MY9AA_DANRE
ID MY9AA_DANRE Reviewed; 2522 AA.
AC E7EZG2;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Unconventional myosin-IXAa {ECO:0000250|UniProtKB:B2RTY4};
DE AltName: Full=Myosin IXAa {ECO:0000312|ZFIN:ZDB-GENE-080424-5};
GN Name=myo9aa {ECO:0000312|ZFIN:ZDB-GENE-080424-5};
GN Synonyms=myo9al1 {ECO:0000312|ZFIN:ZDB-GENE-080424-5};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27259756; DOI=10.1093/brain/aww130;
RA O'Connor E., Toepf A., Mueller J.S., Cox D., Evangelista T., Colomer J.,
RA Abicht A., Senderek J., Hasselmann O., Yaramis A., Laval S.H.,
RA Lochmueller H.;
RT "Identification of mutations in the MYO9A gene in patients with congenital
RT myasthenic syndrome.";
RL Brain 139:2143-2153(2016).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Regulates Rho
CC by stimulating it's GTPase activity in neurons (By similarity).
CC Required for the regulation of neurite branching and motor neuron axon
CC guidance (PubMed:27259756). {ECO:0000250|UniProtKB:Q9Z1N3,
CC ECO:0000269|PubMed:27259756}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9Z1N3}.
CC Synapse {ECO:0000250|UniProtKB:Q8C170}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q8C170}. Note=Localized in the cytoplasm of cell
CC bodies, dendrites and axons with occasional hints of an enrichment near
CC the plasma membrane. Localized at the neuromuscular junction.
CC {ECO:0000250|UniProtKB:Q8C170, ECO:0000250|UniProtKB:Q9Z1N3}.
CC -!- DISRUPTION PHENOTYPE: Morpholino-induced knockdown affects tail
CC morphology, and causes cardiac edema and abnormal swimming in response
CC to tactile stimulation. Morphants show aberrant axons, either short or
CC over-extended, with some axons appearing to branch to the adjacent
CC myotome. {ECO:0000269|PubMed:27259756}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000255|PROSITE-ProRule:PRU00782}.
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DR EMBL; AL929115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX470121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR388017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT030707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009301790.1; XM_009303515.2.
DR AlphaFoldDB; E7EZG2; -.
DR SMR; E7EZG2; -.
DR STRING; 7955.ENSDARP00000039809; -.
DR PaxDb; E7EZG2; -.
DR PeptideAtlas; E7EZG2; -.
DR Ensembl; ENSDART00000039810; ENSDARP00000039809; ENSDARG00000076729.
DR GeneID; 100006612; -.
DR KEGG; dre:100006612; -.
DR CTD; 100006612; -.
DR ZFIN; ZDB-GENE-080424-5; myo9aa.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000154905; -.
DR HOGENOM; CLU_000192_2_2_1; -.
DR InParanoid; E7EZG2; -.
DR OMA; KYQAANM; -.
DR OrthoDB; 14881at2759; -.
DR PhylomeDB; E7EZG2; -.
DR TreeFam; TF319651; -.
DR Reactome; R-DRE-8980692; RHOA GTPase cycle.
DR Reactome; R-DRE-9013424; RHOV GTPase cycle.
DR PRO; PR:E7EZG2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000076729; Expressed in retina and 22 other tissues.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044295; C:axonal growth cone; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0061564; P:axon development; IGI:ZFIN.
DR GO; GO:0048675; P:axon extension; IGI:ZFIN.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007626; P:locomotory behavior; IGI:ZFIN.
DR GO; GO:0098529; P:neuromuscular junction development, skeletal muscle fiber; IGI:ZFIN.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0036269; P:swimming behavior; IGI:ZFIN.
DR CDD; cd00029; C1; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR028558; MYO9A.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF3; PTHR46184:SF3; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 1.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Actin-binding; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW GTPase activation; Membrane; Metal-binding; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome; Repeat; Synapse; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..2522
FT /note="Unconventional myosin-IXAa"
FT /id="PRO_0000447239"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 15..113
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 147..1007
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1012..1039
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1063..1092
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1102..1131
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1125..1154
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2054..2242
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 1990..2039
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 767..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..910
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1012..1149
FT /note="Neck or regulatory domain"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT REGION 1150..2497
FT /note="Tail"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT REGION 1218..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1630..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1799..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1962..1983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2274..2325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2348..2522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1456..1525
FT /evidence="ECO:0000255"
FT COILED 2317..2344
FT /evidence="ECO:0000255"
FT COMPBIAS 770..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1458..1527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1593..1610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1667
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1809..1823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2359..2381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2397..2412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2414..2461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2472..2491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240..247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2522 AA; 290166 MW; 1BE0A62458DF92E6 CRC64;
MSVHDVGGRR RFEDSELTLR IYPGIIAEGT IYCPVAARKI TSAAEVIEQV IDRLQLDRTK
CYVLAEVKEF GGEEWILNPT DYPVQRMMLW PRMALENRFS SEDYRFLLRE KNLDGSIHYG
NLQMWLQVTE ERRRMVERGF LPQPLPKDFD DLCNLPDLNE KTLLDNLRSR FKQEKIYTYV
GSILIVINPF KFLPIYNPKY VKMYDNHQLG KLEPHIYAVA DVAYHAMLQS RQNQCIVISG
ESGSGKTQST NFLIHHLTAL SQKGFASGVE QIILGAGPVL EAFGNAKTAH NNNSSRFGKF
IQVNYQESGT VRGAYVEKYL LEKSRLVYQE HNERNYHVFY YLLAGTSEEE RTAFHLKKPE
EYHYLNQMTK KPHRPHWGNY YENEPDCFTV EGEDLKHDFE RLQLAMEMVG FLPTTRKQIF
SLLSAILHLG NIRYKKKIYR DDSIDICNPE VLPVVSELLE VKEEMLFEAL TTRKTVTVGE
KLIVPYKLAE AGTVRDSMAK SLYSALFDWI VFRINHALLN QRDLEESAKI LSIGVLDIFG
FEDYENNSFE QFCINFANER LQHYFNQHIF KLEQEEYRAE GITWHNIDYI DNTSCITLIS
KKPTALLHLL DEECNFPQAT NQTLLDKFKR QHEGNSYIEF PAVMEPAFII KHYAGKVKYG
VKDFREKNTD HMRPDIVALL KSSKNAFICG LIGIDPVATF RWAVLRAYFR AMVAFRDAGK
RHVEKRSGHD AAAPAVKSVD SFSFLHHPVH QRSLEILQRC KEEKYSVNRR NPRTPLSDLQ
GSNAINQREG WNGRPGRQNR LSSFGSFSEE EGIFINSTSS KLLERAHGIL MRNKNYKMKP
SLPKHLLDVK SLKYLSNLTL QDRITKSLLH LHKKKKPPSI SAQFQASLNK LMETLGQSQP
YFVKCIRSNS EKLPLRFNDS LVLRQLRYTG MLETVRIRQS GYSIKYTFQD FARHFHVLLP
EGSNQASQEA IRQYLQQVDL TPEGFQVGRT MVFLREIERQ RLQDLLHKEV LSRIVYLQRR
FRALLERKNF LRVRQAACQI QNWWRSCQSL QRDSQLEYDM RVQEGAVVCI QSAWRGFRER
RRLLLWREAS VLIQRTWRLY RQRRAALQIQ TAWRRHRARE LFLRQRDATI RLQAVGRGYL
ARQRFRELQK QRLKITHLPN GKASLLTEED KLEDMGLDAS MLEDSFEEQD RSKQALSSAV
EASGAGVLEE MEVEMMEGMA PAQPSPEVTI RERPRTLEDP NQRTRAKRES RRMRELEQAK
FSLELLKVRS TGGTSPSDER RWSMELVSEI AHTPQGTPDS QSSKGSFELL NIDDYFKDKA
PCAEPEDLGS PSSVPDQHNV LPSDTSTPDI LSKPDDQSKP PRMQYSLPTF YTPPSESSSL
VIKSTTNSVT PCPDGLSKPS KDKKESTRRP MVVVISMQKE TLLNEADVKP LEVKDSAAQT
SEPPSPAQPS TDSSYVLEKL EKLNEEKEER QKHQRQQNEK EMMEQIRQQT HILEEQRRNL
VQNEREKLEK QRAETLRRIE QSRQESSGGR TDRPAPIAQP EPDLTSQRPA REKDGAPLIL
RDRPKDAQNL AEGWAPKLTL ESRGDEARSR INKKPSNQNV NISMSERPGN IFFSPKTKIA
YSKLNKDLAN QEKTPGAQNE VSLLGYKSTK TEVGRPGHKK ARMARTRSDF LTRSSSTQGE
GESEEEEYDE TPLYAGTPLP KQDSEESAVE ACHSDSEMLT TAAEEQKNRC KTLPSGELGK
HDTRKNSHGD GRVRGKMRFW GKAKNAEKKS SRERLLCGSD TLEGDYTEAT LLMEEGVERL
SPPHSPDLTL QREFKENKEP SPKVKRRRSV KISSVALEPV QWQNDALQIL TCTSDYKSMN
DFLMKKITDL DTEDGKKDTM VDVVFKKALK EFRVNIFNSY STALAMDDGK SIRYKDLYAL
FEQILEKNMR QEQRDWSESP VKVWVNTFKV FLDEFMTEHK PLDSSLGKAP KPDRKKRRKK
DTDVVEEHNG HIFKSTQYSI PTYCEYCSSL IWMMDKACVC KLCRYACHRK CCQKMTTKCS
KKYDPELSSR QFGVELSRLT NDERTVPLVV EKLVNYIEMH GLYTEGIYRK SGSTNKIKEL
KQGLDTDVNG VNLDDYNINV IASVFKQWLR DLPNPLMTFE LYEEFLRAMG LQDKKEVIRG
VYSVIDQLSR THLNTLERLI FHLVRIALQE ETNRMSANAL AIVFAPCILR CPDTIDPLRS
VQDIGKTTAC VELIICEQMN KYRARLKDIN TLEFAENKAK SRLTFIRRSM GKGPVHRLRY
RTPSPPTSPR SPTAPEVMQD SGEEEPGRDP EVSEQQQVAM QQEEKVLTEQ IESLQKEKEE
LTFEMLALEP RASDDETLES EASIGTADSS ENLNVDSEGA TSDYSERGPA LAATRPKKSE
GKSRRVLRKQ PESLDSIDSC STVSSVSSSY MQPTSRTHKL SLRSKSPSKR LYLSSPSESL
DQPEQDGEER PQFTSRGTFN PEKGKQRLQG AKSSPQRHRE QKKDPELSPQ QVVVYGSNEF
MV
