MYO1D_DANRE
ID MYO1D_DANRE Reviewed; 1004 AA.
AC E7F9L8;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Unconventional myosin-Id;
DE AltName: Full=Myosin 1d {ECO:0000303|PubMed:30139971};
DE AltName: Full=Myosin1D {ECO:0000303|PubMed:29769531};
GN Name=myo1d;
GN ORFNames=si:ch211-94l19.4 {ECO:0000312|Ensembl:ENSDARP00000067761};
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 {ECO:0000312|Proteomes:UP000000437};
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, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=29769531; DOI=10.1038/s41467-018-04284-8;
RA Juan T., Geminard C., Coutelis J.B., Cerezo D., Poles S., Noselli S.,
RA Fuerthauer M.;
RT "Myosin1D is an evolutionarily conserved regulator of animal left-right
RT asymmetry.";
RL Nat. Commun. 9:1942-1942(2018).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30139971; DOI=10.1038/s41467-018-05866-2;
RA Saydmohammed M., Yagi H., Calderon M., Clark M.J., Feinstein T., Sun M.,
RA Stolz D.B., Watkins S.C., Amack J.D., Lo C.W., Tsang M.;
RT "Vertebrate myosin 1d regulates left-right organizer morphogenesis and
RT laterality.";
RL Nat. Commun. 9:3381-3381(2018).
CC -!- FUNCTION: Unconventional myosin that functions as actin-based motor
CC protein with ATPase activity (By similarity). Plays a role in the
CC formation of Kupffer's vesicle, an organ that functions as left-right
CC organizer during embryogenesis (PubMed:29769531, PubMed:30139971).
CC Plays a role in vesicular trafficking events that are required for
CC normal lumen expansion of Kupffer's vesicle (PubMed:30139971). Required
CC for normal orientation of cilia in Kupffer's vesicle, and thus for
CC normal, unidirectional circular flow and normal angular flow velocity,
CC which then mediates asymmetric gene expression and left-right
CC asymmetric development (PubMed:29769531). Plays a role in endosomal
CC protein trafficking, and especially in the transfer of cargo proteins
CC from early to recycling endosomes (By similarity). Required for normal
CC planar cell polarity in ciliated cells, for normal rotational polarity
CC of cilia, and for coordinated, unidirectional ciliary movement (By
CC similarity). {ECO:0000250|UniProtKB:F1PRN2,
CC ECO:0000250|UniProtKB:Q63357, ECO:0000269|PubMed:29769531,
CC ECO:0000269|PubMed:30139971}.
CC -!- SUBUNIT: Interacts (via the two IQ motifs) with calmodulin. Interacts
CC with F-actin. {ECO:0000250|UniProtKB:Q63357}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q63357}.
CC Perikaryon {ECO:0000250|UniProtKB:Q63357}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q63357}. Early endosome
CC {ECO:0000250|UniProtKB:F1PRN2}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q63357}. Note=Colocalizes with the actin
CC cytoskeleton in the cell cortex close to the apical cell membrane.
CC Colocalizes with cytoplasmic puncta that are reminiscent of transport
CC vesicles. {ECO:0000250|UniProtKB:Q63357}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC (PubMed:29769531). Ubiquitous in embryos at the four cell stage
CC (PubMed:30139971). Detected at the eight cell stage. Detected at low
CC levels throughout the embryo at the six somite stage, with higher
CC levels in the developing notochord (PubMed:29769531).
CC {ECO:0000269|PubMed:29769531, ECO:0000269|PubMed:30139971}.
CC -!- DOMAIN: Binds a calmodulin chain via each of the two IQ domains. IQ
CC domain 1 mediates interaction with calmodulin both in the presence and
CC in the absence of Ca(2+). IQ domain 2 mediates interaction with
CC calmodulin in the presence of Ca(2+). {ECO:0000250|UniProtKB:Q63357}.
CC -!- DOMAIN: The TH1 domain is required for activity in complementing
CC zebrafish defects in Kupffer's vesicle lumen size.
CC {ECO:0000250|UniProtKB:Q63357}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes situs
CC inversus, a left-right asymmetry defect where organs are placed at a
CC position corresponding to the mirror image of the normal body plan.
CC Causes laterality defects at the level of the heart, viscera and brain
CC (PubMed:29769531). Morpholino knockdown of the protein leads to the
CC formation of a Kupffer's vesicle with reduced volume and dismorphic
CC shape. Morpholino knockdown of the protein interferes with the normal
CC cellular remodeling that gives rise to anterior-posterior asymmetry of
CC Kupffer's vesicle. Cells with a columnar shape persist at the posterior
CC end of the vesicle, contrary to wild-type, where cells display columnar
CC shape at the anterior part of the vesicle, and squamous or cuboidal
CC shape at the posterior end of Kupffer's vesicle. Epithelial cells
CC lining Kupffer's vesicle display an increased number of vacuoles, and
CC disruption of the normal, directed vacuolar trafficking toward the
CC apical cell membrane (PubMed:30139971). {ECO:0000269|PubMed:29769531,
CC ECO:0000269|PubMed:30139971}.
CC -!- MISCELLANEOUS: Agents that activate cftr increase the size of Kupffer's
CC vesicle in myo1d mutants (PubMed:29769531, PubMed:30139971). Expansion
CC of the lumen size is not sufficient to restore the normal spherical
CC shape of Kupffer's vesicle and rescue laterality defects
CC (PubMed:29769531, PubMed:30139971). Heterologous expression of rat
CC Myo1d can complement the defects in Kupffer's vesicle lumen size and
CC anterior-posterior cell shape changes (PubMed:30139971).
CC {ECO:0000269|PubMed:29769531, ECO:0000269|PubMed:30139971}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000255|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Represents an unconventional myosin that should not be
CC confused with the conventional myosin-1. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Another kind of harmony
CC - Issue 213 of April 2019;
CC URL="https://web.expasy.org/spotlight/back_issues/213/";
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DR EMBL; CR391936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT033798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT033800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_688008.5; XM_682916.7.
DR AlphaFoldDB; E7F9L8; -.
DR SMR; E7F9L8; -.
DR STRING; 7955.ENSDARP00000067761; -.
DR PaxDb; E7F9L8; -.
DR PeptideAtlas; E7F9L8; -.
DR Ensembl; ENSDART00000067762; ENSDARP00000067761; ENSDARG00000036863.
DR GeneID; 559562; -.
DR KEGG; dre:559562; -.
DR CTD; 4642; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000157411; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; E7F9L8; -.
DR OMA; QDVKYGH; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; E7F9L8; -.
DR TreeFam; TF312960; -.
DR PRO; PR:E7F9L8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000036863; Expressed in swim bladder and 26 other tissues.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0071910; P:determination of liver left/right asymmetry; IMP:UniProtKB.
DR GO; GO:0035469; P:determination of pancreatic left/right asymmetry; IMP:UniProtKB.
DR GO; GO:0060287; P:epithelial cilium movement involved in determination of left/right asymmetry; IMP:UniProtKB.
DR GO; GO:0061966; P:establishment of left/right asymmetry; IMP:UniProtKB.
DR GO; GO:0003146; P:heart jogging; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Cell projection; Cytoplasm;
KW Developmental protein; Endosome; Motor protein; Myosin; Nucleotide-binding;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1004
FT /note="Unconventional myosin-Id"
FT /id="PRO_0000446322"
FT DOMAIN 9..695
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 699..719
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 721..741
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 812..1003
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 572..594
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1004 AA; 115885 MW; 77990A4B7D4C2754 CRC64;
MAEHESLEFG KADFVLLDNV SLEEFMANLK LRFEKGRIYS YIGEVVVSVN PYRAMNIYGR
DVIEQYKGRE LYERPPHLFA IADAAYKAMK RRNKDTCIVI SGESGAGKTE ASKYIMQYIA
AITNPSQRAE VERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH
INNYLLEKSR VIFQQEGERS FHSFYQLVKG APDAQLRSLH IQRDPTAYNY IKVGGQLKSS
INDSAEFKAV ADAMKVIGFT TEEIQTVYKI LATILHLGNL KFGTDGDVTL IENSKLVSVL
GDLLSTKEEN VEKAMLYRTV ATGRDVIDKQ HTHQEASYGR DALAKAIYER LFCWIVGRIN
DIIEVKNYDA RVHGKNTVIG VLDIYGFEIF QNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ
EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIFAVLDEAC MNVGKVTDEM FLQALNGKLA
KHAHYTSRKL SPTDKNLEFE RDFRIRHYAG DVTYSVVGFI DKNKDTLFQD FKRLLYNSSN
PVLKAMWPEG KLSITEVTKR PLTAATLFKN SMISLVEKLA SKEPYYVRCI KPNDVKSPLL
FEHERCKHQV EYLGLLENVR VRRAGFANRQ TYPRFLQRYK MISEFTWPNH DLSSDKEAVK
RLLQGCGFEH DVAYGKTKVF IRTPRTIFSL EEQRAEMVKR IVLFLQKVWR GTLARMRYRR
MRAALIIIRA YRRYKVKSYI REVIRRFKNV RDMKDHGKHV KWPTPPKVLR KFEEALRSIY
NRWWAWTLIK PLSPEKTVQI RAKVATLECL KGQRADLGLQ RAWEGNYLKK DSPGTASSFT
LVSSDLQRKD KFMRVLFSSN VRKINRFNKA EDRALLITDR HLYKMDPLKQ YKPMKSIPLY
NVTGVSISPG KDQLVVFHTK DNRDLIVCLQ GMVPAGDSRI GELVGTLLSH FKSEKRKLQV
NTVSPIHCSM NGRKCTVVVE TKISQSQPDF TKSRSGYILS VPGN
