MYO7A_AEDAE
ID MYO7A_AEDAE Reviewed; 2163 AA.
AC Q17LW0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Myosin-VIIa;
DE AltName: Full=Protein crinkled;
GN Name=ck {ECO:0000250|UniProtKB:Q9V3Z6}; ORFNames=AAEL001220;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000312|EMBL:EAT47711.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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}.
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DR EMBL; CH477210; EAT47711.1; -; Genomic_DNA.
DR RefSeq; XP_001658316.1; XM_001658266.1.
DR AlphaFoldDB; Q17LW0; -.
DR SMR; Q17LW0; -.
DR STRING; 7159.AAEL001220-PA; -.
DR PRIDE; Q17LW0; -.
DR VEuPathDB; VectorBase:AAEL001220; -.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_14_1_1; -.
DR InParanoid; Q17LW0; -.
DR OMA; LHRGNKH; -.
DR OrthoDB; 527681at2759; -.
DR PhylomeDB; Q17LW0; -.
DR Proteomes; UP000008820; Chromosome 2.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0120025; C:plasma membrane bounded cell projection; IEA:UniProt.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0032027; F:myosin light chain binding; ISS:UniProtKB.
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:0035317; P:imaginal disc-derived wing hair organization; ISS:UniProtKB.
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..2163
FT /note="Myosin-VIIa"
FT /id="PRO_0000306375"
FT DOMAIN 58..728
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 731..753
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 754..783
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 800..822
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 823..852
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1003..1239
FT /note="MyTH4 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1244..1554
FT /note="FERM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 1552..1621
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1697..1845
FT /note="MyTH4 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1851..2154
FT /note="FERM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 607..629
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P08799"
FT REGION 707..721
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P08799"
FT REGION 937..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 886..914
FT /evidence="ECO:0000255"
FT BINDING 151..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08799"
SQ SEQUENCE 2163 AA; 250159 MW; 22D27AD802948931 CRC64;
MGDYIWIEPV SGREFDVAIG ARVISAEGRR IQVRDDDGNE LWLTPERRIK AMHASSVQGV
EDMISLGDLH EAGILRNLLI RYNDNLIYTY TGSILVAVNP YQILPIYTAD QIKLYKERKI
GELPPHIFAI GDNSYANMRR YGQDQCIVIS GESGAGKTES TKLILQYLAA ISGKHSWIEQ
QILEANPILE AFGNAKTVRN DNSSRFGKYI DIHFNNSGVI EGAEIEQYLL EKSRIVSQNA
EERNYHIFYC LLAGLSSDEK RKLNLGYASD YRYLTGGGCI KCDGRNDAAE FADIRSAMKV
LCFSDHEIWE ILKLLAALLH TGNITYRATV IDNLDATEIP EHINVERVAN LLEVPFQPFI
DALTRKTLFA HGETVVSTLS RDQSMDVRDA FVKGIYGRLF VLIVKKINSA IYKPKSSTRS
AIGVLDIFGF ENFKHNSFEQ FCINFANENL QQFFVRHIFK LEQEEYNHES INWQHIEFVD
NQDALDLIAI KQLNIMALID EESKFPKGTD QTMLAKLHKT HGTHRNYLKP KSDINTSFGL
NHFAGVVFYD TRGFLEKNRD TFSADLLQLI SSSTNRFLQM VFAEDIGMGA ETRKRTPTLS
TQFKKSLDSL MKTLSSCQPF FIRCIKPNEL KKPMMFDRAL CCRQLRYSGM METIRIRRAG
YPIRHKFKDF VERYRFLISG IPPAHRTDCR LATSKICASV LGRSDYQLGH TKVFLKDAHD
LFLEQERDRV LTRKILILQR SIRGWVYRRR FLRMRQAAVT IQKFWKGYAQ RQRYKKMKIG
YMRLQALIRS RVLSHRFRHL RGHIVRLQAR IRGYLVRREY GLKMWAVIKI QSHVRRMIAM
NRYQKLKLEY RRHHEALRLR RMEEEELKHQ GNKRAKEIAE QHYRDRLNEI ERKEIEQELE
ERRRVEVKKN IINDAARKAD EPVDDSKLVE AMFDFLPDSS SEAPTPHGGR ETSVFNDLPV
NQDNHEDIIG PIHTISEDEE DLSEFKFQKF AATYFQGNIT HFYSRKPLKH PLLPLHTQGD
QLAAQALWIT ILRFTGDLPE PRYHTMDRDN TSVMSKVTAT LGRNFIRSKE FQEAQMMGLD
PEAFLKQKPR SIRHKLVSLT LKRKNKLGED VRRRLQDEEY TADSYQSWLE SRPTSNLEKL
HFIIGHGILR AELRDEIYCQ ICKQLTNNPS KSSHARGWIL LSLCVGCFAP SEKFVNYLRS
FIREGPPGYA PYCEERLKRT FNNGTRNQPP SWLELQATKS KKPIMLPITF MDGNTKTLLA
DSATTARELC NQLSDKIALK DQFGFSLYIA LFDKVSSLGS GGDHVMDAIS QCEQYAKEQG
AQERNAPWRL FFRKEIFAPW HNPIEDQVAT NLIYQQVVRG VKFGEYRCDK EEDLAMIAAQ
QYYIEYNTDM SMDRLYTLLP NFIPDYCLTG IEKAIDRWAA LVLQAYKKSY YLKDKAAALK
VKEDVVSYAK YKWPLLFSRF YEAYRNSGPN LPKNDVIIAV NWTGVYVVDD QEQVLLELSF
PEITAVSSQK TNKVFTQTFS LSTVRNEEFT FQSPNAEDIR DLVVYFLEGL KKRSKFVIAL
QDYKAPGEGT SFLSFLKGDL IILEDESTGE SVLNSGWCIG CCERTQERGD FPAEIVYVLP
SLTKPPPDIL ALFSVEDAHH GKRLNSIHSN GGTETREHPH TLADYSLDHF RPPPKRTMSK
ALSTLSSKRG GDELWRYSRE PLKQPLLKKL LAKEELAEEA CLAFIAIMKY MGDLPSKRPR
IGNEITDHIF DGPLKHEILR DEIYCQLMKQ LTDNRNRMSE ERGWELMWLS TGLFACSQQL
LKELTVFLRT RRHPISQDSL HRLQKTIRNG QRKYPPHQVE VEAIQHKTTQ IFHKVYFPDD
TDEAFEVDSS TRAKDFCQNI SQRLNLRSSE GFSLFVKIAD KVISVPEGDF FFDFVRHLTD
WIKKARPTRD GTNPQFTYQV FFMKKLWTNT VPGKDKNADL IFHYHQELPK LLRGYHKCSK
EEAVKLAALV YRVRFGESKQ ELQAIPQMLR ELVPSDLIKL QTTNDWKRSI VAAYNQDAGM
SPEDAKVTFL KIVYRWPTFG SAFFEVKQTT EPNYPEMLLI AINKHGVSLI HPSSKDILVT
HPFTRISNWS SGNTYFHMTI GNLVRGSKLL CETSLGYKMD DLLTSYISLM LTNMNKQRTI
RIK
