ID MYO1C_MOUSE Reviewed; 1063 AA.
AC Q9WTI7; O08571; O08834; Q3TBQ4; Q3U231; Q5ND46; Q5ND48; Q5ND49; Q9ERB6;
AC Q9QW54;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 24-JAN-2024, entry version 204.
DE RecName: Full=Unconventional myosin-Ic;
DE AltName: Full=Myosin I beta;
DE Short=MMI-beta;
DE Short=MMIb;
GN Name=Myo1c;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=DBA/2J; TISSUE=Brain;
RX PubMed=9182797; DOI=10.1016/s0896-6273(00)80312-8;
RA Hamilton B.A., Smith D.J., Mueller K.L., Kerrebrock A.W., Bronson R.T.,
RA van Berkel V., Daly M.J., Kruglyak L., Reeve M.P., Nemhauser J.L.,
RA Hawkins T.L., Rubin E.M., Lander E.S.;
RT "The vibrator mutation causes neurodegeneration via reduced expression of
RT PITP alpha: positional complementation cloning and extragenic
RT suppression.";
RL Neuron 18:711-722(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH POLR2A, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=11030652; DOI=10.1126/science.290.5490.337;
RA Pestic-Dragovich L., Stojiljkovic L., Philimonenko A.A., Nowak G., Ke Y.,
RA Settlage R.E., Shabanowitz J., Hunt D.F., Hozak P., de Lanerolle P.;
RT "A myosin I isoform in the nucleus.";
RL Science 290:337-341(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-842 (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Cochlea;
RX PubMed=9119401; DOI=10.1006/geno.1996.4526;
RA Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
RA Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G., Weil D.,
RA Pujol R., Petit C.;
RT "Cloning of the genes encoding two murine and human cochlear unconventional
RT type I myosins.";
RL Genomics 40:332-341(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-34 (ISOFORM 1).
RC TISSUE=Placenta;
RA Gerhard D.S.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 181-628 (ISOFORM 1/2/3/4).
RX PubMed=8449986; DOI=10.1083/jcb.120.6.1405;
RA Sherr E.H., Joyce M.P., Greene L.A.;
RT "Mammalian myosin I alpha, I beta, and I gamma: new widely expressed genes
RT of the myosin I family.";
RL J. Cell Biol. 120:1405-1416(1993).
RN [10]
RP FUNCTION.
RX PubMed=11853671; DOI=10.1016/s0092-8674(02)00629-3;
RA Holt J.R., Gillespie S.K., Provance D.W., Shah K., Shokat K.M., Corey D.P.,
RA Mercer J.A., Gillespie P.G.;
RT "A chemical-genetic strategy implicates myosin-1c in adaptation by hair
RT cells.";
RL Cell 108:371-381(2002).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12490950; DOI=10.1038/nature01246;
RA Bose A., Guilherme A., Robida S.I., Nicoloro S.M., Zhou Q.L., Jiang Z.Y.,
RA Pomerleau D.P., Czech M.P.;
RT "Glucose transporter recycling in response to insulin is facilitated by
RT myosin Myo1c.";
RL Nature 420:821-824(2002).
RN [12]
RP FUNCTION.
RX PubMed=15014434; DOI=10.1038/sj.emboj.7600169;
RA Batters C., Arthur C.P., Lin A., Porter J., Geeves M.A., Milligan R.A.,
RA Molloy J.E., Coluccio L.M.;
RT "Myo1c is designed for the adaptation response in the inner ear.";
RL EMBO J. 23:1433-1440(2004).
RN [13]
RP FUNCTION.
RX PubMed=14980509; DOI=10.1016/j.yexcr.2003.10.028;
RA Fomproix N., Percipalle P.;
RT "An actin-myosin complex on actively transcribing genes.";
RL Exp. Cell Res. 294:140-148(2004).
RN [14]
RP INTERACTION WITH PLEKHB1.
RX PubMed=15976448; DOI=10.1242/jcs.02424;
RA Etournay R., El-Amraoui A., Bahloul A., Blanchard S., Roux I., Pezeron G.,
RA Michalski N., Daviet L., Hardelin J.-P., Legrain P., Petit C.;
RT "PHR1, an integral membrane protein of the inner ear sensory cells,
RT directly interacts with myosin 1c and myosin VIIa.";
RL J. Cell Sci. 118:2891-2899(2005).
RN [15]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16102537; DOI=10.1016/j.neuron.2005.07.024;
RA Stauffer E.A., Scarborough J.D., Hirono M., Miller E.D., Shah K.,
RA Mercer J.A., Holt J.R., Gillespie P.G.;
RT "Fast adaptation in vestibular hair cells requires myosin-1c activity.";
RL Neuron 47:541-553(2005).
RN [16]
RP FUNCTION (ISOFORM 3), INTERACTION WITH BAZ1B, POLR1A AND SMARCA5, AND
RP SUBCELLULAR LOCATION (ISOFORM 3).
RX PubMed=16514417; DOI=10.1038/sj.embor.7400657;
RA Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G., Krueger T.,
RA Thyberg J., Scheer U., Grummt I., Oestlund Farrants A.-K.O.;
RT "The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin
RT 1 and has a role in RNA polymerase I transcription.";
RL EMBO Rep. 7:525-530(2006).
RN [17]
RP FUNCTION, AND INTERACTION WITH POLR2A.
RX PubMed=16960872; DOI=10.1002/jcb.21035;
RA Hofmann W.A., Vargas G.M., Ramchandran R., Stojiljkovic L., Goodrich J.A.,
RA de Lanerolle P.;
RT "Nuclear myosin I is necessary for the formation of the first
RT phosphodiester bond during transcription initiation by RNA polymerase II.";
RL J. Cell. Biochem. 99:1001-1009(2006).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF LYS-927 AND ARG-938.
RX PubMed=16971510; DOI=10.1091/mbc.e06-05-0449;
RA Hokanson D.E., Laakso J.M., Lin T., Sept D., Ostap E.M.;
RT "Myo1c binds phosphoinositides through a putative pleckstrin homology
RT domain.";
RL Mol. Biol. Cell 17:4856-4865(2006).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16492791; DOI=10.1073/pnas.0505685103;
RA Hokanson D.E., Ostap E.M.;
RT "Myo1c binds tightly and specifically to phosphatidylinositol 4,5-
RT bisphosphate and inositol 1,4,5-trisphosphate.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3118-3123(2006).
RN [20]
RP INDUCTION, SUBCELLULAR LOCATION (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=16957816; DOI=10.1007/s00418-006-0231-0;
RA Kahle M., Pridalova J., Spacek M., Dzijak R., Hozak P.;
RT "Nuclear myosin is ubiquitously expressed and evolutionary conserved in
RT vertebrates.";
RL Histochem. Cell Biol. 127:139-148(2007).
RN [21]
RP INTERACTION WITH CABP1 AND CIB1, AND SUBCELLULAR LOCATION.
RX PubMed=17994197; DOI=10.1007/s10974-007-9124-7;
RA Tang N., Lin T., Yang J., Foskett J.K., Ostap E.M.;
RT "CIB1 and CaBP1 bind to the myo1c regulatory domain.";
RL J. Muscle Res. Cell Motil. 28:285-291(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [23]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GLUT4, AND ACTIN-BINDING.
RX PubMed=22918957; DOI=10.1091/mbc.e12-04-0263;
RA Boguslavsky S., Chiu T., Foley K.P., Osorio-Fuentealba C., Antonescu C.N.,
RA Bayer K.U., Bilan P.J., Klip A.;
RT "Myo1c binding to submembrane actin mediates insulin-induced tethering of
RT GLUT4 vesicles.";
RL Mol. Biol. Cell 23:4065-4078(2012).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [25]
RP INTERACTION WITH LLPH.
RX PubMed=26961175; DOI=10.1038/srep22892;
RA Yu N.K., Kim H.F., Shim J., Kim S., Kim D.W., Kwak C., Sim S.E., Choi J.H.,
RA Ahn S., Yoo J., Choi S.L., Jang D.J., Lim C.S., Lee Y.S., Kang C.,
RA Choi S.Y., Kaang B.K.;
RT "A transducible nuclear/nucleolar protein, mLLP, regulates neuronal
RT morphogenesis and synaptic transmission.";
RL Sci. Rep. 6:22892-22892(2016).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails bind to membranous compartments, which then are moved
CC relative to actin filaments. Involved in glucose transporter recycling
CC in response to insulin by regulating movement of intracellular GLUT4-
CC containing vesicles to the plasma membrane. Component of the hair
CC cell's (the sensory cells of the inner ear) adaptation-motor complex.
CC Acts as a mediator of adaptation of mechanoelectrical transduction in
CC stereocilia of vestibular hair cells. Binds phosphoinositides and links
CC the actin cytoskeleton to cellular membranes.
CC {ECO:0000269|PubMed:16971510}.
CC -!- FUNCTION: [Isoform 3]: Involved in regulation of transcription.
CC Associated with transcriptional active ribosomal genes. Appears to
CC cooperate with the WICH chromatin-remodeling complex to facilitate
CC transcription. Necessary for the formation of the first phosphodiester
CC bond during transcription initiation. {ECO:0000269|PubMed:16514417}.
CC -!- SUBUNIT: Interacts (via its IQ motifs) with CABP1 and CIB1; the
CC interaction with CABP1 and CIB1 is calcium-dependent (PubMed:17994197).
CC Interacts (via tail domain) with PLEKHB1 (via PH domain); the
CC interaction is not affected by the presence or absence of calcium and
CC CALM (PubMed:15976448). Interacts with POLR1A (PubMed:16514417).
CC Interacts with POLR2A (PubMed:11030652, PubMed:16960872). Component of
CC the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF,
CC SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 (PubMed:16514417).
CC Interacts (via its IQ motifs) with CALM; this precludes interaction
CC with YWHAB (By similarity). Interacts with YWHAB; this precludes
CC interaction with CALM (By similarity). Interacts with RPS6 (By
CC similarity). Interacts with actin (By similarity). Interacts with LLPH
CC (PubMed:26961175). Interacts with GLUT4 (PubMed:22918957). Interacts
CC (via its IQ motifs) with SH3BGRL3; the interaction is dependent on
CC calcium and takes place at membrane ruffles (By similarity).
CC {ECO:0000250|UniProtKB:O00159, ECO:0000269|PubMed:11030652,
CC ECO:0000269|PubMed:15976448, ECO:0000269|PubMed:16514417,
CC ECO:0000269|PubMed:16960872, ECO:0000269|PubMed:17994197,
CC ECO:0000269|PubMed:22918957, ECO:0000269|PubMed:26961175}.
CC -!- INTERACTION:
CC Q9WTI7; Q9QYE9-1: Plekhb1; NbExp=4; IntAct=EBI-777558, EBI-1127141;
CC Q9WTI7; Q9QYE9-2: Plekhb1; NbExp=2; IntAct=EBI-777558, EBI-1127145;
CC Q9WTI7-2; P62158: CALM3; Xeno; NbExp=9; IntAct=EBI-16129068, EBI-397435;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11030652,
CC ECO:0000269|PubMed:12490950, ECO:0000269|PubMed:16492791}. Nucleus
CC {ECO:0000250|UniProtKB:O00159}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:12490950, ECO:0000269|PubMed:16492791,
CC ECO:0000269|PubMed:17994197}. Cell projection, stereocilium membrane
CC {ECO:0000250|UniProtKB:Q92002}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:22918957}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:17994197, ECO:0000269|PubMed:22918957}.
CC Note=Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles
CC and punctate regions on the cell membrane (PubMed:17994197).
CC Colocalizes in adipocytes with GLUT4 at actin-based membranes
CC (PubMed:12490950). Colocalizes with GLUT4 at insulin-induced ruffles at
CC the cell membrane (PubMed:22918957). Localizes transiently at cell
CC membrane to region known to be enriched in PIP2 (PubMed:16492791).
CC Activation of phospholipase C results in its redistribution to the
CC cytoplasm (PubMed:16492791). Colocalizes with RNA polymerase II (By
CC similarity). Translocates to nuclear speckles upon exposure to
CC inhibitors of RNA polymerase II transcription (By similarity).
CC {ECO:0000250|UniProtKB:O00159, ECO:0000269|PubMed:12490950,
CC ECO:0000269|PubMed:16492791, ECO:0000269|PubMed:17994197,
CC ECO:0000269|PubMed:22918957}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleolus
CC {ECO:0000269|PubMed:11030652, ECO:0000269|PubMed:16514417,
CC ECO:0000305|PubMed:16957816}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:16514417}. Note=Colocalizes with RNA polymerase II
CC in the nucleus (PubMed:11030652). Colocalizes with RNA polymerase I in
CC nucleoli (PubMed:16514417). In the nucleolus, is localized
CC predominantly in dense fibrillar component (DFC) and in granular
CC component (GC) (By similarity). Accumulates strongly in DFC and GC
CC during activation of transcription (By similarity). Colocalizes with
CC transcription sites (PubMed:16514417). Colocalizes in the granular
CC cortex at the periphery of the nucleolus with RPS6 (By similarity).
CC Colocalizes in nucleoplasm with RPS6 and actin that are in contact with
CC RNP particles (By similarity). Colocalizes with RPS6 at the nuclear
CC pore level (By similarity). {ECO:0000250|UniProtKB:O00159,
CC ECO:0000269|PubMed:11030652, ECO:0000269|PubMed:16514417}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9WTI7-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q9WTI7-2; Sequence=VSP_036863;
CC Name=3; Synonyms=Nuclear myosin 1, NM1;
CC IsoId=Q9WTI7-3; Sequence=VSP_036864;
CC Name=4; Synonyms=B;
CC IsoId=Q9WTI7-4; Sequence=VSP_003350;
CC -!- TISSUE SPECIFICITY: Isoform 3 is expressed in small intestine,
CC pancreas, brain, kidney, skin, heart muscle, testis, striated muscle,
CC spleen, liver and lung (at protein level). Expressed in brain, testis,
CC adrenal glands, thymus, spleen, kidney, lung, heart, cochlea and
CC vestibule. Expressed in sensory hair cells of the inner ear. Expressed
CC in adipocytes. {ECO:0000269|PubMed:12490950,
CC ECO:0000269|PubMed:16102537, ECO:0000269|PubMed:16957816,
CC ECO:0000269|PubMed:9119401}.
CC -!- INDUCTION: Up-regulated by serum. {ECO:0000269|PubMed:16957816}.
CC -!- DOMAIN: Binds directly to large unilamellar vesicles (LUVs) containing
CC phosphatidylinositol 4,5-bisphosphate (PIP2) or inositol 1,4,5-
CC trisphosphate (InsP3). The PIP2-binding site corresponds to the myosin
CC tail domain (PH-like) present in its tail domain.
CC {ECO:0000269|PubMed:16971510}.
CC -!- PTM: Isoform 2 contains a N-acetylmethionine at position 1.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to a frameshift. {ECO:0000305}.
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}.
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DR EMBL; U96723; AAC53264.1; -; mRNA.
DR EMBL; U96726; AAC60758.1; -; Genomic_DNA.
DR EMBL; AY007255; AAG02570.1; -; mRNA.
DR EMBL; AK004743; BAB23524.1; -; mRNA.
DR EMBL; AK154294; BAE32495.1; -; mRNA.
DR EMBL; AK155530; BAE33311.1; -; mRNA.
DR EMBL; AK171107; BAE42253.1; -; mRNA.
DR EMBL; AL591440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12832.1; -; Genomic_DNA.
DR EMBL; CH466596; EDL12833.1; -; Genomic_DNA.
DR EMBL; BC021481; AAH21481.1; -; mRNA.
DR EMBL; X99638; CAA67956.1; -; mRNA.
DR EMBL; CF615767; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS25054.1; -. [Q9WTI7-2]
DR CCDS; CCDS36228.1; -. [Q9WTI7-3]
DR CCDS; CCDS88191.1; -. [Q9WTI7-1]
DR PIR; B45438; B45438.
DR PIR; H75634; H75634.
DR RefSeq; NP_001074243.1; NM_001080774.1. [Q9WTI7-2]
DR RefSeq; NP_001074244.1; NM_001080775.1. [Q9WTI7-3]
DR RefSeq; NP_032685.1; NM_008659.3. [Q9WTI7-2]
DR RefSeq; XP_006532492.1; XM_006532429.3.
DR PDB; 4R8G; X-ray; 3.50 A; E=733-1063.
DR PDBsum; 4R8G; -.
DR AlphaFoldDB; Q9WTI7; -.
DR SMR; Q9WTI7; -.
DR BioGRID; 201664; 153.
DR ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex. [Q9WTI7-3]
DR CORUM; Q9WTI7; -.
DR DIP; DIP-35498N; -.
DR IntAct; Q9WTI7; 148.
DR MINT; Q9WTI7; -.
DR STRING; 10090.ENSMUSP00000104069; -.
DR GlyGen; Q9WTI7; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9WTI7; -.
DR PhosphoSitePlus; Q9WTI7; -.
DR SwissPalm; Q9WTI7; -.
DR EPD; Q9WTI7; -.
DR jPOST; Q9WTI7; -.
DR MaxQB; Q9WTI7; -.
DR PaxDb; 10090-ENSMUSP00000104069; -.
DR PeptideAtlas; Q9WTI7; -.
DR ProteomicsDB; 286126; -. [Q9WTI7-1]
DR ProteomicsDB; 286127; -. [Q9WTI7-2]
DR ProteomicsDB; 286128; -. [Q9WTI7-3]
DR ProteomicsDB; 286129; -. [Q9WTI7-4]
DR Pumba; Q9WTI7; -.
DR Antibodypedia; 953; 200 antibodies from 27 providers.
DR DNASU; 17913; -.
DR Ensembl; ENSMUST00000069057.13; ENSMUSP00000070388.7; ENSMUSG00000017774.20. [Q9WTI7-2]
DR Ensembl; ENSMUST00000102504.10; ENSMUSP00000099562.4; ENSMUSG00000017774.20. [Q9WTI7-2]
DR Ensembl; ENSMUST00000102505.10; ENSMUSP00000099563.4; ENSMUSG00000017774.20. [Q9WTI7-1]
DR Ensembl; ENSMUST00000108431.3; ENSMUSP00000104069.3; ENSMUSG00000017774.20. [Q9WTI7-3]
DR GeneID; 17913; -.
DR KEGG; mmu:17913; -.
DR UCSC; uc007kem.1; mouse. [Q9WTI7-1]
DR UCSC; uc007keo.1; mouse. [Q9WTI7-3]
DR AGR; MGI:106612; -.
DR CTD; 4641; -.
DR MGI; MGI:106612; Myo1c.
DR VEuPathDB; HostDB:ENSMUSG00000017774; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000157915; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; Q9WTI7; -.
DR OrthoDB; 1094820at2759; -.
DR PhylomeDB; Q9WTI7; -.
DR TreeFam; TF312960; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR BioGRID-ORCS; 17913; 3 hits in 80 CRISPR screens.
DR ChiTaRS; Myo1c; mouse.
DR PRO; PR:Q9WTI7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WTI7; Protein.
DR Bgee; ENSMUSG00000017774; Expressed in right lung and 256 other cell types or tissues.
DR ExpressionAtlas; Q9WTI7; baseline and differential.
DR Genevisible; Q9WTI7; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0110016; C:B-WICH complex; ISO:ComplexPortal.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031941; C:filamentous actin; ISO:MGI.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; NAS:ComplexPortal.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0032420; C:stereocilium; IDA:MGI.
DR GO; GO:0032421; C:stereocilium bundle; ISO:MGI.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0000146; F:microfilament motor activity; EXP:Reactome.
DR GO; GO:0005543; F:phospholipid binding; TAS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to type II interferon; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; NAS:ComplexPortal.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0038089; P:positive regulation of cell migration by vascular endothelial growth factor signaling pathway; ISO:MGI.
DR GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; IDA:MGI.
DR GO; GO:0035066; P:positive regulation of histone acetylation; NAS:ComplexPortal.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:MGI.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; NAS:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:ComplexPortal.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:ComplexPortal.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; ISO:MGI.
DR GO; GO:0006612; P:protein targeting to membrane; ISO:MGI.
DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0030050; P:vesicle transport along actin filament; IDA:MGI.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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 PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF255; UNCONVENTIONAL MYOSIN-IC; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW ATP-binding; Calmodulin-binding; Cell membrane; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Membrane; Methylation; Motor protein; Myosin;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1063
FT /note="Unconventional myosin-Ic"
FT /id="PRO_0000123446"
FT DOMAIN 47..731
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 734..757
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 758..786
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 885..1059
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 608..630
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 139..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 192..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 383
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00159"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00159"
FT MOD_RES 486
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63355"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63355"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63355"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9119401,
FT ECO:0000303|PubMed:9182797"
FT /id="VSP_036863"
FT VAR_SEQ 1..25
FT /note="MALQVELIPTGEIIRVVHPHRPCKL -> MRYRAS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11030652,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036864"
FT VAR_SEQ 932..1063
FT /note="GYKPRPRQLLLTPSAVVIVEDAKVKQRIDYANLTGISVSSLSDSLFVLHVQR
FT EDNKQKGDVVLQSDHVIETLTKTALSADRVNNININQGSITFAGGPGRDGIIDFTSGSE
FT LLITKAKNGHLAVVAPRLNSR -> VTSLAPGSCCSRPVLWSLWRMLKSSRELIMPT
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9182797"
FT /id="VSP_003350"
FT MUTAGEN 927
FT /note="K->A: Inhibits binding to PIP2 and disrupts membrane
FT binding."
FT /evidence="ECO:0000269|PubMed:16971510"
FT MUTAGEN 938
FT /note="R->A: Inhibits binding to PIP2 and disrupts membrane
FT binding."
FT /evidence="ECO:0000269|PubMed:16971510"
FT CONFLICT 69..70
FT /note="RR -> GG (in Ref. 7; CAA67956)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..99
FT /note="SRQ -> RRK (in Ref. 7; CAA67956)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="E -> G (in Ref. 3; BAE33311)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="V -> I (in Ref. 3; BAE33311)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="T -> A (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="C -> F (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..287
FT /note="VM -> LL (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="R -> A (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..403
FT /note="LAS -> VPA (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="Q -> R (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 517..519
FT /note="VKP -> IKH (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="M -> T (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="S -> G (in Ref. 9)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="Q -> R (in Ref. 7; CAA67956)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="R -> G (in Ref. 7; CAA67956)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="E -> D (in Ref. 7; CAA67956)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="T -> A (in Ref. 3; BAE33311)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9WTI7-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250"
FT MOD_RES Q9WTI7-3:10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1063 AA; 121944 MW; 494A31B8634A1AF9 CRC64;
MALQVELIPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD FVLLENFTSE
AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH MERYRGVSFY EVPPHLFAVA
DTVYRALRTE RRDQAVMISG ESGAGKTEAT KRLLQFYAET CPAPERGGAV RDRLLQSNPV
LEAFGNAKTL RNDNSSRFGK YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHVF
YQLLEGGEEE TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVMRKA LSVIDFTEDE
VEDLLSIVAS VLHLGNIHFA ADEDSNAQVT TENQLKYLTR LLGVEGTTLR EALTHRKIIA
KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVRKINRS LASKDAESPS WRSTTVLGLL
DIYGFEVFQH NSFEQFCINY CNEKLQQLFI ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC
DLVEEKFKGI ISILDEECLR PGEATDLTFL EKLEDTVKPH PHFLTHKLAD QKTRKSLDRG
EFRLLHYAGE VTYSVTGFLD KNNDLLFRNL KETMCSSMNP IMAQCFDKSE LSDKKRPETV
ATQFKMSLLQ LVEILRSKEP AYIRCIKPND AKQPGRFDEV LIRHQVKYLG LMENLRVRRA
GFAYRRKYEA FLQRYKSLCP ETWPMWAGRP QDGVAVLVRH LGYKPEEYKM GRTKIFIRFP
KTLFATEDSL EVRRQSLATK IQAAWRGFHW RQKFLRVKRS AICIQSWWRG TLGRRKAAKR
KWAAQTIRRL IRGFILRHSP RCPENAFFLD HVRASFLLNL RRQLPRNVLD TSWPTPPPAL
REASELLREL CMKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR
LGTEEISPRV LQSLGSEPIQ YAVPVVKYDR KGYKPRPRQL LLTPSAVVIV EDAKVKQRID
YANLTGISVS SLSDSLFVLH VQREDNKQKG DVVLQSDHVI ETLTKTALSA DRVNNININQ
GSITFAGGPG RDGIIDFTSG SELLITKAKN GHLAVVAPRL NSR
//
