MY9AB_DANRE
ID MY9AB_DANRE Reviewed; 2286 AA.
AC E7F3F0;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 3.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Unconventional myosin-IXAb {ECO:0000250|UniProtKB:B2RTY4};
DE AltName: Full=Myosin IXAb {ECO:0000312|ZFIN:ZDB-GENE-080424-6};
GN Name=myo9ab {ECO:0000312|ZFIN:ZDB-GENE-080424-6};
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; CABZ01074925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01074926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01074927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01074928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01074929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01074930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU633744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E7F3F0; -.
DR SMR; E7F3F0; -.
DR STRING; 7955.ENSDARP00000032580; -.
DR Ensembl; ENSDART00000028997; ENSDARP00000032580; ENSDARG00000073843.
DR ZFIN; ZDB-GENE-080424-6; myo9ab.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000154905; -.
DR HOGENOM; CLU_000192_2_1_1; -.
DR InParanoid; E7F3F0; -.
DR TreeFam; TF319651; -.
DR PRO; PR:E7F3F0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 25.
DR Bgee; ENSDARG00000073843; Expressed in brain and 20 other tissues.
DR ExpressionAtlas; E7F3F0; baseline and differential.
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:InterPro.
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 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; 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; 3.
DR Pfam; PF00612; IQ; 2.
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 Membrane; Metal-binding; Motor protein; Myosin; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..2286
FT /note="Unconventional myosin-IXAb"
FT /id="PRO_0000447240"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 16..114
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 148..971
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 976..996
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1025..1054
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1066..1095
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1089..1118
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1823..2011
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 1759..1808
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 853..875
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 976..1113
FT /note="Neck or regulatory domain"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT REGION 1114..2254
FT /note="Tail"
FT /evidence="ECO:0000250|UniProtKB:B2RTY4"
FT REGION 1118..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1732..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2032..2087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2113..2286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2080..2107
FT /evidence="ECO:0000255"
FT COMPBIAS 1133..1178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2033..2048
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2160..2175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2179..2215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2239..2271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 242..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2286 AA; 262083 MW; DF9F1A1A2DEF882C CRC64;
IMSCHDVGGR RRFEDSEFTL RVYPGSLSES TIYCPVSARK VTTAAEVIER VIERLQLDRT
RLYVLAEVKE FGGEEWILNP SDCPAQRMML WPRMALENRL LGEDYRFLLR EKNLDGSIHY
GSLQMWLRVT EERRRMVERG LLPQPPAAQF VADLCSLPDL NEHTMLENLR GRFRQENIYT
YVGSILIAVN PFKFLPIYNP KYVKMYDKHR LGQLEPHIFA VADAAYHAML QRHRNQCIVI
SGESGSGKTQ STNFLIHHLT ALSQKGFASG VEQIILGAGP VLEAFGNAKT AHNNNSSRFG
KFIQVNYQES GTVRGAYVEK YLLEKSRLVY QEHNERCSCV NIFSKLVCHE LKVCVCMCVQ
DCFSVEAEDL KHDFERLQLA MEMVGFLPTT RKQIFSLLSA ILHLGNIRYK KKTFRDDSID
ICNPEVLPIV SELLEVKEEM LFEALTTRKT VTVGERLIVP YKLAEVRKGT SHQLIQTFRT
SHSLLHQRYF HIHTSPTRIL SIGVLDIFGF EDYENNSFEQ FCINFANETL QHYFNQHVFK
LEQEEYRSEG INWHMIDYID NTACINLISK KPTALLHLLD EECNFPQASN QTLLDKFKRQ
HEGNAYMEFP AVMEPAFIIR HYAGKVKYSV KDFREKNTDH LRPDIVSLLK SSRKAFICGL
MGLDPVASFR WAVIRAFFRA LVAFRHAGLQ HRDNRSSSDV HLQPQKSVDS FSFLHHPVHQ
RSLEILQRCK DDRYNSCVSR RSPRTPLSDL QGANTFSSNG RGWRSERVSS FAHEDEGIFV
NSVNNRLLER AQGILMRNKN YKPKPSLPKH LLDVKSLKYL SSLTLHDRIT KSLLHLHKKK
KPPSISAQFN VSLNKLMETL GQSEPYFVKC IRSNAEKLPL RFNDALVLRQ LRYTGMLETV
RIRQSGYSVK YSFKDFAHHF HVLLPAGFSA SQMGIREFLR SADLEPSGYQ VGRSMVFLHE
RLRQRLQDEL HQEVLRRIVC LQRSFRTQRD RKHFCRQRRA ARLIQRWWRS CISQADGSVC
ALELQQGAAL RLQAVWRGFR ARRLYLQQRR AVLIIQRCWR RVLNTRNTAA TLIQAVWRTR
THRRSFLQQR RAAVTLQAAC RGQQSRQRCR ILREQQCREQ SKHPSTVTKS LHQNTEEAEK
LEEVWEKQTT DPPPKAVDDS TLKSRNKRES RRQRELEQAT FSLELLKVRS GSNTEDAQIP
PSKHHPPHQA STDSQESFEL LENEDSASAK LELSKSEPME VNQTSPAASF KPHFYIPDED
GSPINSAPQT PNRAKQIREK KESVVVIISM QKENPVDRSS LQTLEAQDVP LSNGESASDC
SIIPEPRTNH ELDTGSSFSV SSKPLQLDLR SAASNEEPSE PKADVQKKFV SQSISISMKE
TAANVAFPPK RSRLTFSKSD KDLVNQERSL AIQREAGFRS LKNRDVTRAG CKKKARMART
RSDFLSRACS TEADCEEDED DEYEDTPVLS CTRPPHSPSS PDIDCVFHSD SEMSSQKEQK
RIQKTMSSGD LGKMDSLRKS MSQTDSRVRG KMRFWSKSKH GDKKISSRGR SADSELTDRR
NDSPPGSPEH AGVSERRRDS KENREPMLGM MSMKRRRSLK ISSVSLESTA WQNDALHILT
STADYRSMND FLMKKISDLD AEDGQKDTAV DVVFKKALKE FRLNIFNSYS TALAMDDGRS
IRYKDLYALF EHILEKSMRL EQRDWSESPV KVWVNTFKVF LDEFMTEYKP MDGTISKAPK
PERKKRRKKE SDTVEEHMGH IFKSTQYSIP TYCEFCSSLI WMMDKACVCK LCRYACHKKC
CLRMTTKCSK KFDPELSSRQ FGVELSRLTS DERSVPLVVE KLINYIEMHG LYTEGIYRKS
GSTNKIKELK QGLDTDANSV NLDDYNIHVI ASVLKQWLRD LPNPLMTFEL YEEFLRAMGL
QDKREVVQGV YSIIDQLSRT HLNTLERLIF HLVRISFQEE TNRMSANALA IVFAPCILRC
PDTTDPLQSV RDISKTTACV ELIICEQMRK YKARLKDINT LEFAENKAKS RLTHIRRSMG
KSRARKSGHH TPSPPLSPRA SEREEPVDEG AEPVLSEQQQ AAMQQEEKVL TQQIENLQKE
KEELTYEMLA LEPRASDDEM LESEASIGTA DSSENLMESE GAASDPWEKS PGAVSASRWR
KSESKSRRCL RRQPESLDSV DSAVASLSSV SSTPHYRFRS SSSGPLFSSS SPTGDLHILP
DPESCEQASL SARCASSSEK TRPRPRANRS CPPKPREPGD TGGRRREHEF GSSQPLVLYG
SNEFMV
