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MYO1C_MOUSE
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   03-AUG-2022, entry version 196.
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   INTERACTION WITH BAZ1B, POLR1A AND SMARCA5, AND SUBCELLULAR LOCATION.
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, 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 is 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.
CC   -!- SUBUNIT: Interacts (via its IQ motifs) with CALM; this precludes
CC       interaction with YWHAB. Interacts with YWHAB; this precludes
CC       interaction with CALM. Interacts with RPS6 (By similarity). Interacts
CC       with actin filaments. Interacts (via its IQ motifs) with CABP1 and
CC       CIB1; the interaction with CABP1 and CIB1 is calcium-dependent.
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. Interacts with POLR1A and POLR2A. Component of the B-WICH
CC       complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK,
CC       MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with GLUT4. Interacts with
CC       LLPH (PubMed:26961175). {ECO:0000250, 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. Cell membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Cell projection, stereocilium membrane.
CC       Cytoplasmic vesicle. Cell projection, ruffle. Note=Colocalizes with
CC       CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on
CC       the cell membrane. Colocalizes in adipocytes with GLUT4 at actin-based
CC       membranes. Colocalizes with GLUT4 at insulin-induced ruffles at the
CC       cell membrane. Localizes transiently at cell membrane to region known
CC       to be enriched in PIP2. Activation of phospholipase C results in its
CC       redistribution to the cytoplasm.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleolus. Nucleus,
CC       nucleoplasm {ECO:0000250}. Nucleus, nuclear pore complex {ECO:0000250}.
CC       Note=In the nucleolus, is localized predominantly in dense fibrillar
CC       component (DFC) and in granular component (GC). Accumulates strongly in
CC       DFC and GC during activation of transcription. Colocalizes with
CC       transcription sites. Colocalizes in the granular cortex at the
CC       periphery of the nucleolus with RPS6. Colocalizes in nucleoplasm with
CC       RPS6 and actin that are in contact with RNP particles. Colocalizes with
CC       RPS6 at the nuclear pore level (By similarity). Colocalizes with RNA
CC       polymerase II in the nucleus. Colocalizes with RNA polymerase I in
CC       nucleoli. {ECO:0000250}.
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; 152.
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   iPTMnet; Q9WTI7; -.
DR   PhosphoSitePlus; Q9WTI7; -.
DR   SwissPalm; Q9WTI7; -.
DR   EPD; Q9WTI7; -.
DR   jPOST; Q9WTI7; -.
DR   MaxQB; Q9WTI7; -.
DR   PaxDb; Q9WTI7; -.
DR   PeptideAtlas; Q9WTI7; -.
DR   PRIDE; Q9WTI7; -.
DR   ProteomicsDB; 286126; -. [Q9WTI7-1]
DR   ProteomicsDB; 286127; -. [Q9WTI7-2]
DR   ProteomicsDB; 286128; -. [Q9WTI7-3]
DR   ProteomicsDB; 286129; -. [Q9WTI7-4]
DR   Antibodypedia; 953; 177 antibodies from 27 providers.
DR   DNASU; 17913; -.
DR   Ensembl; ENSMUST00000069057; ENSMUSP00000070388; ENSMUSG00000017774. [Q9WTI7-2]
DR   Ensembl; ENSMUST00000102504; ENSMUSP00000099562; ENSMUSG00000017774. [Q9WTI7-2]
DR   Ensembl; ENSMUST00000102505; ENSMUSP00000099563; ENSMUSG00000017774. [Q9WTI7-1]
DR   Ensembl; ENSMUST00000108431; ENSMUSP00000104069; ENSMUSG00000017774. [Q9WTI7-3]
DR   GeneID; 17913; -.
DR   KEGG; mmu:17913; -.
DR   UCSC; uc007kem.1; mouse. [Q9WTI7-1]
DR   UCSC; uc007keo.1; mouse. [Q9WTI7-3]
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; 122881at2759; -.
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 74 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 252 other 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:MGI.
DR   GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR   GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; 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:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IC:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
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: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:0008022; F:protein C-terminus binding; IPI: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 interferon-gamma; IDA:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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; IC: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; IC:ComplexPortal.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI.
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; 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; 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; SSF52540; 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; mRNA transport;
KW   Myosin; Nuclear pore complex; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Repeat; Translocation; Transport.
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
 
 
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