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Protein

Unconventional myosin-VIIa

Gene

Myo7a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.2 Publications

Caution

Represents an unconventional myosin. This protein should not be confused with the conventional myosin-7 (MYH7).Curated
Originally predicted to contain a coiled coil domain but proposed to contain a stable SAH domain instead.Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi158 – 165ATPCurated8

GO - Molecular functioni

GO - Biological processi

  • actin filament-based movement Source: MGI
  • auditory receptor cell stereocilium organization Source: MGI
  • cell projection organization Source: MGI
  • equilibrioception Source: MGI
  • inner ear auditory receptor cell differentiation Source: MGI
  • inner ear development Source: MGI
  • inner ear morphogenesis Source: MGI
  • inner ear receptor cell differentiation Source: MGI
  • inner ear receptor cell stereocilium organization Source: MGI
  • intracellular protein transport Source: MGI
  • lysosome organization Source: UniProtKB
  • mechanoreceptor differentiation Source: MGI
  • microtubule-based movement Source: InterPro
  • phagocytosis Source: MGI
  • phagolysosome assembly Source: MGI
  • pigment granule localization Source: MGI
  • pigment granule transport Source: MGI
  • post-embryonic animal organ morphogenesis Source: MGI
  • sensory perception Source: MGI
  • sensory perception of light stimulus Source: MGI
  • sensory perception of sound Source: MGI
  • visual perception Source: MGI

Keywordsi

Molecular functionActin-binding, Calmodulin-binding, Motor protein, Myosin
Biological processHearing, Transport
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2453902 The canonical retinoid cycle in rods (twilight vision)

Names & Taxonomyi

Protein namesi
Recommended name:
Unconventional myosin-VIIa
Gene namesi
Name:Myo7a
Synonyms:Myo7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:104510 Myo7a

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

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.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1189A → E: Strongly reduced affinity for USH1G. 1 Publication1
Mutagenesisi1473F → Q: Reduced affinity for USH1G. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001234671 – 2215Unconventional myosin-VIIaAdd BLAST2215

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1563PhosphothreonineCombined sources1
Modified residuei1569PhosphoserineCombined sources1
Modified residuei1571PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP97479
PaxDbiP97479
PeptideAtlasiP97479
PRIDEiP97479

PTM databases

iPTMnetiP97479
PhosphoSitePlusiP97479

Expressioni

Tissue specificityi

Detected in mechanosensory stereocilia of cochlea hair cells (at protein level). Expressed in the retina, cochlea, kidney and liver.3 Publications

Developmental stagei

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.

Gene expression databases

BgeeiENSMUSG00000030761
CleanExiMM_MYO7A
ExpressionAtlasiP97479 baseline and differential
GenevisibleiP97479 MM

Interactioni

Subunit structurei

Might homodimerize in a two headed molecule through the formation of a coiled-coil rod (By similarity). Identified in a complex with USH1C and USH1G (By similarity). Interacts with MYRIP (PubMed:12221080). Interacts with RPE65 (PubMed:21493626). Interacts with CIB2 (By similarity). May interact with CALM (By similarity). Interacts with WHRN (PubMed:15590698). Interacts with PLEKHB1 (via PH domain) (PubMed:15976448). Interacts with PCDH15 (PubMed:16481439). Interacts with TWF2 (PubMed:19774077). Interacts with USH1G (PubMed:21311020). Interacts with Myh9 (PubMed:27331610).By similarity8 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201669, 5 interactors
IntActiP97479, 5 interactors
MINTiP97479
STRINGi10090.ENSMUSP00000102745

Structurei

Secondary structure

12215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi828 – 853Combined sources26
Helixi866 – 929Combined sources64
Helixi1001 – 1008Combined sources8
Helixi1032 – 1048Combined sources17
Helixi1070 – 1075Combined sources6
Turni1076 – 1079Combined sources4
Helixi1084 – 1088Combined sources5
Helixi1150 – 1163Combined sources14
Helixi1165 – 1167Combined sources3
Helixi1168 – 1178Combined sources11
Helixi1185 – 1201Combined sources17
Turni1206 – 1208Combined sources3
Helixi1209 – 1217Combined sources9
Turni1221 – 1223Combined sources3
Helixi1224 – 1237Combined sources14
Helixi1246 – 1254Combined sources9
Beta strandi1258 – 1264Combined sources7
Beta strandi1269 – 1274Combined sources6
Helixi1280 – 1290Combined sources11
Beta strandi1299 – 1305Combined sources7
Beta strandi1308 – 1313Combined sources6
Helixi1319 – 1331Combined sources13
Turni1332 – 1334Combined sources3
Helixi1337 – 1339Combined sources3
Beta strandi1343 – 1348Combined sources6
Helixi1357 – 1359Combined sources3
Helixi1361 – 1376Combined sources16
Helixi1385 – 1400Combined sources16
Helixi1406 – 1416Combined sources11
Helixi1419 – 1421Combined sources3
Beta strandi1424 – 1426Combined sources3
Helixi1428 – 1444Combined sources17
Helixi1451 – 1465Combined sources15
Turni1467 – 1469Combined sources3
Beta strandi1472 – 1482Combined sources11
Beta strandi1487 – 1494Combined sources8
Beta strandi1497 – 1501Combined sources5
Beta strandi1507 – 1512Combined sources6
Helixi1513 – 1515Combined sources3
Beta strandi1516 – 1522Combined sources7
Beta strandi1564 – 1566Combined sources3
Beta strandi1569 – 1574Combined sources6
Beta strandi1579 – 1583Combined sources5
Helixi1587 – 1604Combined sources18
Beta strandi1607 – 1612Combined sources6
Beta strandi1632 – 1634Combined sources3
Helixi1640 – 1645Combined sources6
Beta strandi1646 – 1653Combined sources8
Turni1654 – 1656Combined sources3
Beta strandi1659 – 1663Combined sources5
Helixi1664 – 1666Combined sources3
Beta strandi1667 – 1669Combined sources3
Helixi1678 – 1684Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3PVLX-ray2.80A965-1687[»]
5WSTX-ray2.10A/B866-932[»]
5WSUX-ray3.00C/D834-935[»]
5WSVX-ray2.33B/D828-870[»]
ProteinModelPortaliP97479
SMRiP97479
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini65 – 741Myosin motorPROSITE-ProRule annotationAdd BLAST677
Domaini745 – 765IQ 1PROSITE-ProRule annotationAdd BLAST21
Domaini768 – 788IQ 2PROSITE-ProRule annotationAdd BLAST21
Domaini791 – 811IQ 3PROSITE-ProRule annotationAdd BLAST21
Domaini814 – 834IQ 4PROSITE-ProRule annotationAdd BLAST21
Domaini837 – 857IQ 5PROSITE-ProRule annotationAdd BLAST21
Domaini1017 – 1253MyTH4 1PROSITE-ProRule annotationAdd BLAST237
Domaini1258 – 1602FERM 1PROSITE-ProRule annotationAdd BLAST345
Domaini1603 – 1672SH3PROSITE-ProRule annotationAdd BLAST70
Domaini1747 – 1896MyTH4 2PROSITE-ProRule annotationAdd BLAST150
Domaini1902 – 2205FERM 2PROSITE-ProRule annotationAdd BLAST304

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni632 – 639Actin-bindingCurated8
Regioni858 – 935SAHBy similarityAdd BLAST78

Domaini

The SAH (single alpha-helix) region is characterized by a high content of charged residues which are predicted to stabilize the alpha-helical structure by ionic bonds.By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG4229 Eukaryota
COG5022 LUCA
GeneTreeiENSGT00900000140810
HOGENOMiHOG000007836
HOVERGENiHBG052557
InParanoidiP97479
KOiK10359
OMAiTPWHNPS
OrthoDBiEOG091G00BB
TreeFamiTF335306

Family and domain databases

CDDicd14473 FERM_B-lobe, 2 hits
cd01381 MYSc_Myo7, 1 hit
Gene3Di1.20.80.10, 2 hits
1.25.40.530, 1 hit
2.30.29.30, 3 hits
2.30.30.360, 1 hit
3.40.850.10, 3 hits
InterProiView protein in InterPro
IPR019749 Band_41_domain
IPR014352 FERM/acyl-CoA-bd_prot_sf
IPR035963 FERM_2
IPR019748 FERM_central
IPR000299 FERM_domain
IPR000048 IQ_motif_EF-hand-BS
IPR036961 Kinesin_motor_dom_sf
IPR001609 Myosin_head_motor_dom
IPR008989 Myosin_S1_N
IPR036106 MYSc_Myo7
IPR000857 MyTH4_dom
IPR038185 MyTH4_dom_sf
IPR027417 P-loop_NTPase
IPR011993 PH-like_dom_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR029071 Ubiquitin-like_domsf
PfamiView protein in Pfam
PF00373 FERM_M, 1 hit
PF00612 IQ, 3 hits
PF00063 Myosin_head, 1 hit
PF00784 MyTH4, 2 hits
PRINTSiPR00193 MYOSINHEAVY
SMARTiView protein in SMART
SM00295 B41, 2 hits
SM00015 IQ, 4 hits
SM00242 MYSc, 1 hit
SM00139 MyTH4, 2 hits
SM00326 SH3, 1 hit
SUPFAMiSSF47031 SSF47031, 2 hits
SSF50044 SSF50044, 1 hit
SSF52540 SSF52540, 2 hits
SSF54236 SSF54236, 2 hits
PROSITEiView protein in PROSITE
PS50057 FERM_3, 2 hits
PS50096 IQ, 3 hits
PS51456 MYOSIN_MOTOR, 1 hit
PS51016 MYTH4, 2 hits
PS50002 SH3, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P97479-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVILQKGDYV WMDLKSGQEF DVPIGAVVKL CDSGQIQVVD DEDNEHWISP
60 70 80 90 100
QNATHIKPMH PTSVHGVEDM IRLGDLNEAG ILRNLLIRYR DHLIYTYTGS
110 120 130 140 150
ILVAVNPYQL LSIYSPEHIR QYTNKKIGEM PPHIFAIADN CYFNMKRNNR
160 170 180 190 200
DQCCIISGES GAGKTESTKL ILQFLAAISG QHSWIEQQVL EATPILEAFG
210 220 230 240 250
NAKTIRNDNS SRFGKYIDIH FNKRGAIEGA KIEQYLLEKS RVCRQAPDER
260 270 280 290 300
NYHVFYCMLE GMNEEEKKKL GLGQAADYNY LAMGNCITCE GRVDSQEYAN
310 320 330 340 350
IRSAMKVLMF TDTENWEISK LLAAILHMGN LQYEARTFEN LDACEVLFSP
360 370 380 390 400
SLATAASLLE VNPPDLMSCL TSRTLITRGE TVSTPLSREQ ALDVRDAFVK
410 420 430 440 450
GIYGRLFVWI VEKINAAIYK PPPLEVKNSR RSIGLLDIFG FENFTVNSFE
460 470 480 490 500
QLCINFANEH LQQFFVRHVF KLEQEEYDLE SIDWLHIEFT DNQEALDMIA
510 520 530 540 550
NRPMNVISLI DEESKFPKGT DATMLHKLNS QHKLNANYVP PKNSHETQFG
560 570 580 590 600
INHFAGVVYY ESQGFLEKNR DTLHGDIIQL VHSSRNKFIK QIFQADVAMG
610 620 630 640 650
AETRKRSPTL SSQFKRSLEL LMRTLGACQP FFVRCIKPNE FKKPMLFDRH
660 670 680 690 700
LCVRQLRYSG MMETIRIRHA GYPIRYSFVE FVERYRVLLP GVKPAYKQGD
710 720 730 740 750
LRGTCQRMAE AVLGTHDDWQ IGKTKIFLKD HHDMLLEVER DKAITDRVIL
760 770 780 790 800
LQKVIRGFKD RSNFLRLKSA ATLIQRHWRG HHCRKNYELI RLGFLRLQAL
810 820 830 840 850
HRSRKLHKQY RLARQRIIEF QARCRAYLVR KAFRHRLWAV ITVQAYARGM
860 870 880 890 900
IARRLHRRLR VEYQRRLEAE RMRLAEEEKL RKEMSAKKAK EEAERKHQER
910 920 930 940 950
LAQLAREDAE RELKEKEEAR RKKELLEQME KARHEPINHS DMVDKMFGFL
960 970 980 990 1000
GTSGSLPGQE GQAPSGFEDL ERGRREMVEE DVDAALPLPD EDEEDLSEYK
1010 1020 1030 1040 1050
FAKFAATYFQ GTTTHSYTRR PLKQPLLYHD DEGDQLAALA VWITILRFMG
1060 1070 1080 1090 1100
DLPEPKYHTA MSDGSEKIPV MTKIYETLGK KTYKRELQAL QGEGETQLPE
1110 1120 1130 1140 1150
GQKKTSVRHK LVHLTLKKKS KLTEEVTKRL NDGESTVQGN SMLEDRPTSN
1160 1170 1180 1190 1200
LEKLHFIIGN GILRPALRDE IYCQISKQLT HNPSKSSYAR GWILVSLCVG
1210 1220 1230 1240 1250
CFAPSEKFVK YLRNFIHGGP PGYAPYCEER LRRTFVNGTR TQPPSWLELQ
1260 1270 1280 1290 1300
ATKSKKPIML PVTFMDGTTK TLLTDSATTA RELCNALADK ISLKDRFGFS
1310 1320 1330 1340 1350
LYIALFDKVS SLGSGSDHVM DAISQCEQYA KEQGAQERNA PWRLFFRKEV
1360 1370 1380 1390 1400
FTPWHNPSED NVATNLIYQQ VVRGVKFGEY RCEKEDDLAE LASQQYFVDY
1410 1420 1430 1440 1450
GSEMILERLL SLVPTYIPDR EITPLKNLEK WAQLAIAAHK KGIYAQRRTD
1460 1470 1480 1490 1500
SQKVKEDVVN YARFKWPLLF SRFYEAYKFS GPPLPKSDVI VAVNWTGVYF
1510 1520 1530 1540 1550
VDEQEQVLLE LSFPEIMAVS SSRECRVLLS LGCSDLGCAT CQSGRAGLTP
1560 1570 1580 1590 1600
AGPCSPCWSC RGTKMMAPSF TLATIKGDEY TFTSSNAEDI RDLVVTFLEG
1610 1620 1630 1640 1650
LRKRSKYVVA LQDNPNPAGE ESGFLSFAKG DLIILDHDTG EQVMNSGWAN
1660 1670 1680 1690 1700
GINERTKQRG DFPTDCVYVM PTVTLPPREI VALVTMTPDQ RQDVVRLLQL
1710 1720 1730 1740 1750
RTAEPEVRAK PYTLEEFSYD YFRPPPKHTL SRVMVSKARG KDRLWSHTRE
1760 1770 1780 1790 1800
PLKQALLKKI LGSEELSQEA CMAFVAVLKY MGDYPSKRMR SVNELTDQIF
1810 1820 1830 1840 1850
EWALKAEPLK DEAYVQILKQ LTDNHIRYSE ERGWELLWLC TGLFPPSNIL
1860 1870 1880 1890 1900
LPHVQRFLQS RKHCPLAIDC LQRLQKALRN GSRKYPPHLV EVEAIQHKTT
1910 1920 1930 1940 1950
QIFHKVYFPD DTDEAFEVES STKAKDFCQN IASRLLLKSS EGFSLFVKIA
1960 1970 1980 1990 2000
DKVISVPEND FFFDFVRHLT DWIKKARPIK DGIVPSLTYQ VFFMKKLWTT
2010 2020 2030 2040 2050
TVPGKDPMAD SIFHYYQELP KYLRGYHKCT REEVLQLGAL IYRVKFEEDK
2060 2070 2080 2090 2100
SYFPSIPKLL RELVPQDLIR QVSPDDWKRS IVAYFNKHAG KSKEEAKLAF
2110 2120 2130 2140 2150
LKLIFKWPTF GSAFFEVKQT TEPNFPEILL IAINKYGVSL IDPRTKDILT
2160 2170 2180 2190 2200
THPFTKISNW SSGNTYFHIT IGNLVRGSKL LCETSLGYKM DDLLTSYISQ
2210
MLTAMSKQRN SRSGR
Length:2,215
Mass (Da):254,939
Last modified:July 27, 2011 - v2
Checksum:iD942FC7674B75EC7
GO
Isoform 2 (identifier: P97479-2) [UniParc]FASTAAdd to basket

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

Show »
Length:2,177
Mass (Da):251,097
Checksum:iB11BA144AE43B63D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti85L → R in AAB40708 (PubMed:7870172).Curated1
Sequence conflicti238E → S in AAB40708 (PubMed:7870172).Curated1
Sequence conflicti589I → V in AAB40708 (PubMed:7870172).Curated1
Sequence conflicti682V → G in AAB40708 (PubMed:7870172).Curated1
Sequence conflicti1156F → L in AAB40708 (PubMed:7870172).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti241R → P in sh-1. 1
Natural varianti502R → P in sh-1. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0422381523 – 1560Missing in isoform 2. 1 PublicationAdd BLAST38

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS40026.1 [P97479-2]
CCDS57565.1 [P97479-1]
PIRiT30870
RefSeqiNP_001243010.1, NM_001256081.1 [P97479-1]
NP_001243012.1, NM_001256083.1
NP_032689.2, NM_008663.2 [P97479-2]
XP_011239993.1, XM_011241691.1
UniGeneiMm.1403

Genome annotation databases

EnsembliENSMUST00000107127; ENSMUSP00000102744; ENSMUSG00000030761 [P97479-2]
ENSMUST00000107128; ENSMUSP00000102745; ENSMUSG00000030761 [P97479-1]
GeneIDi17921
KEGGimmu:17921
UCSCiuc009ijy.2 mouse [P97479-2]
uc009ijz.2 mouse [P97479-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiMYO7A_MOUSE
AccessioniPrimary (citable) accession number: P97479
Secondary accession number(s): E9QLP7, Q5MJ57
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: May 23, 2018
This is version 174 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health