOG; KOG4229; Eukaryota.
DR   InParanoid; Q28970; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
DR   GO; GO:0120044; C:stereocilium base; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0042490; P:mechanoreceptor differentiation; ISS:UniProtKB.
DR   GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR   CDD; cd01381; MYSc_Myo7; 1.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036106; MYSc_Myo7.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; ATP-binding; Cytoplasm; Cytoskeleton; Hearing;
KW   Motor protein; Myosin; Nucleotide-binding; Reference proteome; Synapse.
FT   CHAIN           1..>566
FT                   /note="Unconventional myosin-VIIa"
FT                   /id="PRO_0000123468"
FT   DOMAIN          67..>566
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT   BINDING         160..167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   NON_TER         566
SQ   SEQUENCE   566 AA;  64634 MW;  FD76C2D99CBAD240 CRC64;
     MVILQQGDYV WMDLRSGQEF DVPIGAVVKL CDSGQIQVVD DEGNEHWISP QNATHIKPMH
     PTSVTGMMED MIQHLGDLNE AGILRNLLIR YRDHLIYTYT GSILVAVNPY QLLSIYSPEH
     IRQYTNKKIG EMPPHIFAIA DNCYFNMKRN SRDQCCIISG ESGAGKTEST KLILQFLAAI
     SGQHSWIEQQ VLEATPILEA FGNAKTIRND NSSRFGKYID IHFNKRGAIE GARIEQYLLE
     KSRVCRQAPD ERNYHVFYCM LEGMSEEQKK KLGLGQATDY NYLAMGNCIT CEGREDSQEY
     ANIRSAMKVL MFTDTENWEI SKLLAAILHL GNLQYKDRTF ENLDACEVLF STALATAASL
     LEVNPPDLMN CLTSRTLITR GETVSTPLSR EQALDVRDAF VKGIYGRLFV WIVDKINAAI
     YKPPSQEVKN PRRSIGLLDI FGFENFAVNS FEQLCINFAN EHLQQFFVRH VFKLEQEEYD
     LESIDWLHIE FTDNQDALDM IANKPMNIIS LIDEESKFPK GTDTTMLHKL NSQHRLNSNY
     IPPKYNHETQ FGINHFAGVV YYESQG