MYO1D_XENLA
ID MYO1D_XENLA Reviewed; 1007 AA.
AC Q6GPA1; A0A1L8ESA8; Q719M4;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Unconventional myosin-Id;
DE AltName: Full=Unconventional myosin 1d {ECO:0000303|PubMed:19382939, ECO:0000303|PubMed:29478852};
GN Name=myo1d {ECO:0000303|PubMed:19382939,
GN ECO:0000312|Xenbase:XB-GENE-5877264}; ORFNames=XELAEV_18043319mg;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:AAH73240.1};
RN [1] {ECO:0000312|EMBL:AAQ11360.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=19382939; DOI=10.1111/j.1440-169x.2009.01107.x;
RA LeBlanc-Straceski J.M., Sokac A., Bement W., Sobrado P., Lemoine L.;
RT "Developmental expression of Xenopus myosin 1d and identification of a
RT myo1d tail homology that overlaps TH1.";
RL Dev. Growth Differ. 51:443-451(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J;
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [3] {ECO:0000312|EMBL:AAH73240.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH73240.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29478852; DOI=10.1016/j.cub.2018.01.075;
RA Tingler M., Kurz S., Maerker M., Ott T., Fuhl F., Schweickert A.,
RA LeBlanc-Straceski J.M., Noselli S., Blum M.;
RT "A Conserved Role of the Unconventional Myosin 1d in Laterality
RT Determination.";
RL Curr. Biol. 28:810-816(2018).
CC -!- FUNCTION: Unconventional myosin that functions as actin-based motor
CC protein with ATPase activity (By similarity). Plays an important role
CC in the establishment of left-right asymmetry during embryonic
CC development (PubMed:29478852). Required for normal cilia orientation,
CC and for normal, directed flow at the transient ciliated epithelium that
CC functions as left-right organizer during embryogenesis
CC (PubMed:29478852). Plays a role in endosomal protein trafficking, and
CC especially in the transfer of cargo proteins from early to recycling
CC endosomes (By similarity). Required for normal planar cell polarity in
CC ciliated cells, for normal rotational polarity of cilia, and for
CC coordinated, unidirectional ciliary movement (By similarity).
CC {ECO:0000250|UniProtKB:F1PRN2, ECO:0000250|UniProtKB:Q63357,
CC ECO:0000269|PubMed:29478852}.
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: Detected at low levels in eggs and in embryos at
CC stage 12. Expression increases from stage 18 to 34 during embryonic
CC development (at protein level). First detected at stage 17, when
CC somites begin to form. Detected in somites, neural tube and neural
CC crest cells at stage 20-30. {ECO:0000269|PubMed:19382939}.
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 at the four
CC cell stage disrupts body left-right asymmetry at the level of the
CC heart, gall bladder and gut (PubMed:29478852). The left-right
CC organizer, a transient ciliated epithelium of the gastrocoel roof
CC plate, displays abnormally short cilia and disruption of the normal
CC cilia orientation toward the posterior pole of cells, leading to
CC disordered flow direction and reduced flow velocity. Additional
CC phenotypes include delayed neural tube closure due to impaired
CC convergent-extension of dorsal marginal zone tissue, and a transient
CC delay in the ciliation of multi-ciliated cells in the larval skin,
CC suggesting that planar cell polarity pathways are affected. Combined
CC morpholino knockdown with sub-phenotypic doses for myo1d and vangl2
CC disrupts left-right axis formation, with predominantly bilateral
CC expression of pitx2 (PubMed:29478852). {ECO:0000269|PubMed:29478852}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000255, ECO:0000255|PROSITE-
CC ProRule:PRU00782}.
CC -!- CAUTION: Represents an unconventional myosin that should not be
CC confused with the conventional myosin-1. {ECO:0000305}.
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DR EMBL; AF540952; AAQ11360.1; -; mRNA.
DR EMBL; CM004482; OCT62234.1; -; Genomic_DNA.
DR EMBL; BC073240; AAH73240.1; -; mRNA.
DR RefSeq; NP_001083106.1; NM_001089637.1.
DR AlphaFoldDB; Q6GPA1; -.
DR SMR; Q6GPA1; -.
DR STRING; 8355.Q6GPA1; -.
DR MaxQB; Q6GPA1; -.
DR DNASU; 398749; -.
DR GeneID; 398749; -.
DR KEGG; xla:398749; -.
DR CTD; 398749; -.
DR Xenbase; XB-GENE-5877264; myo1d.L.
DR OMA; QDVKYGH; -.
DR OrthoDB; 122881at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 398749; Expressed in intestine and 20 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: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: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 1: Evidence at protein 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..1007
FT /note="Unconventional myosin-Id"
FT /id="PRO_0000446323"
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..1006
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"
FT CONFLICT 258
FT /note="G -> E (in Ref. 1; AAQ11360)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="D -> G (in Ref. 3; AAH73240)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="A -> T (in Ref. 1; AAQ11360)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="R -> K (in Ref. 1; AAQ11360)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="R -> G (in Ref. 1; AAQ11360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1007 AA; 116136 MW; E2EE54A8422A939F CRC64;
MAEQEGLQYG KADFVLMDSV TLPEFMENLK LRFEKGRIYT FIGEVVVSVN PYKNLPIYGR
DTIEQYKGRE LYERPPHLFA IADAAYKAMK RRCKDTCIVI SGESGAGKTE ASKYIMQYIA
AITNPSQRAE VERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH
ISNYLLEKSR VIVQQLGERN FHSFYQMILG APEQTLRSLH LQRDISSYAY TRSLAQLKSS
NNDAGDFKEV AEAMKVIGFK PEEIQTVYKI LAAILHLGNL KFIVDGDTTL IENGKVVSVV
ADLLGTRSEQ VEKALLFRTV ATGRDVIDKQ HTEKEANYGR DAFAKAIYER LFCWIVNRIN
DVIDVKQQDA SLHGKNTVIG VLDIYGFEIF DNNSLEQFCI NYCNEKLQQL FIQLVLTQEQ
AEYQREGIPW KHIDYFDNQI IVDLVEQQHK GIISLLDDAC MNVGKVTDDM FLEALNKQLG
KHAHYSSRKV CATDKALEYN RDFRIRHYAG DVVYSVVGFI DKNKDTLFQD FKRLMFNSSN
PVLKTMWPEG KLSITEVTKR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNEKKSPAL
FDEVRCRHQV EYLGLLENVR VRRAGFAYRQ VYDKFLHRYK LISSLTWPNH SLPSDRIAVE
RFMVDCGLNH DAAYGKTKIF IRTPRTLFSL EERRSEMLIR IILFLQKLWR GTLARRRCKR
IRAGLTILRY YRRYKVKSYL REVMHRFNGV KNSRDYGKHV KWPTPPRVLR RFQEALQNIY
NRWRGYQIIK SLPPAEIPKV RAKVAAFENL KGHRVDMGLQ RCWEGSYLAS NQENARNSNQ
FVSRSNELQR KDKFMQALFS CHVQKVNRFN KVQDRAIFIT DRHLYKMDPG KEYKVMTSTP
LYNVSGISVT SGKDQLVVFH MKDNKDLIVC LGCSGQGPYD SRIGELVGVL ANHFKSERRP
LQVTVSHPIQ CRQHGRSCSI TVETKINQSQ PQFTKNRAGF TLSVPAN
