MYO1D_RAT
ID MYO1D_RAT Reviewed; 1006 AA.
AC Q63357; Q5PQU2;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Unconventional myosin-Id {ECO:0000303|PubMed:26446290};
DE AltName: Full=Myosin heavy chain myr 4;
GN Name=Myo1d; Synonyms=Myr4 {ECO:0000303|PubMed:8034741};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley;
RX PubMed=8034741; DOI=10.1083/jcb.126.2.375;
RA Baehler M., Kroschewski R., Stoeffler H.E., Behrmann T.;
RT "Rat myr4 defines a novel subclass of myosin I: identification,
RT distribution, localization, and mapping of calmodulin-binding sites with
RT differential calcium sensitivity.";
RL J. Cell Biol. 126:375-389(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, INTERACTION WITH CALMODULIN, DOMAIN, AND ACTIN-BINDING.
RX PubMed=12719468; DOI=10.1083/jcb.200212039;
RA Koehler D., Ruff C., Meyhoefer E., Baehler M.;
RT "Different degrees of lever arm rotation control myosin step size.";
RL J. Cell Biol. 161:237-241(2003).
RN [4]
RP FUNCTION, DOMAIN, INTERACTION WITH CALMODULIN, AND ACTIN-BINDING.
RX PubMed=15853803; DOI=10.1111/j.1742-4658.2005.04642.x;
RA Koehler D., Struchholz S., Baehler M.;
RT "The two IQ-motifs and Ca2+/calmodulin regulate the rat myosin 1d ATPase
RT activity.";
RL FEBS J. 272:2189-2197(2005).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=24903835; DOI=10.1002/jnr.23419;
RA Yamazaki R., Ishibashi T., Baba H., Yamaguchi Y.;
RT "Unconventional myosin ID is expressed in myelinating oligodendrocytes.";
RL J. Neurosci. Res. 92:1286-1294(2014).
RN [6]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=26446290; DOI=10.1002/cm.21259;
RA Hegan P.S., Ostertag E., Geurts A.M., Mooseker M.S.;
RT "Myosin Id is required for planar cell polarity in ciliated tracheal and
RT ependymal epithelial cells.";
RL Cytoskeleton 72:503-516(2015).
RN [7]
RP RESCUE OF KUPFFER'S VESICLE LUMEN SIZE AND ANTERIOR-POSTERIOR CELL
RP MORPHOLOGY DEFECTS, AND DOMAIN.
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 (PubMed:12719468, PubMed:15853803). Plays
CC a role in endosomal protein trafficking, and especially in the transfer
CC of cargo proteins from early to recycling endosomes (By similarity).
CC Required for normal planar cell polarity in ciliated tracheal cells,
CC for normal rotational polarity of cilia, and for coordinated,
CC unidirectional ciliary movement in the trachea. Required for normal,
CC polarized cilia organization in brain ependymal epithelial cells
CC (PubMed:26446290). {ECO:0000250|UniProtKB:F1PRN2,
CC ECO:0000269|PubMed:12719468, ECO:0000269|PubMed:15853803,
CC ECO:0000269|PubMed:26446290}.
CC -!- SUBUNIT: Interacts (via the two IQ motifs) with calmodulin
CC (PubMed:8034741, PubMed:12719468, PubMed:15853803). Binds an additional
CC calmodulin chain via a third, C-terminal region (PubMed:8034741).
CC Interacts with F-actin (PubMed:12719468, PubMed:15853803).
CC {ECO:0000269|PubMed:12719468, ECO:0000269|PubMed:15853803,
CC ECO:0000269|PubMed:8034741}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24903835,
CC ECO:0000269|PubMed:8034741}. Perikaryon {ECO:0000269|PubMed:8034741}.
CC Cell projection, dendrite {ECO:0000269|PubMed:8034741}. Early endosome
CC {ECO:0000250|UniProtKB:F1PRN2}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:26446290}. Note=Colocalizes with the actin
CC cytoskeleton in the cell cortex close to the apical cell membrane
CC (PubMed:26446290). Colocalizes with cytoplasmic puncta that are
CC reminiscent of transport vesicles (PubMed:8034741).
CC {ECO:0000269|PubMed:26446290, ECO:0000269|PubMed:8034741}.
CC -!- TISSUE SPECIFICITY: Detected on tracheal epithelial cells, and on
CC epithelial cells and brush border cells in duodenum, jejunum and ileum
CC (PubMed:26446290). Detected on myelinated white matter in the
CC cerebellum, and the myelinated part of the optic nerve. Detected on
CC mature oligodendrocites. Detected on the outside of the myelin sheet
CC that surrounds axons (at protein level) (PubMed:24903835). Ubiquitous.
CC Highest levels in adult brain, and spinal chord. Moderate levels in
CC lung, kidney, liver and spleen. Low levels in testis and heart (at
CC protein level). {ECO:0000269|PubMed:24903835,
CC ECO:0000269|PubMed:26446290, ECO:0000269|PubMed:8034741}.
CC -!- DEVELOPMENTAL STAGE: Not detected in brain one week after birth, prior
CC to the onset of myelination, and levels are low two weeks after birth.
CC Expressed at high and constant levels in brain after three weeks and
CC later (at protein level) (PubMed:24903835). Expression is
CC developmentally regulated during brain ontogeny, rising 2-3 week
CC postnatally, and is maximal in adult brain (PubMed:8034741,
CC PubMed:24903835). {ECO:0000269|PubMed:24903835,
CC ECO:0000269|PubMed:8034741}.
CC -!- DOMAIN: Binds a calmodulin chain via each of the two IQ domains
CC (PubMed:12719468, PubMed:15853803). IQ domain 1 mediates interaction
CC with calmodulin both in the presence and in the absence of Ca(2+). IQ
CC domain 2 mediates interaction with calmodulin in the presence of Ca(2+)
CC (PubMed:8034741, PubMed:15853803). {ECO:0000269|PubMed:12719468,
CC ECO:0000269|PubMed:15853803, ECO:0000269|PubMed:8034741}.
CC -!- DOMAIN: The TH1 domain is required for activity in complementing
CC zebrafish defects in Kupffer's vesicle lumen size.
CC {ECO:0000269|PubMed:30139971}.
CC -!- DISRUPTION PHENOTYPE: Mutants display no defects in body left-right
CC asymmetry, no obvious motor defects, and normal kidney and liver
CC morphology. Tracheal epithelial cells display aberrant ciliary bending
CC angles and disordered ciliary bending patterns. Likewise, planar cell
CC polarity is disrupted in ependymal epithelial cells.
CC {ECO:0000269|PubMed:26446290}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Contrary to the situation in zebrafish, xenopus and
CC drosophila, rat Myo1d defects have no effects on left-right body
CC asymmetry. {ECO:0000269|PubMed:26446290}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-1 (MYH1). {ECO:0000305}.
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DR EMBL; X71997; CAA50871.1; -; mRNA.
DR EMBL; BC087027; AAH87027.1; -; mRNA.
DR PIR; A53933; A53933.
DR RefSeq; NP_037115.2; NM_012983.2.
DR AlphaFoldDB; Q63357; -.
DR SMR; Q63357; -.
DR BioGRID; 247518; 3.
DR IntAct; Q63357; 1.
DR MINT; Q63357; -.
DR STRING; 10116.ENSRNOP00000004609; -.
DR iPTMnet; Q63357; -.
DR PhosphoSitePlus; Q63357; -.
DR jPOST; Q63357; -.
DR PaxDb; Q63357; -.
DR PRIDE; Q63357; -.
DR Ensembl; ENSRNOT00000004609; ENSRNOP00000004609; ENSRNOG00000003276.
DR GeneID; 25485; -.
DR KEGG; rno:25485; -.
DR CTD; 4642; -.
DR RGD; 621321; Myo1d.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000157411; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; Q63357; -.
DR OMA; QDVKYGH; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; Q63357; -.
DR TreeFam; TF312960; -.
DR PRO; PR:Q63357; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003276; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q63357; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0097440; C:apical dendrite; IDA:UniProtKB.
DR GO; GO:0030673; C:axolemma; IDA:RGD.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0051641; P:cellular localization; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
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; PF00612; IQ; 1.
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 Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
KW Cell projection; Cytoplasm; Endosome; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O94832"
FT CHAIN 2..1006
FT /note="Unconventional myosin-Id"
FT /id="PRO_0000123449"
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 ECO:0000305|PubMed:8034741"
FT DOMAIN 721..741
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305|PubMed:8034741"
FT DOMAIN 812..1005
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 REGION 776..896
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000269|PubMed:8034741"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O94832"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94832"
FT MOD_RES 536
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5SYD0"
FT CONFLICT 82
FT /note="A -> L (in Ref. 1; CAA50871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1006 AA; 116095 MW; ECD245C8ACACEA53 CRC64;
MAEQESLEFG KADFVLMDTV SMPEFMANLR LRFEKGRIYT FIGEVVVSVN PYKVLNIYGR
DTIEQYKGRE LYERPPHLFA IADAAYKAMK RRSKDTCIMI SGESGAGKTE ASKYIMQYIA
AITNPSQRAE IERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH
INNYLLEKSR VIVQQPGERS FHSFYQLLQG GSEQMLHSLH LQKSLSSYNY IRVGAQLKSS
INDAAEFKVV ADAMKVIGFK PEEIQTVYKI LAAILHLGNL KFIVDGDTPL IENGKVVSVI
AELLSTKADM VEKALLYRTV ATGRDIIDKQ HTEQEASYGR DAFAKAIYER LFCWIVTRIN
DIIEVKNYDT TVHGKNTVIG VLDIYGFEIF DNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ
EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIIAILDDAC MNVGKVTDGM FLEALNSKLG
KHGHFSSRKT CASDKILEFD RDFRIRHYAG DVVYSVIGFI DKNKDTLFQD FKRLMYNSSN
PVLKNMWPEG KLSITEVTKR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNDKKSPQI
FDDERCRHQV EYLGLLENVR VRRAGFAFRQ TYEKFLHRYK MISEFTWPNH DLPSDKEAVK
KLIERCGFQD DVAYGKTKIF IRTPRTLFTL EELRAQMLVR VVLFLQKVWR GTLARMRYKR
TKAALTIIRY YRRYKVKSYI HEVARRFHGV KNMRDYGKHV KWPTPPKVLR RFEEALQSIF
NRWRASQLIK TIPASDLPQV RAKVAAMEML KGQRADLGLQ RAWEGNYLAS KPDTPQTSGT
FVPVANELKR KDKYMNVLFS CHVRKVNRFS KVEDRAIFVT DRHLYKMDPT KQYKVMKTIP
LYNLTGLSVS NGKDQLVVFH TKDNKDLIVC LFSKQPTHES RIGELVGVLV NHFKSEKRHL
QVNVTNPVQC SLHGKKCTVS VETRLNQPQP DFTKNRSGFI LSVPGN
