MYL9_BOVIN
ID MYL9_BOVIN Reviewed; 172 AA.
AC Q5E9E2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 110.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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. {ECO:0000250}.
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DR EMBL; BT020978; AAX08995.1; -; mRNA.
DR EMBL; BC118244; AAI18245.1; -; mRNA.
DR RefSeq; NP_001015640.1; NM_001015640.2.
DR RefSeq; XP_005224259.1; XM_005224202.3.
DR AlphaFoldDB; Q5E9E2; -.
DR SMR; Q5E9E2; -.
DR STRING; 9913.ENSBTAP00000021328; -.
DR iPTMnet; Q5E9E2; -.
DR PaxDb; Q5E9E2; -.
DR PRIDE; Q5E9E2; -.
DR Ensembl; ENSBTAT00000021328; ENSBTAP00000021328; ENSBTAG00000016024.
DR GeneID; 531505; -.
DR KEGG; bta:531505; -.
DR CTD; 10627; -.
DR VEuPathDB; HostDB:ENSBTAG00000016024; -.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000153607; -.
DR HOGENOM; CLU_061288_9_3_1; -.
DR InParanoid; Q5E9E2; -.
DR OMA; GFVDHED; -.
DR TreeFam; TF314218; -.
DR Reactome; R-BTA-3928664; Ephrin signaling.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000016024; Expressed in gluteus medius and 104 other tissues.
DR GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IDA:UniProtKB.
DR GO; GO:0097513; C:myosin II filament; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0035254; F:glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0032036; F:myosin heavy chain binding; IBA:GO_Central.
DR GO; GO:0031032; P:actomyosin structure organization; IDA:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR015070; EF_hand_DJBP.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF08976; EF-hand_11; 1.
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; 3.
PE 2: Evidence at transcript 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_0000247600"
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 MOD_RES 20
FT /note="Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1,
FT ROCK2, DAPK1, DAPK2 and ZIPK/DAPK3"
FT /evidence="ECO:0000250|UniProtKB:P24844"
SQ SEQUENCE 172 AA; 19865 MW; 27DB2A9FC9BC086B CRC64;
MSSKRAKTKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS
LGKNPTDEYL DAMMNEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEATGTIQE
DYLRELLTTM GDRFTDEEVD ELYREAPIDK KGNFNYIEFT RILKHGAKDK DD
