MYO7A_DROPS
ID MYO7A_DROPS Reviewed; 2168 AA.
AC Q29P71;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Myosin-VIIa;
DE AltName: Full=Protein crinkled;
GN Name=ck; ORFNames=GA20466;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL34422.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements: can function
CC in cells as a single-molecule cargo transporter. A very slow and high-
CC duty-ratio motor, may be suitable for tension maintenance of actin
CC filaments. Their highly divergent tails are presumed to bind to
CC membranous compartments, which would be moved relative to actin
CC filaments. Plays a key role in the formation of cellular projections
CC and other actin-based functions required for embryonic and larval
CC viability. Necessary for auditory transduction: plays a role in
CC Johnston organ (JO) organization by functioning in scolopidial apical
CC attachment and therefore to acoustic stimulus propagation from the
CC antenna a2/a3 joint to transducing elements (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimerizes in a two headed molecule through the formation
CC of a coiled-coil rod. {ECO:0000250|UniProtKB:Q9V3Z6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9V3Z6}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL34422.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH379058; EAL34422.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001357353.1; XM_001357317.2.
DR AlphaFoldDB; Q29P71; -.
DR SMR; Q29P71; -.
DR STRING; 7237.FBpp0279362; -.
DR EnsemblMetazoa; FBtr0280924; FBpp0279362; FBgn0080461.
DR GeneID; 4818109; -.
DR KEGG; dpo:Dpse_GA20466; -.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_14_1_1; -.
DR InParanoid; Q29P71; -.
DR OMA; LHRGNKH; -.
DR PhylomeDB; Q29P71; -.
DR Proteomes; UP000001819; Chromosome 4.
DR Bgee; FBgn0080461; Expressed in female reproductive system and 1 other tissue.
DR GO; GO:0045179; C:apical cortex; IEA:EnsemblMetazoa.
DR GO; GO:0045180; C:basal cortex; IEA:EnsemblMetazoa.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0035182; C:female germline ring canal outer rim; IEA:EnsemblMetazoa.
DR GO; GO:0070825; C:micropyle; IEA:EnsemblMetazoa.
DR GO; GO:0005902; C:microvillus; IEA:EnsemblMetazoa.
DR GO; GO:0031477; C:myosin VII complex; IEA:EnsemblMetazoa.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IEA:EnsemblMetazoa.
DR GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0032027; F:myosin light chain binding; ISS:UniProtKB.
DR GO; GO:0060002; F:plus-end directed microfilament motor activity; IEA:EnsemblMetazoa.
DR GO; GO:0007015; P:actin filament organization; IEA:EnsemblMetazoa.
DR GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR GO; GO:0048800; P:antennal morphogenesis; ISS:UniProtKB.
DR GO; GO:0008407; P:chaeta morphogenesis; ISS:UniProtKB.
DR GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IEA:EnsemblMetazoa.
DR GO; GO:0046847; P:filopodium assembly; IEA:EnsemblMetazoa.
DR GO; GO:0032529; P:follicle cell microvillus organization; IEA:EnsemblMetazoa.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; ISS:UniProtKB.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 2.
DR CDD; cd13198; FERM_C1_MyoVII; 1.
DR CDD; cd13199; FERM_C2_MyoVII; 1.
DR CDD; cd01381; MYSc_Myo7; 1.
DR Gene3D; 1.20.80.10; -; 2.
DR Gene3D; 1.25.40.530; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041793; MyoVII_FERM_C1.
DR InterPro; IPR041794; MyoVII_FERM_C2.
DR InterPro; IPR036106; MYSc_Myo7.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 2.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47031; SSF47031; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50057; FERM_3; 2.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2168
FT /note="Myosin-VIIa"
FT /id="PRO_0000306377"
FT DOMAIN 63..733
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 736..758
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 759..788
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 805..827
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 828..857
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1008..1245
FT /note="MyTH4 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1250..1560
FT /note="FERM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 1558..1627
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1702..1850
FT /note="MyTH4 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1856..2159
FT /note="FERM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 612..634
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P08799"
FT REGION 712..726
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P08799"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08799"
SQ SEQUENCE 2168 AA; 250150 MW; E9AB5981F080B81F CRC64;
MVIVTRGDYI WIEPASGREF DVAIGARVIS AEGRRIQVRD DDGDEVWLAP ERRIKAMHAS
SVQGVEDMIS LGDLHEAGIL RNLLIRYKEN LIYTYTGSIL VAVNPYQILP IYTGDQIKLY
KERKIGELPP HIFAIGDNAY AHMKRYLQDQ CIVISGESGA GKTESTKLIL QYLAAISGKH
SWIEQQILEA NPILEAFGNA KTIRNDNSSR FGKYIDIHFS ANGVIEGAKI EQYLLEKSRI
VSQNHSERNY HVFYCILAGL SSEEKSRLDL GAAADYKYLT GGNSITCEGR DDAAEFSDIR
SAMKVLLFSD QEIWEIIKLL AALLHCGNIK YKATVVDNLD ATEIPEHINV ERVAGLLGLP
IQPLIDALTR RTLFAHGETV VSTLSRDQSV DVRDAFVKGI YGRLFVHIVR KINTAIFKPR
ATSRNAIGVL DIFGFENFDQ NSFEQFCINY ANENLQQFFV QHIFKLEQEE YNHEAINWQH
IEFVDNQDAL DLIAIKQLNI MALIDEEARF PKGTDTTMLA KLHKTHGSHK NYLKPKSDIN
TSFGLNHFAG VVFYDTRGFL DKNRDTFSPD LLHLVSQSGN KFLRQIFAQD IEMGAETRKR
TPTLSTQFRK SLDALMKTLS SCQPFFIRCI KPNELKKPMM FDRGLCCRQL RYSGMMETIR
IRRAGYPIRH GFREFVERYR FLIPGVPPAH RTDCQVATSR ICAMVLGKSD YQLGHTKVFL
KDAHDLFLEQ ERDRVLTRKI LILQRSIRGW VYRRRFLRLR AAAISVQRFW KGYAQRKRYR
NMRVGYMRLQ ALIRSRVLSH RFRHLRGHIV GLQAHARGYL VRREYGHKMW AVIKIQSHVR
RMIAVRRYRK LRLEHKQFAE VLHLRKMEEQ ELMHRGNKHA REIAEQHYRD RLHELERREI
ATQLEDRRRV EVKMNIINDA ARKQEEPVDD GKLVEAMFDF LPDSSSDAPT PHGGRETSVF
MDLPQGQAAN QEDIIAQLHV SEDEEDLSEF KFQKFAATYF QGNVNHQYAK KALKHPLLPL
HTQGDQLAAQ ALWITILRFT GDMPEPKYHT MDRMDTTSVM SKVTATLGRN FIRSKEFQEA
QLMGLDPDAF LKQKPRSIRH KLVSLTLKRK NKLGEDVRRR LQDDEYTADS YQSWLQSRPT
SNLEKLHFII GHGILRAELR DEIYCQICKQ LTNNPLKSSH ARGWILLSLC VGCFAPSEKF
VNYLRAFIRE GPPGYAPYCE ERLKRTFNNG TRNQPPSWLE LQATKSKKPI MLPITFMDGN
TKTLLADSAT TARELCNQLS DKITLKDQFG FSLYIALFDK VSSLGSGGDH VMDAISQCEQ
YAKEQGAQER NAPWRLFFRK EIFAPWHEPT HDQVATNLIY QQVVRGVKFG EYRCDKEEDL
AMIAAQQYFI EYGTDMSMER LFTLLPNFIP DFCLSGVDKA IERWAALVLQ AYKKSYYVKD
KIAALKIKED IVSYAKYKWP LLFSRFYEAY RNSGPNLPKN DVIIAVNWTG VYVVDDQEQV
LLELSFPEIT AVSSQKTTKV FTQTFSLSTV RGEEFTFQSP NAEDIRDLVV YFLDGLKKRS
KYVIALQDYR APSDGTSFLS FFKGDLIILE DESCGESVLN NGWCIGRCDR SQERGDFPAE
TVYVLPTLSK PPQDILALFN IEDAAHHGRR LSMASNGGTV EPRDRPHTLM EYALDHFRLP
PKRTMSKTLT LSSKRSEELW RYSRDPIKLP LLRKLQSKEE LAEEACFAFA AILKYMGDLP
SKRPRMGNEI TDHIFDGPLK HEILRDEIYC QLMKQLTDNR NRMSEERGWE LMWLATGLFA
CSQGLLKELS LFLRTRRHPI SQDSMHRLQK TIRHGQRKYP PHQVEVEAIQ HKTTQIFHKV
YFPDDTDEAF EVDSSTRAKD FCNNISQRLS LRTSEGFSLF VKIADKVISV PEGDFFFDFV
RHLTDWIKKA RPIRDGANPQ FTYQVFFMKK LWTNTVPGKD RNADLIFHYH QELPKLLRGY
HKCSREEAAK LAALVFRVRF GENKTELQAI PQMLRELIPS DIMKMQSTNE WKRSIVASYN
QDGGMTSEDA KVAFLKIVYR WPTFGSAFFE VKQTTEPNYP EMLLIAINKH GVSLIHPVTK
DILVTHPFTR ISNWSSGNTY FHMTIGNLVR GSKLLCETSL GYKMDDLLTS YISLMLTNMN
KNRTIRAN
