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P97479 (MYO7A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional myosin-VIIa
Gene names
Name:Myo7a
Synonyms:Myo7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2215 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. In the retina, plays an important role in the renewal of the outer photoreceptor disks. Plays an important role in the distribution and migration of retinal pigment epithelial (RPE) melanosomes and phagosomes, and in the regulation of opsin transport in retinal photoreceptors. Mediates intracellular transport of RPE65 in the retina pigment epithelium. In the inner ear, plays an important role in differentiation, morphogenesis and organization of cochlear hair cell bundles. Motor protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing. Involved in hair-cell vesicle trafficking of aminoglycosides, which are known to induce ototoxicity. Ref.10 Ref.11

Subunit structure

Might homodimerize in a two headed molecule through the formation of a coiled-coil rod. May interact with CALM By similarity. Binds MYRIP and WHRN. Interacts with PLEKHB1 (via PH domain). Identified in a complex with USH1C and USH1G. Interacts with RPE65. Interacts with PCDH15. Interacts with TWF2. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12

Subcellular location

Cytoplasm. Cytoplasmcell cortex. Cytoplasmcytoskeleton. Note: In the photoreceptor cells, mainly localized in the inner and base of outer segments as well as in the synaptic ending region. Colocalizes with a subset of melanosomes in retinal pigment epithelium cells By similarity. Detected at the tip of cochlear hair cell stereocilia. The complex formed by MYO7A, USH1C and USH1G colocalizes with F-actin. Ref.11

Tissue specificity

Detected in mechanosensory stereocilia of cochlea hair cells (at protein level). Expressed in the retina, cochlea, kidney and liver. Ref.4 Ref.10 Ref.11

Developmental stage

In the inner ear of the 16.5 day old embryo, expressed only in the cochlear and vestibular sensory hair cells. In addition, expression also occurs in the epithelial cells of the small intestine, hepatocytes, and choroidal plexus.

Involvement in disease

Defects in Myo7a are the cause of the shaker-1 (sh-1) phenotype which affects only the inner ear. Sh-1 homozygote mutants show hyperactivity, head tossing and circling due to vestibular dysfunction, together with typical neuroepithelial-type cochlear defects involving dysfunction and progressive degeneration of the organ of Corti. Ref.1

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family.

Contains 2 FERM domains.

Contains 5 IQ domains.

Contains 1 myosin motor domain.

Contains 2 MyTH4 domains.

Contains 1 SH3 domain.

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-7 (MYH7).

Ontologies

Keywords
   Biological processHearing
Transport
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DiseaseDeafness
Disease mutation
   DomainCoiled coil
Repeat
SH3 domain
   LigandActin-binding
ATP-binding
Calmodulin-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament-based movement

Inferred from electronic annotation. Source: Ensembl

auditory receptor cell differentiation

Inferred from mutant phenotype PubMed 11753415PubMed 12121736PubMed 15389316. Source: MGI

auditory receptor cell stereocilium organization

Inferred from mutant phenotype PubMed 11753415PubMed 12121736PubMed 17050716. Source: MGI

cell projection organization

Inferred from mutant phenotype PubMed 9435277. Source: MGI

equilibrioception

Inferred from electronic annotation. Source: Ensembl

inner ear development

Inferred from mutant phenotype PubMed 13336002PubMed 14198707PubMed 6627025PubMed 9435277. Source: MGI

inner ear morphogenesis

Inferred from mutant phenotype PubMed 11753415PubMed 15389316PubMed 5795329. Source: MGI

inner ear receptor cell differentiation

Inferred from mutant phenotype PubMed 9435277Ref.2. Source: MGI

intracellular protein transport

Inferred from mutant phenotype PubMed 10414956. Source: MGI

lysosome organization

Inferred from sequence or structural similarity. Source: UniProtKB

mechanoreceptor differentiation

Inferred from mutant phenotype PubMed 17567809. Source: MGI

phagocytosis

Inferred from mutant phenotype PubMed 12743369. Source: MGI

phagolysosome assembly

Inferred from mutant phenotype PubMed 12743369. Source: MGI

pigment granule localization

Inferred from mutant phenotype PubMed 14609561PubMed 14978221PubMed 15572405. Source: MGI

pigment granule transport

Inferred from mutant phenotype PubMed 15572405PubMed 9620764. Source: MGI

post-embryonic organ morphogenesis

Inferred from mutant phenotype PubMed 13336002PubMed 14198707PubMed 6627025. Source: MGI

sensory perception

Inferred from mutant phenotype PubMed 11162241. Source: MGI

sensory perception of light stimulus

Inferred from mutant phenotype PubMed 14609561. Source: MGI

sensory perception of sound

Inferred from sequence or structural similarity. Source: UniProtKB

visual perception

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 9620764. Source: MGI

cell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 11023859PubMed 14978221PubMed 15572405PubMed 15590703PubMed 15905332PubMed 17666436PubMed 18796539PubMed 20016102PubMed 21146598. Source: MGI

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

lysosomal membrane

Inferred from sequence or structural similarity. Source: UniProtKB

melanosome

Inferred from direct assay PubMed 14978221PubMed 15572405. Source: MGI

microvillus

Inferred from sequence alignment PubMed 7568224. Source: MGI

myosin VII complex

Inferred from electronic annotation. Source: Ensembl

photoreceptor connecting cilium

Inferred from direct assay PubMed 10414956. Source: MGI

photoreceptor inner segment

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor outer segment

Inferred from sequence or structural similarity. Source: UniProtKB

stereocilium

Inferred from direct assay PubMed 12485990Ref.8PubMed 20016102. Source: MGI

synapse

Inferred from direct assay PubMed 11964381. Source: UniProtKB

   Molecular_functionADP binding

Inferred from electronic annotation. Source: Ensembl

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

actin-dependent ATPase activity

Inferred from electronic annotation. Source: Ensembl

calmodulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

microfilament motor activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.6Ref.7. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 17666436. Source: MGI

spectrin binding

Inferred from sequence orthology PubMed 23704327. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ush1gQ80T114EBI-1149557,EBI-7418889

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P97479-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P97479-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1523-1560: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22152215Unconventional myosin-VIIa
PRO_0000123467

Regions

Domain65 – 741677Myosin motor
Domain745 – 76521IQ 1
Domain768 – 78821IQ 2
Domain791 – 81121IQ 3
Domain814 – 83421IQ 4
Domain837 – 85721IQ 5
Domain1017 – 1253237MyTH4 1
Domain1258 – 1602345FERM 1
Domain1603 – 167270SH3
Domain1747 – 1896150MyTH4 2
Domain1902 – 2205304FERM 2
Nucleotide binding158 – 1658ATP Probable
Region632 – 6398Actin-binding Probable
Coiled coil858 – 93578 Potential

Natural variations

Alternative sequence1523 – 156038Missing in isoform 2.
VSP_042238
Natural variant2411R → P in sh-1.
Natural variant5021R → P in sh-1.

Experimental info

Mutagenesis11891A → E: Strongly reduced affinity for USH1G. Ref.12
Mutagenesis14731F → Q: Reduced affinity for USH1G. Ref.12
Sequence conflict851L → R in AAB40708. Ref.1
Sequence conflict2381E → S in AAB40708. Ref.1
Sequence conflict5891I → V in AAB40708. Ref.1
Sequence conflict6821V → G in AAB40708. Ref.1
Sequence conflict11561F → L in AAB40708. Ref.1

Secondary structure

............................................................................................ 2215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: D942FC7674B75EC7

FASTA2,215254,939
        10         20         30         40         50         60 
MVILQKGDYV WMDLKSGQEF DVPIGAVVKL CDSGQIQVVD DEDNEHWISP QNATHIKPMH 

        70         80         90        100        110        120 
PTSVHGVEDM IRLGDLNEAG ILRNLLIRYR DHLIYTYTGS ILVAVNPYQL LSIYSPEHIR 

       130        140        150        160        170        180 
QYTNKKIGEM PPHIFAIADN CYFNMKRNNR DQCCIISGES GAGKTESTKL ILQFLAAISG 

       190        200        210        220        230        240 
QHSWIEQQVL EATPILEAFG NAKTIRNDNS SRFGKYIDIH FNKRGAIEGA KIEQYLLEKS 

       250        260        270        280        290        300 
RVCRQAPDER NYHVFYCMLE GMNEEEKKKL GLGQAADYNY LAMGNCITCE GRVDSQEYAN 

       310        320        330        340        350        360 
IRSAMKVLMF TDTENWEISK LLAAILHMGN LQYEARTFEN LDACEVLFSP SLATAASLLE 

       370        380        390        400        410        420 
VNPPDLMSCL TSRTLITRGE TVSTPLSREQ ALDVRDAFVK GIYGRLFVWI VEKINAAIYK 

       430        440        450        460        470        480 
PPPLEVKNSR RSIGLLDIFG FENFTVNSFE QLCINFANEH LQQFFVRHVF KLEQEEYDLE 

       490        500        510        520        530        540 
SIDWLHIEFT DNQEALDMIA NRPMNVISLI DEESKFPKGT DATMLHKLNS QHKLNANYVP 

       550        560        570        580        590        600 
PKNSHETQFG INHFAGVVYY ESQGFLEKNR DTLHGDIIQL VHSSRNKFIK QIFQADVAMG 

       610        620        630        640        650        660 
AETRKRSPTL SSQFKRSLEL LMRTLGACQP FFVRCIKPNE FKKPMLFDRH LCVRQLRYSG 

       670        680        690        700        710        720 
MMETIRIRHA GYPIRYSFVE FVERYRVLLP GVKPAYKQGD LRGTCQRMAE AVLGTHDDWQ 

       730        740        750        760        770        780 
IGKTKIFLKD HHDMLLEVER DKAITDRVIL LQKVIRGFKD RSNFLRLKSA ATLIQRHWRG 

       790        800        810        820        830        840 
HHCRKNYELI RLGFLRLQAL HRSRKLHKQY RLARQRIIEF QARCRAYLVR KAFRHRLWAV 

       850        860        870        880        890        900 
ITVQAYARGM IARRLHRRLR VEYQRRLEAE RMRLAEEEKL RKEMSAKKAK EEAERKHQER 

       910        920        930        940        950        960 
LAQLAREDAE RELKEKEEAR RKKELLEQME KARHEPINHS DMVDKMFGFL GTSGSLPGQE 

       970        980        990       1000       1010       1020 
GQAPSGFEDL ERGRREMVEE DVDAALPLPD EDEEDLSEYK FAKFAATYFQ GTTTHSYTRR 

      1030       1040       1050       1060       1070       1080 
PLKQPLLYHD DEGDQLAALA VWITILRFMG DLPEPKYHTA MSDGSEKIPV MTKIYETLGK 

      1090       1100       1110       1120       1130       1140 
KTYKRELQAL QGEGETQLPE GQKKTSVRHK LVHLTLKKKS KLTEEVTKRL NDGESTVQGN 

      1150       1160       1170       1180       1190       1200 
SMLEDRPTSN LEKLHFIIGN GILRPALRDE IYCQISKQLT HNPSKSSYAR GWILVSLCVG 

      1210       1220       1230       1240       1250       1260 
CFAPSEKFVK YLRNFIHGGP PGYAPYCEER LRRTFVNGTR TQPPSWLELQ ATKSKKPIML 

      1270       1280       1290       1300       1310       1320 
PVTFMDGTTK TLLTDSATTA RELCNALADK ISLKDRFGFS LYIALFDKVS SLGSGSDHVM 

      1330       1340       1350       1360       1370       1380 
DAISQCEQYA KEQGAQERNA PWRLFFRKEV FTPWHNPSED NVATNLIYQQ VVRGVKFGEY 

      1390       1400       1410       1420       1430       1440 
RCEKEDDLAE LASQQYFVDY GSEMILERLL SLVPTYIPDR EITPLKNLEK WAQLAIAAHK 

      1450       1460       1470       1480       1490       1500 
KGIYAQRRTD SQKVKEDVVN YARFKWPLLF SRFYEAYKFS GPPLPKSDVI VAVNWTGVYF 

      1510       1520       1530       1540       1550       1560 
VDEQEQVLLE LSFPEIMAVS SSRECRVLLS LGCSDLGCAT CQSGRAGLTP AGPCSPCWSC 

      1570       1580       1590       1600       1610       1620 
RGTKMMAPSF TLATIKGDEY TFTSSNAEDI RDLVVTFLEG LRKRSKYVVA LQDNPNPAGE 

      1630       1640       1650       1660       1670       1680 
ESGFLSFAKG DLIILDHDTG EQVMNSGWAN GINERTKQRG DFPTDCVYVM PTVTLPPREI 

      1690       1700       1710       1720       1730       1740 
VALVTMTPDQ RQDVVRLLQL RTAEPEVRAK PYTLEEFSYD YFRPPPKHTL SRVMVSKARG 

      1750       1760       1770       1780       1790       1800 
KDRLWSHTRE PLKQALLKKI LGSEELSQEA CMAFVAVLKY MGDYPSKRMR SVNELTDQIF 

      1810       1820       1830       1840       1850       1860 
EWALKAEPLK DEAYVQILKQ LTDNHIRYSE ERGWELLWLC TGLFPPSNIL LPHVQRFLQS 

      1870       1880       1890       1900       1910       1920 
RKHCPLAIDC LQRLQKALRN GSRKYPPHLV EVEAIQHKTT QIFHKVYFPD DTDEAFEVES 

      1930       1940       1950       1960       1970       1980 
STKAKDFCQN IASRLLLKSS EGFSLFVKIA DKVISVPEND FFFDFVRHLT DWIKKARPIK 

      1990       2000       2010       2020       2030       2040 
DGIVPSLTYQ VFFMKKLWTT TVPGKDPMAD SIFHYYQELP KYLRGYHKCT REEVLQLGAL 

      2050       2060       2070       2080       2090       2100 
IYRVKFEEDK SYFPSIPKLL RELVPQDLIR QVSPDDWKRS IVAYFNKHAG KSKEEAKLAF 

      2110       2120       2130       2140       2150       2160 
LKLIFKWPTF GSAFFEVKQT TEPNFPEILL IAINKYGVSL IDPRTKDILT THPFTKISNW 

      2170       2180       2190       2200       2210 
SSGNTYFHIT IGNLVRGSKL LCETSLGYKM DDLLTSYISQ MLTAMSKQRN SRSGR 

« Hide

Isoform 2 [UniParc].

Checksum: B11BA144AE43B63D
Show »

FASTA2,177251,097

References

« Hide 'large scale' references
[1]"A type VII myosin encoded by the mouse deafness gene shaker-1."
Gibson F., Walsh J., Mburu P., Varela A., Brown K.A., Antonio M., Beisel K.W., Steel K.P., Brown S.D.M.
Nature 374:62-64(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DISEASE.
[2]"Mutation analysis of the mouse myosin VIIA deafness gene."
Mburu P., Liu X.-Z., Walsh J., Saw D. Jr., Cope M.J., Gibson F., Kendrick-Jones J., Steel K.P., Brown S.D.M.
Genes Funct. 1:191-203(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Myosin-XVa is required for tip localization of whirlin and differential elongation of hair-cell stereocilia."
Belyantseva I.A., Boger E.T., Naz S., Frolenkov G.I., Sellers J.R., Ahmed Z.M., Griffith A.J., Friedman T.B.
Nat. Cell Biol. 7:148-156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-2215 (ISOFORM 2), TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Inner ear.
[5]"Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin."
Fukuda M., Kuroda T.S.
J. Biol. Chem. 277:43096-43103(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYRIP.
[6]"Myosin XVa and whirlin, two deafness gene products required for hair bundle growth, are located at the stereocilia tips and interact directly."
Delprat B., Michel V., Goodyear R., Yamasaki Y., Michalski N., El-Amraoui A., Perfettini I., Legrain P., Richardson G., Hardelin J.-P., Petit C.
Hum. Mol. Genet. 14:401-410(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WHRN.
[7]"PHR1, an integral membrane protein of the inner ear sensory cells, directly interacts with myosin 1c and myosin VIIa."
Etournay R., El-Amraoui A., Bahloul A., Blanchard S., Roux I., Pezeron G., Michalski N., Daviet L., Hardelin J.-P., Legrain P., Petit C.
J. Cell Sci. 118:2891-2899(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLEKHB1.
[8]"Physical and functional interaction between protocadherin 15 and myosin VIIa in mechanosensory hair cells."
Senften M., Schwander M., Kazmierczak P., Lillo C., Shin J.B., Hasson T., Geleoc G.S., Gillespie P.G., Williams D., Holt J.R., Muller U.
J. Neurosci. 26:2060-2071(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCDH15.
[9]"MyosinVIIa interacts with Twinfilin-2 at the tips of mechanosensory stereocilia in the inner ear."
Rzadzinska A.K., Nevalainen E.M., Prosser H.M., Lappalainen P., Steel K.P.
PLoS ONE 4:E7097-E7097(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TWF2.
Strain: C3Heb/FeJ.
Tissue: Inner ear.
[10]"The Usher 1B protein, MYO7A, is required for normal localization and function of the visual retinoid cycle enzyme, RPE65."
Lopes V.S., Gibbs D., Libby R.T., Aleman T.S., Welch D.L., Lillo C., Jacobson S.G., Radu R.A., Steel K.P., Williams D.S.
Hum. Mol. Genet. 20:2560-2570(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RPE65.
[11]"Myosin VIIa and sans localization at stereocilia upper tip-link density implicates these Usher syndrome proteins in mechanotransduction."
Grati M., Kachar B.
Proc. Natl. Acad. Sci. U.S.A. 108:11476-11481(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[12]"Structure of MyTH4-FERM domains in myosin VIIa tail bound to cargo."
Wu L., Pan L., Wei Z., Zhang M.
Science 331:757-760(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 965-1687 IN COMPLEX WITH USH1G, INTERACTION WITH USH1G, MUTAGENESIS OF ALA-1189 AND PHE-1473.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U81453 mRNA. Translation: AAB40708.1.
AC115022 Genomic DNA. No translation available.
AC119880 Genomic DNA. No translation available.
AC157792 Genomic DNA. No translation available.
AY821853 mRNA. Translation: AAV87212.1.
CCDSCCDS40026.1. [P97479-2]
CCDS57565.1. [P97479-1]
PIRT30870.
RefSeqNP_001243010.1. NM_001256081.1. [P97479-1]
NP_001243012.1. NM_001256083.1.
NP_032689.2. NM_008663.2. [P97479-2]
UniGeneMm.1403.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PVLX-ray2.80A965-1687[»]
ProteinModelPortalP97479.
SMRP97479. Positions 993-1686.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97479. 2 interactions.
MINTMINT-1896820.

PTM databases

PhosphoSiteP97479.

Proteomic databases

MaxQBP97479.
PaxDbP97479.
PRIDEP97479.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000084979; ENSMUSP00000082046; ENSMUSG00000030761.
ENSMUST00000107127; ENSMUSP00000102744; ENSMUSG00000030761. [P97479-2]
ENSMUST00000107128; ENSMUSP00000102745; ENSMUSG00000030761. [P97479-1]
GeneID17921.
KEGGmmu:17921.
UCSCuc009ijy.2. mouse. [P97479-2]
uc009ijz.2. mouse. [P97479-1]

Organism-specific databases

CTD4647.
MGIMGI:104510. Myo7a.

Phylogenomic databases

eggNOGCOG5022.
GeneTreeENSGT00750000117545.
HOGENOMHOG000007836.
HOVERGENHBG052557.
KOK10359.
OMATPWHNPS.
OrthoDBEOG7QG433.
TreeFamTF335306.

Gene expression databases

ArrayExpressP97479.
BgeeP97479.
CleanExMM_MYO7A.
GenevestigatorP97479.

Family and domain databases

Gene3D1.20.80.10. 2 hits.
2.30.29.30. 1 hit.
InterProIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR000299. FERM_domain.
IPR000048. IQ_motif_EF-hand-BS.
IPR001609. Myosin_head_motor_dom.
IPR000857. MyTH4_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_like_dom.
IPR001452. SH3_domain.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF00612. IQ. 3 hits.
PF00063. Myosin_head. 1 hit.
PF00784. MyTH4. 2 hits.
[Graphical view]
PRINTSPR00193. MYOSINHEAVY.
SMARTSM00295. B41. 2 hits.
SM00015. IQ. 4 hits.
SM00242. MYSc. 1 hit.
SM00139. MyTH4. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 2 hits.
SSF50044. SSF50044. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54236. SSF54236. 2 hits.
PROSITEPS50057. FERM_3. 2 hits.
PS50096. IQ. 3 hits.
PS51456. MYOSIN_MOTOR. 1 hit.
PS51016. MYTH4. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMYO7A. mouse.
NextBio292781.
PROP97479.
SOURCESearch...

Entry information

Entry nameMYO7A_MOUSE
AccessionPrimary (citable) accession number: P97479
Secondary accession number(s): E9QLP7, Q5MJ57
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot