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Q9V3Z6 (MYO7A_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin-VIIa

Short name=DmVIIa
Alternative name(s):
Protein crinkled
Gene names
Name:ck
ORF Names:CG7595
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length2167 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: can function in cells as a single-molecule cargo transporter. A very slow and high-duty-ratio motor, may be suitable for tension maintenance of actin filaments. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. Plays a key role in the formation of cellular projections and other actin-based functions required for embryonic and larval viability. Necessary for auditory transduction: plays a role in Johnston organ (JO) organization by functioning in scolopidial apical attachment and therefore to acoustic stimulus propagation from the antenna a2/a3 joint to transducing elements. Ref.1 Ref.5 Ref.6

Subunit structure

Homodimerizes in a two headed molecule through the formation of a coiled-coil rod. Homodimers motility is approximately 8-10 times slower than that of myosin V, and its step size is 30 nm, which is consistent with the presence of five IQ motifs in its neck region. Ref.6

Subcellular location

Cytoplasm. Note: In scolopale cells (radially organized units in the Johnston organ), protein is concentrated along actin-rich scolopale rods and more apically near scolopale cell-cap cell junctions. In neurons, protein is concentrated near the basal body where neurons are tethered to the scolopale cell. Ref.5

Tissue specificity

Expressed in the setae, micro- and macrochaetae on the head, thorax and wing. Ref.1

Developmental stage

Expressed both maternally and zygotically. Expression peaks in 12-18 hour embryos, and continues at a constant low level of expression through to adults. Ref.1

Disruption phenotype

Flies exhibit altered morphology of setae, micro- and macrochaetae on the head, thorax and wing. The number and distribution of setae on the thorax is altered, as is the morphology of the aristae. Mutants also exhibit scolopidial apical detachment and overall Johnston organ (JO) disorganization. Ref.1

Sequence similarities

Contains 2 FERM domains.

Contains 4 IQ domains.

Contains 1 myosin head-like domain.

Contains 2 MyTH4 domains.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainCoiled coil
Repeat
SH3 domain
   LigandActin-binding
ATP-binding
Nucleotide-binding
   Molecular functionMotor protein
Myosin
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 16415346Ref.6PubMed 19255446. Source: GOC

actin filament organization

Inferred from mutant phenotype PubMed 22219350. Source: FlyBase

actin filament-based movement

Inferred from direct assay Ref.6. Source: FlyBase

antennal development

Inferred from mutant phenotype PubMed 18461180. Source: FlyBase

antennal morphogenesis

Inferred from mutant phenotype PubMed 12070612. Source: FlyBase

chaeta morphogenesis

Inferred from mutant phenotype Ref.1. Source: FlyBase

chitin-based larval cuticle pattern formation

Inferred from genetic interaction PubMed 22219350. Source: FlyBase

imaginal disc-derived wing hair organization

Inferred from genetic interaction PubMed 11301004PubMed 15596016. Source: FlyBase

imaginal disc-derived wing vein morphogenesis

Inferred from genetic interaction PubMed 15596016. Source: FlyBase

metabolic process

Inferred from sequence or structural similarity PubMed 10908588. Source: GOC

sensory organ development

Inferred from mutant phenotype PubMed 18461180. Source: FlyBase

sensory perception of sound

Inferred from mutant phenotype Ref.5. Source: FlyBase

   Cellular_componentapical cortex

Inferred from direct assay PubMed 19270738. Source: FlyBase

cytoplasm

Inferred from direct assay Ref.5. Source: UniProtKB

microvillus

Inferred from direct assay PubMed 19270738. Source: FlyBase

myosin VII complex

Inferred from physical interaction PubMed 16917818. Source: FlyBase

myosin complex

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

unconventional myosin complex

Inferred from sequence or structural similarity PubMed 10471707PubMed 10908588. Source: FlyBase

   Molecular_functionATP binding

Inferred from direct assay PubMed 16415346Ref.6. Source: FlyBase

ATPase activity, coupled

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

actin binding

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

actin-dependent ATPase activity

Inferred from direct assay PubMed 16415346Ref.6PubMed 19255446. Source: FlyBase

motor activity

Inferred from sequence or structural similarity PubMed 10908588. Source: FlyBase

myosin light chain binding

Inferred from physical interaction PubMed 16917818. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 21672167Myosin-VIIa
PRO_0000306376

Regions

Domain65 – 721657Myosin head-like
Domain736 – 75823IQ 1
Domain759 – 78830IQ 2
Domain805 – 82723IQ 3
Domain828 – 85730IQ 4
Domain1008 – 1245238MyTH4 1
Domain1250 – 1560311FERM 1
Domain1558 – 162770SH3
Domain1701 – 1849149MyTH4 2
Domain1855 – 2158304FERM 2
Nucleotide binding156 – 1638ATP By similarity UniProtKB P08799
Region612 – 63423Actin-binding By similarity UniProtKB P08799
Region712 – 72615Actin-binding By similarity UniProtKB P08799
Coiled coil886 – 91934 Potential

Amino acid modifications

Modified residue16511Phosphoserine Ref.7
Modified residue16541Phosphoserine Ref.7
Modified residue20451Phosphothreonine Ref.7

Experimental info

Sequence conflict20241I → M in AAR96124. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9V3Z6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 3C57E34ADDD89A42

FASTA2,167250,309
        10         20         30         40         50         60 
MVIVTRGDYI WIEPASGREF DVAIGARVVS AEGRRIQVRD DDGDEVWLAP ERRIKAMHAS 

        70         80         90        100        110        120 
SVQGVEDMIS LGDLHEAGIL RNLLIRYKEN LIYTYTGSIL VAVNPYQILP IYTGDQIKLY 

       130        140        150        160        170        180 
KERKIGELPP HIFAIGDNAY AHMKRYRQDQ CIVISGESGA GKTESTKLIL QYLAAISGKH 

       190        200        210        220        230        240 
SWIEQQILEA NPILEAFGNA KTIRNDNSSR FGKYIDIHFS ANGVIEGAKI EQYLLEKSRI 

       250        260        270        280        290        300 
VSQNHSERNY HVFYCILAGL SADEKSRLDL GMAADYKYLT GGNSITCEGR DDAAEFSDIR 

       310        320        330        340        350        360 
SAMKVLLFSD QEIWEIIKLL AALLHCGNIK YKATVVDNLD ATEIPEHINV ERVAGLLGLP 

       370        380        390        400        410        420 
IQPLIDALTR RTLFAHGETV VSTLSRDQSV DVRDAFVKGI YGRMFVHIVR KINTAIFKPR 

       430        440        450        460        470        480 
GTSRNAIGVL DIFGFENFDQ NSFEQFCINY ANENLQQFFV QHIFKLEQEE YNHEAINWQH 

       490        500        510        520        530        540 
IEFVDNQDAL DLIAIKQLNI MALIDEEARF PKGTDQTMLA KLHKTHGSHK NYLKPKSDIN 

       550        560        570        580        590        600 
TSFGLNHFAG VVFYDTRGFL DKNRDTFSPD LLHLVSQSTN KFLRQIFAQD IEMGAETRKR 

       610        620        630        640        650        660 
TPTLSTQFRK SLDALMKTLS SCQPFFIRCI KPNELKKPMM FDRGLCCRQL RYSGMMETIR 

       670        680        690        700        710        720 
IRRAGYPIRH GFREFVERYR FLIPGVPPAH RTDCQAATSR ICAVVLGKSD YQLGHTKVFL 

       730        740        750        760        770        780 
KDAHDLFLEQ ERDRVLTRKI LILQRSIRGW VYRRRFLRLR AAAITVQRFW KGYAQRKRYR 

       790        800        810        820        830        840 
NMRVGYMRLQ ALIRSRVLSH RFRHLRGHIV GLQAHARGYL VRREYGHKMW AVIKIQSHVR 

       850        860        870        880        890        900 
RMIAMRRYRK LRLEHKQFAE VLQLRKLEEQ ELLHRGNKHA REIAEQHYRD RLHELERREI 

       910        920        930        940        950        960 
QEQLENRRRV EVNMNIINDA ARKQEEPVDD GKLVEAMFDF LPDSSSDAPT PHGGRETSVF 

       970        980        990       1000       1010       1020 
NDLPHAQNVN QDDIIAPIHI SEDEEDLSEF KFQKFAATYF QGNVNHQYAK KALKHPLLPL 

      1030       1040       1050       1060       1070       1080 
HTQGDQLAAQ ALWITILRFT GDMPEPKYHT MDRMDTTSVM SKVTATLGRN FIRSKEFQEA 

      1090       1100       1110       1120       1130       1140 
QLMGLDPDAF LKQKPRSIRH KLVSLTLKRK NKLGEDVRRR LQDDEYTADS YQSWLQSRPT 

      1150       1160       1170       1180       1190       1200 
SNLEKLHFII GHGILRAELR DEIYCQICKQ LTNNPLKSSH ARGWILLSLC VGCFAPSEKF 

      1210       1220       1230       1240       1250       1260 
VNYLRAFIRE GPPGYAPYCE ERLKRTFNNG TRNQPPSWLE LQATKSKKPI MLPITFMDGN 

      1270       1280       1290       1300       1310       1320 
TKTLLADSAT TARELCNQLS DKISLKDQFG FSLYIALFDK VSSLGSGGDH VMDAISQCEQ 

      1330       1340       1350       1360       1370       1380 
YAKEQGAQER NAPWRLFFRK EIFAPWHEPT HDQVATNLIY QQVVRGVKFG EYRCDKEEDL 

      1390       1400       1410       1420       1430       1440 
AMIAAQQYFI EYSTDMSMER LFTLLPNFIP DFCLSGVDKA IERWAALVLQ AYKKSYYVKD 

      1450       1460       1470       1480       1490       1500 
KIAPLKIKED IVSYAKYKWP LLFSRFYEAY RNSGPNLPKN DVIIAVNWTG VYVVDDQEQV 

      1510       1520       1530       1540       1550       1560 
LLELSFPEIT AVSSQKTNKV FTQTFSLSTV RGEEFTFQSP NAEDIRDLVV YFLDGLKKRS 

      1570       1580       1590       1600       1610       1620 
KYVIALQDYR APSDGTSFLS FFKGDLIILE DESCGESVLN NGWCIGRCDR SQERGDFPAE 

      1630       1640       1650       1660       1670       1680 
TVYVLPTLSK PPQDILALFN IEEAHHGRRL SMASNGGAVE PRDRPHTLME YALDHFRLPP 

      1690       1700       1710       1720       1730       1740 
KRTMSKTLTL SSKRSEELWR YSRDPIKAPL LRKLQSKEEF AEEACFAFAA ILKYMGDLPS 

      1750       1760       1770       1780       1790       1800 
KRPRMGNEIT DHIFDGPLKH EILRDEIYCQ LMKQLTDNRN RMSEERGWEL MWLATGLFAC 

      1810       1820       1830       1840       1850       1860 
SQGLLKELLL FLRTRRHPIS QDSMHRLQKT IRHGQRKYPP HQVEVEAIQH KTTQIFHKVY 

      1870       1880       1890       1900       1910       1920 
FPDDTDEAFE VDSSTRAKDF CNNISQRLSL RTSEGFSLFV KIADKVISVP EGDFFFDFVR 

      1930       1940       1950       1960       1970       1980 
HLTDWIKKAR PIRDGANPQF TYQVFFMKKL WTNTVPGKDR NADLIFHYHQ ELPKLLRGYH 

      1990       2000       2010       2020       2030       2040 
KCSREEAAKL AALVFRVRFG ENKQELQAIP QMLRELIPSD IMKIQSTSEW KRSIVASYNQ 

      2050       2060       2070       2080       2090       2100 
DGGMTSEDAK VAFLKIVYRW PTFGSAFFEV KQTTEPNYPE MLLIAINKHG VSLIHPVTKD 

      2110       2120       2130       2140       2150       2160 
ILVTHPFTRI SNWSSGNTYF HMTIGNLVRG SKLLCETSLG YKMDDLLTSY ISLMLTNMNK 


NRTIRAN 

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References

« Hide 'large scale' references
[1]"Drosophila crinkled, mutations of which disrupt morphogenesis and cause lethality, encodes fly myosin VIIA."
Kiehart D.P., Franke J.D., Chee M.K., Montague R.A., Chen T.-L., Roote J., Ashburner M.
Genetics 168:1337-1352(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
Strain: Berkeley.
Tissue: Embryo.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Myosin VIIA defects, which underlie the Usher 1B syndrome in humans, lead to deafness in Drosophila."
Todi S.V., Franke J.D., Kiehart D.P., Eberl D.F.
Curr. Biol. 15:862-868(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Dimerized Drosophila myosin VIIa: a processive motor."
Yang Y., Kovacs M., Sakamoto T., Zhang F., Kiehart D.P., Sellers J.R.
Proc. Natl. Acad. Sci. U.S.A. 103:5746-5751(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[7]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1651; SER-1654 AND THR-2045, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014134 Genomic DNA. Translation: AAF53435.1.
AE014134 Genomic DNA. Translation: AAN10886.1.
AY069438 mRNA. Translation: AAL39583.2.
BT011332 mRNA. Translation: AAR96124.1.
RefSeqNP_523571.1. NM_078847.3.
NP_723895.1. NM_165099.2.
UniGeneDm.2128.

3D structure databases

ProteinModelPortalQ9V3Z6.
SMRQ9V3Z6. Positions 2-730, 984-1641, 1662-2157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60900. 4 interactions.
DIPDIP-48747N.

Proteomic databases

PaxDbQ9V3Z6.
PRIDEQ9V3Z6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080723; FBpp0080282; FBgn0000317.
FBtr0080724; FBpp0080283; FBgn0000317.
GeneID34882.
KEGGdme:Dmel_CG7595.

Organism-specific databases

CTD34882.
FlyBaseFBgn0000317. ck.

Phylogenomic databases

eggNOGCOG5022.
GeneTreeENSGT00750000117545.
InParanoidQ9V3Z6.
KOK10359.
OMATPWHNPS.
OrthoDBEOG7QG433.
PhylomeDBQ9V3Z6.

Gene expression databases

BgeeQ9V3Z6.

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.
IPR018979. FERM_N.
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.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00612. IQ. 4 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.
PROSITEPS50057. FERM_3. 2 hits.
PS50096. IQ. 4 hits.
PS51016. MYTH4. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi34882.
NextBio790677.
PROQ9V3Z6.

Entry information

Entry nameMYO7A_DROME
AccessionPrimary (citable) accession number: Q9V3Z6
Secondary accession number(s): Q6NNF6, Q8T0A9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase