MYH9_MOUSE
ID MYH9_MOUSE Reviewed; 1960 AA.
AC Q8VDD5; Q3UHT9; Q3UHU4; Q6KAN6; Q811I2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Myosin-9;
DE AltName: Full=Cellular myosin heavy chain, type A;
DE AltName: Full=Myosin heavy chain 9;
DE AltName: Full=Myosin heavy chain, non-muscle IIa;
DE AltName: Full=Non-muscle myosin heavy chain A;
DE Short=NMMHC-A;
DE AltName: Full=Non-muscle myosin heavy chain IIa;
DE Short=NMMHC II-a;
DE Short=NMMHC-IIA;
GN Name=Myh9;
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 [MRNA].
RX PubMed=11943476; DOI=10.1016/s0378-1119(02)00455-9;
RA D'Apolito M., Guarnieri V., Boncristiano M., Zelante L., Savoia A.;
RT "Cloning of the murine non-muscle myosin heavy chain IIA gene ortholog of
RT human MYH9 responsible for May-Hegglin, Sebastian, Fechtner, and Epstein
RT syndromes.";
RL Gene 286:215-222(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Amnion, Brain, Embryo, Embryonic liver, and Placenta;
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-64; 83-102; 126-139; 144-159; 186-199; 210-225;
RP 241-261; 273-299; 302-355; 374-387; 408-419; 476-494; 518-536; 564-613;
RP 618-637; 645-651; 663-678; 683-702; 712-731; 738-755; 765-775; 802-810;
RP 815-821; 834-850; 910-923; 931-938; 941-959; 975-989; 1001-1014; 1023-1035;
RP 1052-1075; 1081-1091; 1106-1124; 1136-1162; 1166-1174; 1182-1191;
RP 1194-1210; 1227-1234; 1249-1260; 1278-1295; 1302-1322; 1343-1353;
RP 1358-1370; 1393-1400; 1405-1413; 1418-1441; 1445-1454; 1484-1492;
RP 1504-1518; 1529-1566; 1593-1602; 1614-1620; 1659-1669; 1677-1694;
RP 1698-1724; 1731-1751; 1754-1770; 1792-1802; 1807-1828; 1844-1855;
RP 1857-1867; 1877-1888; 1899-1912 AND 1923-1932, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic fibroblast;
RA Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.;
RL Submitted (MAR-2008) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 626-1960.
RC STRAIN=ICR; TISSUE=Embryonic tail;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1066-1960.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DDR1, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=19401332; DOI=10.1242/jcs.046219;
RA Huang Y., Arora P., McCulloch C.A., Vogel W.F.;
RT "The collagen receptor DDR1 regulates cell spreading and motility by
RT associating with myosin IIA.";
RL J. Cell Sci. 122:1637-1646(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1114; THR-1939 AND SER-1943,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [17]
RP INTERACTION WITH RASIP1.
RX PubMed=21396893; DOI=10.1016/j.devcel.2011.02.010;
RA Xu K., Sacharidou A., Fu S., Chong D.C., Skaug B., Chen Z.J., Davis G.E.,
RA Cleaver O.;
RT "Blood vessel tubulogenesis requires Rasip1 regulation of GTPase
RT signaling.";
RL Dev. Cell 20:526-539(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-8; LYS-299; LYS-613;
RP LYS-860; LYS-975; LYS-1024; LYS-1249; LYS-1459; LYS-1793; LYS-1802 AND
RP LYS-1845, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-850 AND LYS-1669,
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS 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 [19]
RP SUBUNIT, DEVELOPMENTAL STAGE, AND UBIQUITINATION.
RX PubMed=27331610; DOI=10.7554/elife.15258;
RA Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
RA Groves A.K., Bellen H.J.;
RT "The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in
RT the auditory organs of Drosophila and mammals.";
RL Elife 5:E15258-E15258(2016).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=31118423; DOI=10.1038/s41467-019-10171-7;
RA Vogt E.J., Tokuhiro K., Guo M., Dale R., Yang G., Shin S.W., Movilla M.J.,
RA Shroff H., Dean J.;
RT "Anchoring cortical granules in the cortex ensures trafficking to the
RT plasma membrane for post-fertilization exocytosis.";
RL Nat. Commun. 10:2271-2271(2019).
CC -!- FUNCTION: Cellular myosin that appears to play a role in cytokinesis,
CC cell shape, and specialized functions such as secretion and capping
CC (PubMed:19401332). Required for cortical actin clearance prior to
CC oocyte exocytosis (PubMed:31118423). Promotes cell motility in
CC conjunction with S100A4 (By similarity). During cell spreading, plays
CC an important role in cytoskeleton reorganization, focal contact
CC formation (in the margins but not the central part of spreading cells),
CC and lamellipodial retraction; this function is mechanically antagonized
CC by MYH10 (By similarity). {ECO:0000250|UniProtKB:P35579,
CC ECO:0000269|PubMed:19401332, ECO:0000269|PubMed:31118423}.
CC -!- SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy chain
CC subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory
CC light chain subunits (MLC-2). Interacts with RASIP1 (PubMed:21396893).
CC Interacts with DDR1 (PubMed:19401332). Interacts with PDLIM2 (By
CC similarity). Interacts with SVIL (By similarity). Interacts with HTRA3
CC (By similarity). Interacts with Myo7a (PubMed:27331610). Interacts with
CC CFAP95 (By similarity). Interacts with LIMCH1; independently of the
CC integration of MYH9 into the myosin complex (By similarity). Interacts
CC with RAB3A (By similarity). Interacts with ZBED4 (By similarity).
CC Interacts with S100A4; this interaction increases cell motility.
CC {ECO:0000250|UniProtKB:P35579, ECO:0000250|UniProtKB:Q62812,
CC ECO:0000269|PubMed:19401332, ECO:0000269|PubMed:21396893,
CC ECO:0000269|PubMed:27331610}.
CC -!- INTERACTION:
CC Q8VDD5; Q923J1: Trpm7; NbExp=4; IntAct=EBI-400906, EBI-8010314;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19401332}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:19401332, ECO:0000269|PubMed:31118423}. Cytoplasmic
CC vesicle, secretory vesicle, Cortical granule
CC {ECO:0000269|PubMed:31118423}. Note=Colocalizes with actin filaments at
CC lamellipodia margins and at the leading edge of migrating cells (By
CC similarity). In retinal pigment epithelial cells, predominantly
CC localized to stress fiber-like structures with some localization to
CC cytoplasmic puncta (By similarity). {ECO:0000250|UniProtKB:P35579}.
CC -!- DEVELOPMENTAL STAGE: In neonatal mouse cochlea, weak levels of
CC expression in both hair cells and supporting cells (at protein level).
CC In the cochlea of six day old mice, expression is restricted to hair
CC cell sterocilia (at protein level). {ECO:0000269|PubMed:27331610}.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- PTM: Ubiquitination. {ECO:0000269|PubMed:27331610}.
CC -!- DISRUPTION PHENOTYPE: Reduced litter size and increased polyspermy in
CC the perivitelline space following fertilization.
CC {ECO:0000269|PubMed:31118423}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE27768.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ312390; CAC85955.1; -; mRNA.
DR EMBL; AK147203; BAE27761.1; -; mRNA.
DR EMBL; AK147206; BAE27763.1; -; mRNA.
DR EMBL; AK147208; BAE27765.1; -; mRNA.
DR EMBL; AK147209; BAE27766.1; -; mRNA.
DR EMBL; AK147210; BAE27767.1; -; mRNA.
DR EMBL; AK147211; BAE27768.1; ALT_INIT; mRNA.
DR EMBL; AK147215; BAE27772.1; -; mRNA.
DR EMBL; AK147216; BAE27773.1; -; mRNA.
DR EMBL; AK147221; BAE27776.1; -; mRNA.
DR EMBL; AK147222; BAE27777.1; -; mRNA.
DR EMBL; AK147223; BAE27778.1; -; mRNA.
DR EMBL; AK147233; BAE27783.1; -; mRNA.
DR EMBL; AK147235; BAE27785.1; -; mRNA.
DR EMBL; AK147296; BAE27829.1; -; mRNA.
DR EMBL; AK147407; BAE27894.1; -; mRNA.
DR EMBL; AK147430; BAE27906.1; -; mRNA.
DR EMBL; AL583886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK131171; BAD21421.1; -; mRNA.
DR EMBL; BC044834; AAH44834.1; -; mRNA.
DR CCDS; CCDS27605.1; -.
DR RefSeq; NP_071855.2; NM_022410.3.
DR AlphaFoldDB; Q8VDD5; -.
DR SMR; Q8VDD5; -.
DR BioGRID; 201650; 258.
DR DIP; DIP-29546N; -.
DR IntAct; Q8VDD5; 215.
DR MINT; Q8VDD5; -.
DR STRING; 10090.ENSMUSP00000016771; -.
DR GlyConnect; 2523; 1 N-Linked glycan (1 site).
DR GlyGen; Q8VDD5; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q8VDD5; -.
DR PhosphoSitePlus; Q8VDD5; -.
DR SwissPalm; Q8VDD5; -.
DR CPTAC; non-CPTAC-3994; -.
DR EPD; Q8VDD5; -.
DR jPOST; Q8VDD5; -.
DR MaxQB; Q8VDD5; -.
DR PaxDb; Q8VDD5; -.
DR PeptideAtlas; Q8VDD5; -.
DR PRIDE; Q8VDD5; -.
DR ProteomicsDB; 293598; -.
DR Antibodypedia; 887; 494 antibodies from 42 providers.
DR DNASU; 17886; -.
DR Ensembl; ENSMUST00000016771; ENSMUSP00000016771; ENSMUSG00000022443.
DR GeneID; 17886; -.
DR KEGG; mmu:17886; -.
DR UCSC; uc007woc.2; mouse.
DR CTD; 4627; -.
DR MGI; MGI:107717; Myh9.
DR VEuPathDB; HostDB:ENSMUSG00000022443; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000155632; -.
DR HOGENOM; CLU_000192_4_2_1; -.
DR InParanoid; Q8VDD5; -.
DR OMA; NAHNEAQ; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; Q8VDD5; -.
DR TreeFam; TF333601; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR BioGRID-ORCS; 17886; 24 hits in 76 CRISPR screens.
DR ChiTaRS; Myh9; mouse.
DR PRO; PR:Q8VDD5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8VDD5; protein.
DR Bgee; ENSMUSG00000022443; Expressed in aortic valve and 270 other tissues.
DR ExpressionAtlas; Q8VDD5; baseline and differential.
DR Genevisible; Q8VDD5; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0042641; C:actomyosin; ISO:MGI.
DR GO; GO:0005826; C:actomyosin contractile ring; ISS:UniProtKB.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR GO; GO:0060473; C:cortical granule; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR GO; GO:0016459; C:myosin complex; IDA:MGI.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IDA:MGI.
DR GO; GO:0097513; C:myosin II filament; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0001931; C:uropod; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISS:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0060471; P:cortical granule exocytosis; IMP:UniProtKB.
DR GO; GO:0032506; P:cytokinetic process; ISS:UniProtKB.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; IDA:MGI.
DR GO; GO:0001768; P:establishment of T cell polarity; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0032418; P:lysosome localization; ISO:MGI.
DR GO; GO:0000212; P:meiotic spindle organization; IDA:MGI.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; IMP:MGI.
DR GO; GO:1903919; P:negative regulation of actin filament severing; IMP:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; ISO:MGI.
DR GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
DR GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
DR GO; GO:1905684; P:regulation of plasma membrane repair; ISO:MGI.
DR GO; GO:0032796; P:uropod organization; IMP:MGI.
DR Gene3D; 2.30.30.360; -; 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; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 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; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; Cell adhesion;
KW Cell shape; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Methylation; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:23806337"
FT CHAIN 2..1960
FT /note="Myosin-9"
FT /id="PRO_0000123417"
FT DOMAIN 27..77
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 81..776
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 779..808
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 2..838
FT /note="Mediates interaction with LIMCH1"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT REGION 654..676
FT /note="Actin-binding"
FT REGION 1035..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1939..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 841..1926
FT /evidence="ECO:0000255"
FT COMPBIAS 1117..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:23806337"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 11
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 613
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 754
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 850
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 860
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 975
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1024
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1357
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1404
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1410
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1459
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1638
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1669
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1793
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1802
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1845
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1923
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1939
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 1943
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17208939, ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CONFLICT 1733
FT /note="Q -> L (in Ref. 1; CAC85955)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1960 AA; 226372 MW; AAAC0E83A0A4F24A CRC64;
MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSSKNG FEPASLKEEV GEEAIVELVE
NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LKERYYSGLI YTYSGLFCVV
INPYKNLPIY SEEIVEMYKG KKRHEMPPHI YAITDTAYRS MMQDREDQSI LCTGESGAGK
TENTKKVIQY LAHVASSHKS KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR
INFDVNGYIV GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEDEQMGLL RVISGVLQLG NIAFKKERNT
DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY VQKAQTKEQA DFAIEALAKA
TYERMFRWLV LRINKALDKT KRQGASFIGI LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF
NHTMFILEQE EYQREGIEWN FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK
SFVEKVVQEQ GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY KEQLAKLMAT
LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN RVVFQEFRQR
YEILTPNSIP KGFMDGKQAC VLMIKALELD SNLYRIGQSK VFFRAGVLAH LEEERDLKIT
DVIIGFQACC RGYLARKAFA KRQQQLTAMK VLQRNCAAYL RLRNWQWWRL FTKVKPLLNS
IRHEDELLAK EAELTKVREK HLAAENRLTE METMQSQLMA EKLQLQEQLQ AETELCAEAE
ELRARLTAKK QELEEICHDL EARVEEEEER CQYLQAEKKK MQQNIQELEE QLEEEESARQ
KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR VAEFTTNLME EEEKSKSLAK
LKNKHEAMIT DLEERLRREE KQRQELEKTR RKLEGDSTDL SDQIAELQAQ IAELKMQLAK
KEEELQAALA RVEEEAAQKN MALKKIRELE TQISELQEDL ESERASRNKA EKQKRDLGEE
LEALKTELED TLDSTAAQQE LRSKREQEVS ILKKTLEDEA KTHEAQIQEM RQKHSQAVEE
LADQLEQTKR VKATLEKAKQ TLENERGELA NEVKALLQGK GDSEHKRKKV EAQLQELQVK
FSEGERVRTE LADKVTKLQV ELDSVTGLLS QSDSKSSKLT KDFSALESQL QDTQELLQEE
NRQKLSLSTK LKQMEDEKNS FREQLEEEEE AKRNLEKQIA TLHAQVTDMK KKMEDGVGCL
ETAEEAKRRL QKDLEGLSQR LEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSVSNLE
KKQKKFDQLL AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA TEDAKLRLEV
NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED ERKQRSMAMA ARKKLEMDLK
DLEAHIDTAN KNREEAIKQL RKLQAQMKDC MRELDDTRAS REEILAQAKE NEKKLKSMEA
EMIQLQEELA AAERAKRQAQ QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE
EQGNTELIND RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KAKLQEMESA
VKSKYKASIA ALEAKIAQLE EQLDNETKER QAASKQVRRT EKKLKDVLLQ VEDERRNAEQ
FKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL EDATETADAM NREVSSLKNK
LRRGDLPFVV TRRIVRKGTG DCSDEEVDGK ADGADAKAAE
