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Myosin-9 (Cellular myosin heavy chain, type A) (Myosin heavy chain 9) (Myosin heavy chain, non-muscle IIa) (Non-muscle myosin heavy chain A) (NMMHC-A) (Non-muscle myosin heavy chain IIa) (NMMHC II-a) (NMMHC-IIA)

 MYH9_MOUSE              Reviewed;        1960 AA.
Q8VDD5; Q3UHT9; Q3UHU4; Q6KAN6; Q811I2;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
02-SEP-2008, sequence version 4.
27-SEP-2017, entry version 148.
RecName: Full=Myosin-9;
AltName: Full=Cellular myosin heavy chain, type A;
AltName: Full=Myosin heavy chain 9;
AltName: Full=Myosin heavy chain, non-muscle IIa;
AltName: Full=Non-muscle myosin heavy chain A;
Short=NMMHC-A;
AltName: Full=Non-muscle myosin heavy chain IIa;
Short=NMMHC II-a;
Short=NMMHC-IIA;
Name=Myh9;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11943476; DOI=10.1016/S0378-1119(02)00455-9;
D'Apolito M., Guarnieri V., Boncristiano M., Zelante L., Savoia A.;
"Cloning of the murine non-muscle myosin heavy chain IIA gene ortholog
of human MYH9 responsible for May-Hegglin, Sebastian, Fechtner, and
Epstein syndromes.";
Gene 286:215-222(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Amnion, Brain, Embryo, Embryonic liver, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
PROTEIN SEQUENCE OF 2-64; 83-102; 126-139; 144-159; 186-199; 210-225;
241-261; 273-299; 302-355; 374-387; 408-419; 476-494; 518-536;
564-613; 618-637; 645-651; 663-678; 683-702; 712-731; 738-755;
765-775; 802-810; 815-821; 834-850; 910-923; 931-938; 941-959;
975-989; 1001-1014; 1023-1035; 1052-1075; 1081-1091; 1106-1124;
1136-1162; 1166-1174; 1182-1191; 1194-1210; 1227-1234; 1249-1260;
1278-1295; 1302-1322; 1343-1353; 1358-1370; 1393-1400; 1405-1413;
1418-1441; 1445-1454; 1484-1492; 1504-1518; 1529-1566; 1593-1602;
1614-1620; 1659-1669; 1677-1694; 1698-1724; 1731-1751; 1754-1770;
1792-1802; 1807-1828; 1844-1855; 1857-1867; 1877-1888; 1899-1912 AND
1923-1932, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic fibroblast;
Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.;
Submitted (MAR-2008) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 626-1960.
STRAIN=ICR; TISSUE=Embryonic tail;
PubMed=15449545; DOI=10.1093/dnares/11.2.127;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of FLJ genes:
the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
DNA Res. 11:127-135(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1066-1960.
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
"Mitochondrial phosphoproteome revealed by an improved IMAC method and
MS/MS/MS.";
Mol. Cell. Proteomics 6:669-676(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DDR1, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19401332; DOI=10.1242/jcs.046219;
Huang Y., Arora P., McCulloch C.A., Vogel W.F.;
"The collagen receptor DDR1 regulates cell spreading and motility by
associating with myosin IIA.";
J. Cell Sci. 122:1637-1646(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1114; THR-1939 AND
SER-1943, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[17]
INTERACTION WITH RASIP1.
PubMed=21396893; DOI=10.1016/j.devcel.2011.02.010;
Xu K., Sacharidou A., Fu S., Chong D.C., Skaug B., Chen Z.J.,
Davis G.E., Cleaver O.;
"Blood vessel tubulogenesis requires Rasip1 regulation of GTPase
signaling.";
Dev. Cell 20:526-539(2011).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-8; LYS-299; LYS-613;
LYS-860; LYS-975; LYS-1024; LYS-1249; LYS-1459; LYS-1793; LYS-1802 AND
LYS-1845, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-850 AND
LYS-1669, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[19]
SUBUNIT, DEVELOPMENTAL STAGE, AND UBIQUITINATION.
PubMed=27331610; DOI=10.7554/eLife.15258;
Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
Groves A.K., Bellen H.J.;
"The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder
proteins in the auditory organs of Drosophila and mammals.";
Elife 5:E15258-E15258(2016).
-!- FUNCTION: During cell spreading, plays an important role in
cytoskeleton reorganization, focal contacts formation (in the
margins but not the central part of spreading cells), and
lamellipodial retraction; this function is mechanically
antagonized by MYH10 (By similarity). Cellular myosin that appears
to play a role in cytokinesis, cell shape, and specialized
functions such as secretion and capping. {ECO:0000250,
ECO:0000269|PubMed:19401332}.
-!- SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy
chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
regulatory light chain subunits (MLC-2). Interacts with RASIP1
(PubMed:21396893). Interacts with DDR1 (PubMed:19401332).
Interacts with SLC6A4 (By similarity). Interacts with PDLIM2 (By
similarity). Interacts with SVIL (By similarity). Interacts with
HTRA3 (By similarity). Interacts with Myo7a (PubMed:27331610).
Interacts with C9orf135 homolog (By similarity).
{ECO:0000250|UniProtKB:P35579, ECO:0000250|UniProtKB:Q62812,
ECO:0000269|PubMed:19401332, ECO:0000269|PubMed:21396893,
ECO:0000269|PubMed:27331610}.
-!- INTERACTION:
Q923J1:Trpm7; NbExp=4; IntAct=EBI-400906, EBI-8010314;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:19401332}. Cytoplasm, cell cortex
{ECO:0000269|PubMed:19401332}. Note=Colocalizes with actin
filaments at lamellipodia margins and at the leading edge of
migrating cells (By similarity). In retinal pigment epthelial
cells, predominantly localized to stress fiber-like structures
with some localization to cytoplasmic puncta (By similarity).
{ECO:0000250|UniProtKB:P35579}.
-!- DEVELOPMENTAL STAGE: In neonatal mouse cochlea, weak levels of
expresion in both hair cells and supporting cells (at protein
level). In the cochlea of six day old mice, expression is
restricted to hair cell sterocilia (at protein level).
{ECO:0000269|PubMed:27331610}.
-!- DOMAIN: The rodlike tail sequence is highly repetitive, showing
cycles of a 28-residue repeat pattern composed of 4 heptapeptides,
characteristic for alpha-helical coiled coils.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Ubiquitination. {ECO:0000269|PubMed:27331610}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE27768.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AJ312390; CAC85955.1; -; mRNA.
EMBL; AK147203; BAE27761.1; -; mRNA.
EMBL; AK147206; BAE27763.1; -; mRNA.
EMBL; AK147208; BAE27765.1; -; mRNA.
EMBL; AK147209; BAE27766.1; -; mRNA.
EMBL; AK147210; BAE27767.1; -; mRNA.
EMBL; AK147211; BAE27768.1; ALT_INIT; mRNA.
EMBL; AK147215; BAE27772.1; -; mRNA.
EMBL; AK147216; BAE27773.1; -; mRNA.
EMBL; AK147221; BAE27776.1; -; mRNA.
EMBL; AK147222; BAE27777.1; -; mRNA.
EMBL; AK147223; BAE27778.1; -; mRNA.
EMBL; AK147233; BAE27783.1; -; mRNA.
EMBL; AK147235; BAE27785.1; -; mRNA.
EMBL; AK147296; BAE27829.1; -; mRNA.
EMBL; AK147407; BAE27894.1; -; mRNA.
EMBL; AK147430; BAE27906.1; -; mRNA.
EMBL; AL583886; CAM23428.1; -; Genomic_DNA.
EMBL; AK131171; BAD21421.1; -; mRNA.
EMBL; BC044834; AAH44834.1; -; mRNA.
CCDS; CCDS27605.1; -.
RefSeq; NP_071855.2; NM_022410.3.
UniGene; Mm.29677; -.
ProteinModelPortal; Q8VDD5; -.
SMR; Q8VDD5; -.
BioGrid; 201650; 206.
DIP; DIP-29546N; -.
IntAct; Q8VDD5; 210.
MINT; MINT-2524850; -.
STRING; 10090.ENSMUSP00000016771; -.
iPTMnet; Q8VDD5; -.
PhosphoSitePlus; Q8VDD5; -.
SwissPalm; Q8VDD5; -.
EPD; Q8VDD5; -.
MaxQB; Q8VDD5; -.
PaxDb; Q8VDD5; -.
PeptideAtlas; Q8VDD5; -.
PRIDE; Q8VDD5; -.
Ensembl; ENSMUST00000016771; ENSMUSP00000016771; ENSMUSG00000022443.
GeneID; 17886; -.
KEGG; mmu:17886; -.
UCSC; uc007woc.2; mouse.
CTD; 4627; -.
MGI; MGI:107717; Myh9.
eggNOG; KOG0161; Eukaryota.
eggNOG; COG5022; LUCA.
GeneTree; ENSGT00760000118919; -.
HOGENOM; HOG000173958; -.
HOVERGEN; HBG004704; -.
InParanoid; Q8VDD5; -.
KO; K10352; -.
OMA; GDSEHKR; -.
OrthoDB; EOG091G009J; -.
PhylomeDB; Q8VDD5; -.
TreeFam; TF333601; -.
Reactome; R-MMU-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
ChiTaRS; Myh9; mouse.
PRO; PR:Q8VDD5; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022443; -.
CleanEx; MM_MYH9; -.
ExpressionAtlas; Q8VDD5; baseline and differential.
Genevisible; Q8VDD5; MM.
GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
GO; GO:0042641; C:actomyosin; ISO:MGI.
GO; GO:0005826; C:actomyosin contractile ring; ISS:UniProtKB.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IDA:MGI.
GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0008305; C:integrin complex; IEA:Ensembl.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0016459; C:myosin complex; IDA:MGI.
GO; GO:0016460; C:myosin II complex; IDA:MGI.
GO; GO:0097513; C:myosin II filament; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0001725; C:stress fiber; IDA:MGI.
GO; GO:0001931; C:uropod; IDA:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0030898; F:actin-dependent ATPase activity; ISO:MGI.
GO; GO:0043531; F:ADP binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
GO; GO:0043495; F:protein anchor; ISS:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
GO; GO:0031032; P:actomyosin structure organization; ISO:MGI.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0043534; P:blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IMP:MGI.
GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
GO; GO:0032506; P:cytokinetic process; ISS:UniProtKB.
GO; GO:0051295; P:establishment of meiotic spindle localization; IDA:MGI.
GO; GO:0001768; P:establishment of T cell polarity; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0000212; P:meiotic spindle organization; IDA:MGI.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
GO; GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
GO; GO:0007520; P:myoblast fusion; IMP:MGI.
GO; GO:1903919; P:negative regulation of actin filament severing; IMP:UniProtKB.
GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
GO; GO:0070527; P:platelet aggregation; ISO:MGI.
GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
GO; GO:0016337; P:single organismal cell-cell adhesion; IMP:MGI.
GO; GO:0032796; P:uropod organization; IMP:MGI.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR004009; Myosin_N.
InterPro; IPR002928; Myosin_tail.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00063; Myosin_head; 1.
Pfam; PF02736; Myosin_N; 1.
Pfam; PF01576; Myosin_tail_1; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM00015; IQ; 1.
SMART; SM00242; MYSc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50096; IQ; 1.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
Cell adhesion; Cell shape; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Methylation; Motor protein;
Myosin; Nucleotide-binding; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:23806337,
ECO:0000269|Ref.4}.
CHAIN 2 1960 Myosin-9.
/FTId=PRO_0000123417.
DOMAIN 81 776 Myosin motor.
DOMAIN 779 808 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
NP_BIND 174 181 ATP. {ECO:0000255}.
REGION 654 676 Actin-binding.
COILED 841 1926 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:23806337,
ECO:0000269|Ref.4}.
MOD_RES 8 8 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 11 11 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 102 102 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 299 299 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 435 435 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35580}.
MOD_RES 613 613 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 628 628 Phosphoserine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 754 754 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 850 850 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 860 860 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 975 975 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1024 1024 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1114 1114 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1234 1234 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q61879}.
MOD_RES 1249 1249 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1357 1357 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1392 1392 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1404 1404 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1410 1410 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1459 1459 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1638 1638 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1669 1669 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1714 1714 Phosphoserine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1793 1793 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1802 1802 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1845 1845 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1923 1923 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q61879}.
MOD_RES 1939 1939 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 1943 1943 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:17208939,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CONFLICT 1733 1733 Q -> L (in Ref. 1; CAC85955).
{ECO:0000305}.
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


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