MYO1D_MOUSE
ID MYO1D_MOUSE Reviewed; 1006 AA.
AC Q5SYD0; Q5SSK7; Q8BWY5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Unconventional myosin-Id;
GN Name=Myo1d {ECO:0000312|EMBL:CAI26106.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC33719.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33719.1};
RC TISSUE=Embryonic stem cell {ECO:0000312|EMBL:BAC33719.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-536, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20089841; DOI=10.1091/mbc.e09-07-0638;
RA Benesh A.E., Nambiar R., McConnell R.E., Mao S., Tabb D.L., Tyska M.J.;
RT "Differential localization and dynamics of class I myosins in the
RT enterocyte microvillus.";
RL Mol. Biol. Cell 21:970-978(2010).
CC -!- FUNCTION: Unconventional myosin that functions as actin-based motor
CC protein with ATPase activity (By similarity). 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 tracheal cells, for normal rotational
CC polarity of cilia, and for coordinated, unidirectional ciliary movement
CC in the trachea. Required for normal, polarized cilia organization in
CC brain ependymal epithelial cells (By similarity).
CC {ECO:0000250|UniProtKB:F1PRN2, ECO:0000250|UniProtKB:Q63357}.
CC -!- SUBUNIT: Interacts (via the two IQ motifs) with calmodulin. Binds an
CC additional calmodulin chain via a third, C-terminal region. 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:0000269|PubMed:20089841}. Basolateral cell membrane
CC {ECO:0000269|PubMed:20089841}. Note=Colocalizes with the actin
CC cytoskeleton in the cell cortex close to the basolateral cell membrane
CC (PubMed:20089841). Colocalizes with the actin cytoskeleton in the cell
CC cortex close to the apical cell membrane (PubMed:20089841). Colocalizes
CC with cytoplasmic puncta that are reminiscent of transport vesicles (By
CC similarity). {ECO:0000250|UniProtKB:Q63357,
CC ECO:0000269|PubMed:20089841}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SYD0-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:16141072};
CC IsoId=Q5SYD0-2; Sequence=VSP_051938, VSP_051939;
CC -!- TISSUE SPECIFICITY: Detected in enterocytes at the intestinal brush
CC border membrane. Detected at the tip of intestinal microvilli (at
CC protein level). {ECO:0000269|PubMed:20089841}.
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-1 (MYH1). {ECO:0000305}.
CC -!- CAUTION: Contrary to the situation in zebrafish, xenopus and
CC drosophila, mammalian MYO1D defects have no effects on left-right body
CC asymmetry. {ECO:0000250|UniProtKB:Q63357}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33719.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK049374; BAC33719.1; ALT_FRAME; mRNA.
DR EMBL; AL591146; CAI24746.1; -; Genomic_DNA.
DR EMBL; AL591410; CAI24746.1; JOINED; Genomic_DNA.
DR EMBL; AL663054; CAI24746.1; JOINED; Genomic_DNA.
DR EMBL; AL591410; CAI26106.1; -; Genomic_DNA.
DR EMBL; AL591146; CAI26106.1; JOINED; Genomic_DNA.
DR EMBL; AL663054; CAI26106.1; JOINED; Genomic_DNA.
DR EMBL; AL591410; CAI26107.1; -; Genomic_DNA.
DR EMBL; AL663054; CAI26107.1; JOINED; Genomic_DNA.
DR EMBL; AL663054; CAI25852.1; -; Genomic_DNA.
DR EMBL; AL591146; CAI25852.1; JOINED; Genomic_DNA.
DR EMBL; AL591410; CAI25852.1; JOINED; Genomic_DNA.
DR EMBL; AL663054; CAI25853.1; -; Genomic_DNA.
DR EMBL; AL591410; CAI25853.1; JOINED; Genomic_DNA.
DR CCDS; CCDS36242.1; -. [Q5SYD0-1]
DR RefSeq; NP_796364.2; NM_177390.3. [Q5SYD0-1]
DR RefSeq; XP_006533648.1; XM_006533585.1. [Q5SYD0-2]
DR AlphaFoldDB; Q5SYD0; -.
DR SMR; Q5SYD0; -.
DR BioGRID; 237219; 11.
DR IntAct; Q5SYD0; 4.
DR MINT; Q5SYD0; -.
DR STRING; 10090.ENSMUSP00000037819; -.
DR iPTMnet; Q5SYD0; -.
DR PhosphoSitePlus; Q5SYD0; -.
DR SwissPalm; Q5SYD0; -.
DR EPD; Q5SYD0; -.
DR jPOST; Q5SYD0; -.
DR MaxQB; Q5SYD0; -.
DR PaxDb; Q5SYD0; -.
DR PeptideAtlas; Q5SYD0; -.
DR PRIDE; Q5SYD0; -.
DR ProteomicsDB; 287581; -. [Q5SYD0-1]
DR ProteomicsDB; 287582; -. [Q5SYD0-2]
DR Antibodypedia; 27274; 109 antibodies from 24 providers.
DR DNASU; 338367; -.
DR Ensembl; ENSMUST00000041065; ENSMUSP00000037819; ENSMUSG00000035441. [Q5SYD0-1]
DR Ensembl; ENSMUST00000070997; ENSMUSP00000066948; ENSMUSG00000035441. [Q5SYD0-2]
DR GeneID; 338367; -.
DR KEGG; mmu:338367; -.
DR UCSC; uc007kmh.1; mouse. [Q5SYD0-1]
DR UCSC; uc011yau.1; mouse. [Q5SYD0-2]
DR CTD; 4642; -.
DR MGI; MGI:107728; Myo1d.
DR VEuPathDB; HostDB:ENSMUSG00000035441; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000157411; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; Q5SYD0; -.
DR OMA; QDVKYGH; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; Q5SYD0; -.
DR TreeFam; TF312960; -.
DR BioGRID-ORCS; 338367; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Myo1d; mouse.
DR PRO; PR:Q5SYD0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SYD0; protein.
DR Bgee; ENSMUSG00000035441; Expressed in prostate gland ventral lobe and 240 other tissues.
DR Genevisible; Q5SYD0; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0097440; C:apical dendrite; ISS:UniProtKB.
DR GO; GO:0030673; C:axolemma; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS: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; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
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; ISO:MGI.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0051641; P:cellular localization; IDA:UniProtKB.
DR GO; GO:0061502; P:early endosome to recycling endosome transport; ISS:UniProtKB.
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; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Cell membrane; Cell projection; Cytoplasm; Endosome;
KW Membrane; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; 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_0000123448"
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..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 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:0007744|PubMed:18034455"
FT VAR_SEQ 904..944
FT /note="LTGLSVSNGKDQLVVFHTKDNKDLIVCLFSKQPTHESRIGE -> ISHAHSS
FT ALTLHLLLGRTNFRTMEWLPPLVRQTGYKGGLQM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051938"
FT VAR_SEQ 945..1006
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051939"
SQ SEQUENCE 1006 AA; 116081 MW; 547A7FDCA656E572 CRC64;
MAEQESLEFG KADFVLMDTV SMPEFMANLR LRFEKGRIYT FIGEVVVSVN PYKVLNIYGR
DTVEQYKGRE LYERPPHLFA IADAAYKAMK RRSKDTCIMI SGESGAGKTE ASKYIMQYIA
AITNPSQRAE IERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH
INNYLLEKSR VIVQQPGERS FHSFYQLLQG GSEQMLHSLH LQKSLSSYNY IRVGAQLKSS
INDAAEFKVV ADAMKVIGFK PEEIQTVYKI LAVILHLGNL KFIVDGDTPL IENGKVVSVI
AELLSTKADM VEKALLYRTV ATGRDIIDKQ HTEQEASYGR DAFAKAIYER LFCWIVTRIN
DIIEVKNYDT TIHGKNTVIG VLDIYGFEIF DNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ
EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIIAILDDAC MNVGKVTDGM FLEALNSKLG
KHGHFSSRKT CASDKILEFD RDFRIRHYAG DVVYSAIGFI DKNKDTLFQD FKRLMYNSSN
PVLKNMWPEG KLSITEVTKR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNDKKSPQI
FDDERCRHQV EYLGLLENVR VRRAGFAFRQ TYEKFLHRYK MISEFTWPNH DLPSDKEAVK
KLIERCGFQD DVAYGKSKIF 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
