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Protein

Myosin-VIIa

Gene

ck

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Myosins are actin-based motor molecules with ATPase activity (PubMed:16585515). Unconventional myosins serve in intracellular movements: can function in cells as a single-molecule cargo transporter (PubMed:16585515). A very slow and high-duty-ratio motor, may be suitable for tension maintenance of actin filaments (PubMed:16585515). Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (PubMed:15579689). Plays a key role in the formation of cellular projections and other actin-based functions required for embryonic and larval viability (PubMed:15579689, PubMed:16585515). Necessary for auditory transduction: plays a role in Johnston's organ organization by functioning in scolopidial apical attachment and therefore to acoustic stimulus propagation from the antenna a2/a3 joint to transducing elements (PubMed:15886106, PubMed:27331610). Interaction with the myosin zip may be important for its function in scolopidial apical attachment (PubMed:27331610). During oogenesis it has Cad99c-dependent and Cad99c-independent roles in regulating the shape and spacing of the follicle cell microvilli which secrete eggshell material such as the vitelline membrane (PubMed:25236597). May be required for the normal expression of Cad99c in the follicle cell microvilli (PubMed:25236597).5 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi156 – 163ATPBy similarity8

GO - Molecular functioni

  • actin binding Source: FlyBase
  • actin-dependent ATPase activity Source: FlyBase
  • actin filament binding Source: InterPro
  • ATPase activity, coupled Source: FlyBase
  • ATP binding Source: FlyBase
  • cadherin binding Source: FlyBase
  • microtubule binding Source: InterPro
  • microtubule motor activity Source: InterPro
  • motor activity Source: FlyBase
  • myosin light chain binding Source: FlyBase

GO - Biological processi

  • actin filament-based movement Source: FlyBase
  • actin filament organization Source: FlyBase
  • antennal development Source: FlyBase
  • antennal morphogenesis Source: FlyBase
  • chaeta morphogenesis Source: FlyBase
  • chitin-based larval cuticle pattern formation Source: FlyBase
  • follicle cell microvillus organization Source: FlyBase
  • imaginal disc-derived wing hair organization Source: FlyBase
  • imaginal disc-derived wing vein morphogenesis Source: FlyBase
  • microtubule-based movement Source: InterPro
  • sensory organ development Source: FlyBase
  • sensory perception of sound Source: FlyBase

Keywordsi

Molecular functionActin-binding, Motor protein, Myosin
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Myosin-VIIa
Short name:
DmVIIa
Alternative name(s):
Protein crinkled
Gene namesi
Name:ckImported
ORF Names:CG7595
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000317 ck

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

Cell projection, Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Flies exhibit altered morphology of setae, micro- and macrochaetae on the head, thorax and wing (PubMed:15579689). The number and distribution of setae on the thorax is altered, as is the morphology of the aristae (PubMed:15579689). Mutants also exhibit scolopidial apical detachment and overall Johnston's organ (JO) disorganization (PubMed:15579689). RNAi-mediated knockdown in Johnston's organs, disrupts the filamentous structure of the glycoprotein NompA at the apical junction (PubMed:27331610). NompA occurs as puncta and scolopidia detatch from the hinge of the second and third antennal segment (PubMed:27331610).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003063761 – 2167Myosin-VIIaAdd BLAST2167

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1651Phosphoserine1 Publication1
Modified residuei1654Phosphoserine1 Publication1
Modified residuei2045Phosphothreonine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9V3Z6
PRIDEiQ9V3Z6

PTM databases

iPTMnetiQ9V3Z6

Expressioni

Tissue specificityi

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

Developmental stagei

Throughout oogenesis expressed in the germline and associated somatic cells (at protein level) (PubMed:25236597). In germline cells of the germarium, expression levels peak during follicle formation and again from mid-oogenesis until late oogenesis (at protein level). Expressed both maternally and zygotically (PubMed:15579689). Expression peaks in 12-18 hour embryos, and continues at a constant low level of expression through to adults (PubMed:15579689).2 Publications

Gene expression databases

BgeeiFBgn0000317
ExpressionAtlasiQ9V3Z6 baseline and differential
GenevisibleiQ9V3Z6 DM

Interactioni

Subunit structurei

Homodimerizes in a two headed molecule through the formation of a coiled-coil rod (PubMed:16585515). 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 (PubMed:16585515). Interacts with Cad99C (via the cytoplasmic domain) (PubMed:25236597, PubMed:27331610). Interacts with zip and Sans (PubMed:27331610).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CamP621523EBI-15762145,EBI-182924

GO - Molecular functioni

  • actin binding Source: FlyBase
  • actin filament binding Source: InterPro
  • cadherin binding Source: FlyBase
  • microtubule binding Source: InterPro
  • myosin light chain binding Source: FlyBase

Protein-protein interaction databases

BioGridi60900, 13 interactors
DIPiDIP-48747N
IntActiQ9V3Z6, 2 interactors
STRINGi7227.FBpp0080282

Structurei

3D structure databases

ProteinModelPortaliQ9V3Z6
SMRiQ9V3Z6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 733Myosin motorPROSITE-ProRule annotationAdd BLAST671
Domaini736 – 758IQ 1PROSITE-ProRule annotationCuratedAdd BLAST23
Domaini759 – 788IQ 2PROSITE-ProRule annotationAdd BLAST30
Domaini805 – 827IQ 3PROSITE-ProRule annotationCuratedAdd BLAST23
Domaini828 – 857IQ 4PROSITE-ProRule annotationAdd BLAST30
Domaini1008 – 1245MyTH4 1PROSITE-ProRule annotationAdd BLAST238
Domaini1250 – 1560FERM 1PROSITE-ProRule annotationAdd BLAST311
Domaini1558 – 1627SH3PROSITE-ProRule annotationAdd BLAST70
Domaini1701 – 1849MyTH4 2PROSITE-ProRule annotationAdd BLAST149
Domaini1855 – 2158FERM 2PROSITE-ProRule annotationAdd BLAST304

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni612 – 634Actin-bindingBy similarityAdd BLAST23
Regioni712 – 726Actin-bindingBy similarityAdd BLAST15

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili886 – 919Sequence analysisAdd BLAST34

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat, SH3 domain

Phylogenomic databases

eggNOGiKOG4229 Eukaryota
COG5022 LUCA
GeneTreeiENSGT00900000140810
InParanoidiQ9V3Z6
KOiK10359
OMAiTPWHNPS
OrthoDBiEOG091G00BB
PhylomeDBiQ9V3Z6

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, 2 hits
2.30.29.30, 2 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, 4 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, 4 hits
PS51456 MYOSIN_MOTOR, 1 hit
PS51016 MYTH4, 2 hits
PS50002 SH3, 1 hit

Sequencei

Sequence statusi: Complete.

Q9V3Z6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVIVTRGDYI WIEPASGREF DVAIGARVVS AEGRRIQVRD DDGDEVWLAP
60 70 80 90 100
ERRIKAMHAS SVQGVEDMIS LGDLHEAGIL RNLLIRYKEN LIYTYTGSIL
110 120 130 140 150
VAVNPYQILP IYTGDQIKLY KERKIGELPP HIFAIGDNAY AHMKRYRQDQ
160 170 180 190 200
CIVISGESGA GKTESTKLIL QYLAAISGKH SWIEQQILEA NPILEAFGNA
210 220 230 240 250
KTIRNDNSSR FGKYIDIHFS ANGVIEGAKI EQYLLEKSRI VSQNHSERNY
260 270 280 290 300
HVFYCILAGL SADEKSRLDL GMAADYKYLT GGNSITCEGR DDAAEFSDIR
310 320 330 340 350
SAMKVLLFSD QEIWEIIKLL AALLHCGNIK YKATVVDNLD ATEIPEHINV
360 370 380 390 400
ERVAGLLGLP IQPLIDALTR RTLFAHGETV VSTLSRDQSV DVRDAFVKGI
410 420 430 440 450
YGRMFVHIVR KINTAIFKPR GTSRNAIGVL DIFGFENFDQ NSFEQFCINY
460 470 480 490 500
ANENLQQFFV QHIFKLEQEE YNHEAINWQH IEFVDNQDAL DLIAIKQLNI
510 520 530 540 550
MALIDEEARF PKGTDQTMLA KLHKTHGSHK NYLKPKSDIN TSFGLNHFAG
560 570 580 590 600
VVFYDTRGFL DKNRDTFSPD LLHLVSQSTN KFLRQIFAQD IEMGAETRKR
610 620 630 640 650
TPTLSTQFRK SLDALMKTLS SCQPFFIRCI KPNELKKPMM FDRGLCCRQL
660 670 680 690 700
RYSGMMETIR IRRAGYPIRH GFREFVERYR FLIPGVPPAH RTDCQAATSR
710 720 730 740 750
ICAVVLGKSD YQLGHTKVFL KDAHDLFLEQ ERDRVLTRKI LILQRSIRGW
760 770 780 790 800
VYRRRFLRLR AAAITVQRFW KGYAQRKRYR NMRVGYMRLQ ALIRSRVLSH
810 820 830 840 850
RFRHLRGHIV GLQAHARGYL VRREYGHKMW AVIKIQSHVR RMIAMRRYRK
860 870 880 890 900
LRLEHKQFAE VLQLRKLEEQ ELLHRGNKHA REIAEQHYRD RLHELERREI
910 920 930 940 950
QEQLENRRRV EVNMNIINDA ARKQEEPVDD GKLVEAMFDF LPDSSSDAPT
960 970 980 990 1000
PHGGRETSVF NDLPHAQNVN QDDIIAPIHI SEDEEDLSEF KFQKFAATYF
1010 1020 1030 1040 1050
QGNVNHQYAK KALKHPLLPL HTQGDQLAAQ ALWITILRFT GDMPEPKYHT
1060 1070 1080 1090 1100
MDRMDTTSVM SKVTATLGRN FIRSKEFQEA QLMGLDPDAF LKQKPRSIRH
1110 1120 1130 1140 1150
KLVSLTLKRK NKLGEDVRRR LQDDEYTADS YQSWLQSRPT SNLEKLHFII
1160 1170 1180 1190 1200
GHGILRAELR DEIYCQICKQ LTNNPLKSSH ARGWILLSLC VGCFAPSEKF
1210 1220 1230 1240 1250
VNYLRAFIRE GPPGYAPYCE ERLKRTFNNG TRNQPPSWLE LQATKSKKPI
1260 1270 1280 1290 1300
MLPITFMDGN TKTLLADSAT TARELCNQLS DKISLKDQFG FSLYIALFDK
1310 1320 1330 1340 1350
VSSLGSGGDH VMDAISQCEQ YAKEQGAQER NAPWRLFFRK EIFAPWHEPT
1360 1370 1380 1390 1400
HDQVATNLIY QQVVRGVKFG EYRCDKEEDL AMIAAQQYFI EYSTDMSMER
1410 1420 1430 1440 1450
LFTLLPNFIP DFCLSGVDKA IERWAALVLQ AYKKSYYVKD KIAPLKIKED
1460 1470 1480 1490 1500
IVSYAKYKWP LLFSRFYEAY RNSGPNLPKN DVIIAVNWTG VYVVDDQEQV
1510 1520 1530 1540 1550
LLELSFPEIT AVSSQKTNKV FTQTFSLSTV RGEEFTFQSP NAEDIRDLVV
1560 1570 1580 1590 1600
YFLDGLKKRS KYVIALQDYR APSDGTSFLS FFKGDLIILE DESCGESVLN
1610 1620 1630 1640 1650
NGWCIGRCDR SQERGDFPAE TVYVLPTLSK PPQDILALFN IEEAHHGRRL
1660 1670 1680 1690 1700
SMASNGGAVE PRDRPHTLME YALDHFRLPP KRTMSKTLTL SSKRSEELWR
1710 1720 1730 1740 1750
YSRDPIKAPL LRKLQSKEEF AEEACFAFAA ILKYMGDLPS KRPRMGNEIT
1760 1770 1780 1790 1800
DHIFDGPLKH EILRDEIYCQ LMKQLTDNRN RMSEERGWEL MWLATGLFAC
1810 1820 1830 1840 1850
SQGLLKELLL FLRTRRHPIS QDSMHRLQKT IRHGQRKYPP HQVEVEAIQH
1860 1870 1880 1890 1900
KTTQIFHKVY FPDDTDEAFE VDSSTRAKDF CNNISQRLSL RTSEGFSLFV
1910 1920 1930 1940 1950
KIADKVISVP EGDFFFDFVR HLTDWIKKAR PIRDGANPQF TYQVFFMKKL
1960 1970 1980 1990 2000
WTNTVPGKDR NADLIFHYHQ ELPKLLRGYH KCSREEAAKL AALVFRVRFG
2010 2020 2030 2040 2050
ENKQELQAIP QMLRELIPSD IMKIQSTSEW KRSIVASYNQ DGGMTSEDAK
2060 2070 2080 2090 2100
VAFLKIVYRW PTFGSAFFEV KQTTEPNYPE MLLIAINKHG VSLIHPVTKD
2110 2120 2130 2140 2150
ILVTHPFTRI SNWSSGNTYF HMTIGNLVRG SKLLCETSLG YKMDDLLTSY
2160
ISLMLTNMNK NRTIRAN
Length:2,167
Mass (Da):250,309
Last modified:May 1, 2000 - v1
Checksum:i3C57E34ADDD89A42
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2024I → M in AAR96124 (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA Translation: AAF53435.1
AE014134 Genomic DNA Translation: AAN10886.1
AY069438 mRNA Translation: AAL39583.2
BT011332 mRNA Translation: AAR96124.1
RefSeqiNP_001285949.1, NM_001299020.1
NP_001285950.1, NM_001299021.1
NP_523571.1, NM_078847.4
NP_723895.1, NM_165099.3
UniGeneiDm.2128

Genome annotation databases

EnsemblMetazoaiFBtr0080723; FBpp0080282; FBgn0000317
FBtr0080724; FBpp0080283; FBgn0000317
FBtr0343686; FBpp0310274; FBgn0000317
FBtr0343687; FBpp0310275; FBgn0000317
GeneIDi34882
KEGGidme:Dmel_CG7595

Similar proteinsi

Entry informationi

Entry nameiMYO7A_DROME
AccessioniPrimary (citable) accession number: Q9V3Z6
Secondary accession number(s): Q6NNF6, Q8T0A9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 141 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families
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