MYL9_MOUSE
ID MYL9_MOUSE Reviewed; 172 AA.
AC Q9CQ19; Q3TW15; Q80X77;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Myosin regulatory light polypeptide 9;
DE AltName: Full=Myosin regulatory light chain 2, smooth muscle isoform;
DE AltName: Full=Myosin regulatory light chain 9;
GN Name=Myl9; Synonyms=Myrl2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, Osteoclast, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland, and Salivary 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 [3]
RP PHOSPHORYLATION AT SER-20.
RX PubMed=17015463; DOI=10.1128/mcb.01383-06;
RA Ma Z., Kanai M., Kawamura K., Kaibuchi K., Ye K., Fukasawa K.;
RT "Interaction between ROCK II and nucleophosmin/B23 in the regulation of
RT centrosome duplication.";
RL Mol. Cell. Biol. 26:9016-9034(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH MYO19.
RX PubMed=24825904; DOI=10.1074/jbc.m114.569087;
RA Lu Z., Ma X.N., Zhang H.M., Ji H.H., Ding H., Zhang J., Luo D., Sun Y.,
RA Li X.D.;
RT "Mouse myosin-19 is a plus-end-directed, high-duty ratio molecular motor.";
RL J. Biol. Chem. 289:18535-18548(2014).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-19 AND SER-20, PTM,
RP AND MUTAGENESIS OF THR-19 AND SER-20.
RX PubMed=29799007; DOI=10.1038/s41467-018-04436-w;
RA Tsuchiya M., Hara Y., Okuda M., Itoh K., Nishioka R., Shiomi A., Nagao K.,
RA Mori M., Mori Y., Ikenouchi J., Suzuki R., Tanaka M., Ohwada T., Aoki J.,
RA Kanagawa M., Toda T., Nagata Y., Matsuda R., Takayama Y., Tominaga M.,
RA Umeda M.;
RT "Cell surface flip-flop of phosphatidylserine is critical for PIEZO1-
RT mediated myotube formation.";
RL Nat. Commun. 9:2049-2049(2018).
CC -!- FUNCTION: Myosin regulatory subunit that plays an important role in
CC regulation of both smooth muscle and nonmuscle cell contractile
CC activity via its phosphorylation. Implicated in cytokinesis, receptor
CC capping, and cell locomotion (By similarity). In myoblasts, regulates
CC PIEZO1-dependent cortical actomyosin assembly involved in myotube
CC formation (PubMed:29799007). {ECO:0000250|UniProtKB:P24844,
CC ECO:0000269|PubMed:29799007}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains:
CC interacts with myosin heavy chain MYO19. {ECO:0000269|PubMed:24825904}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:29799007}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:29799007}. Note=Colocalizes with F-actin, MYH9 and
CC PIEZO1 at the actomyosin cortex in myoblasts.
CC {ECO:0000269|PubMed:29799007}.
CC -!- PTM: Phosphorylation increases the actin-activated myosin ATPase
CC activity and thereby regulates the contractile activity. It is required
CC to generate the driving force in the migration of the cells but not
CC necessary for localization of myosin-2 at the leading edge (By
CC similarity). Phosphorylation is required for myotube formation
CC (PubMed:29799007). {ECO:0000250|UniProtKB:P24844,
CC ECO:0000269|PubMed:29799007}.
CC -!- MISCELLANEOUS: This chain binds calcium. {ECO:0000250}.
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DR EMBL; AK007972; BAB25381.1; -; mRNA.
DR EMBL; AK020258; BAB32043.1; -; mRNA.
DR EMBL; AK159880; BAE35452.1; -; mRNA.
DR EMBL; BC049974; AAH49974.2; -; mRNA.
DR EMBL; BC055439; AAH55439.1; -; mRNA.
DR CCDS; CCDS50779.1; -.
DR RefSeq; NP_742116.1; NM_172118.1.
DR RefSeq; XP_006500516.1; XM_006500453.3.
DR AlphaFoldDB; Q9CQ19; -.
DR SMR; Q9CQ19; -.
DR BioGRID; 221155; 4.
DR IntAct; Q9CQ19; 2.
DR STRING; 10090.ENSMUSP00000085913; -.
DR iPTMnet; Q9CQ19; -.
DR PhosphoSitePlus; Q9CQ19; -.
DR SwissPalm; Q9CQ19; -.
DR jPOST; Q9CQ19; -.
DR MaxQB; Q9CQ19; -.
DR PaxDb; Q9CQ19; -.
DR PeptideAtlas; Q9CQ19; -.
DR PRIDE; Q9CQ19; -.
DR ProteomicsDB; 252630; -.
DR Antibodypedia; 11734; 439 antibodies from 35 providers.
DR Ensembl; ENSMUST00000088552; ENSMUSP00000085913; ENSMUSG00000067818.
DR GeneID; 98932; -.
DR KEGG; mmu:98932; -.
DR UCSC; uc008nnw.2; mouse.
DR CTD; 10398; -.
DR MGI; MGI:2138915; Myl9.
DR VEuPathDB; HostDB:ENSMUSG00000067818; -.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000155458; -.
DR HOGENOM; CLU_061288_9_3_1; -.
DR InParanoid; Q9CQ19; -.
DR OMA; FECFDEN; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; Q9CQ19; -.
DR TreeFam; TF314218; -.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR Reactome; R-MMU-5627123; RHO GTPases activate PAKs.
DR BioGRID-ORCS; 98932; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Myl9; mouse.
DR PRO; PR:Q9CQ19; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CQ19; protein.
DR Bgee; ENSMUSG00000067818; Expressed in ascending aorta and 272 other tissues.
DR Genevisible; Q9CQ19; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032036; F:myosin heavy chain binding; IPI:MGI.
DR GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13405; EF-hand_6; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Cytoplasm; Cytoskeleton; Metal-binding;
KW Motor protein; Muscle protein; Myosin; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P29269"
FT CHAIN 2..172
FT /note="Myosin regulatory light polypeptide 9"
FT /id="PRO_0000198736"
FT DOMAIN 29..64
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 98..133
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 134..169
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P29269"
FT MOD_RES 19
FT /note="Phosphothreonine; by MLCK, CIT and ROCK2"
FT /evidence="ECO:0000250|UniProtKB:P24844,
FT ECO:0000305|PubMed:29799007"
FT MOD_RES 20
FT /note="Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1,
FT ROCK2, DAPK1, DAPK2 and ZIPK/DAPK3"
FT /evidence="ECO:0000305|PubMed:17015463,
FT ECO:0000305|PubMed:29799007"
FT MUTAGEN 19
FT /note="T->D: Prevents aberrant myotube formation in PIEZO1-
FT deficient myoblast; when associated with D-20."
FT /evidence="ECO:0000269|PubMed:29799007"
FT MUTAGEN 20
FT /note="S->D: Prevents aberrant myotube formation in PIEZO1-
FT deficient myoblast; when associated with D-19."
FT /evidence="ECO:0000269|PubMed:29799007"
FT CONFLICT 132
FT /note="D -> V (in Ref. 1; BAE35452)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 172 AA; 19854 MW; D588C708BF5A2D56 CRC64;
MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS
LGKNPTDEYL EGMMNEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEASGFIHE
DHLRELLTTM GDRFTDEEVD EMYREAPIDK KGNFNYVEFT RILKHGAKDK DD
