MYL9_RAT
ID MYL9_RAT Reviewed; 171 AA.
AC Q64122;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Heart ventricle;
RX PubMed=7733921; DOI=10.1006/bbrc.1995.1533;
RA Iwai N., Shimoike H., Kinoshita M.;
RT "Genes up-regulated in hypertrophied ventricle.";
RL Biochem. Biophys. Res. Commun. 209:527-534(1995).
RN [2]
RP PHOSPHORYLATION AT SER-20.
RX PubMed=8702756; DOI=10.1074/jbc.271.34.20246;
RA Amano M., Ito M., Kimura K., Fukata Y., Chihara K., Nakano T., Matsuura Y.,
RA Kaibuchi K.;
RT "Phosphorylation and activation of myosin by Rho-associated kinase (Rho-
RT kinase).";
RL J. Biol. Chem. 271:20246-20249(1996).
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, may
CC regulate PIEZO1-dependent cortical actomyosin assembly involved in
CC myotube formation (By similarity). {ECO:0000250|UniProtKB:P24844,
CC ECO:0000250|UniProtKB:Q9CQ19}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains:
CC interacts with myosin heavy chain MYO19.
CC {ECO:0000250|UniProtKB:Q9CQ19}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9CQ19}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q9CQ19}. Note=Colocalizes with F-actin, MYH9 and
CC PIEZO1 at the actomyosin cortex in myoblasts.
CC {ECO:0000250|UniProtKB:Q9CQ19}.
CC -!- TISSUE SPECIFICITY: Smooth muscle tissues and in some, but not all,
CC nonmuscle cells. {ECO:0000269|PubMed:7733921}.
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.
CC Phosphorylation is required for myotube formation.
CC {ECO:0000250|UniProtKB:P02612, ECO:0000250|UniProtKB:P24844}.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR EMBL; S77900; AAB34127.1; -; mRNA.
DR RefSeq; NP_001094355.1; NM_001100885.1.
DR BioGRID; 255320; 2.
DR IntAct; Q64122; 1.
DR MINT; Q64122; -.
DR STRING; 10116.ENSRNOP00000027445; -.
DR iPTMnet; Q64122; -.
DR PhosphoSitePlus; Q64122; -.
DR jPOST; Q64122; -.
DR PaxDb; Q64122; -.
DR PeptideAtlas; Q64122; -.
DR PRIDE; Q64122; -.
DR GeneID; 296313; -.
DR KEGG; rno:296313; -.
DR UCSC; RGD:1311235; rat.
DR CTD; 10398; -.
DR RGD; 1311235; Myl9.
DR eggNOG; KOG0031; Eukaryota.
DR InParanoid; Q64122; -.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR Reactome; R-RNO-5627123; RHO GTPases activate PAKs.
DR ChiTaRS; Myl9; rat.
DR PRO; PR:Q64122; -.
DR Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
DR GO; GO:0001725; C:stress fiber; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032036; F:myosin heavy chain binding; ISO:RGD.
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 SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
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..171
FT /note="Myosin regulatory light polypeptide 9"
FT /id="PRO_0000198738"
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 REGION 1..21
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 MOD_RES 20
FT /note="Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1,
FT ROCK2, DAPK1, DAPK2 and ZIPK/DAPK3"
FT /evidence="ECO:0000269|PubMed:8702756"
SQ SEQUENCE 171 AA; 19721 MW; 30DCBFFE9FE27CB4 CRC64;
MSSKRAKAKT TKKRPQSATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS
LGKNPTDEXL EGMMNEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEASGFIHE
DHLRELLTTM GDRFTDEEVD EMYRERIDKK GNFNYVEFTR ILKHGAKDKD D
