MYL9_PIG
ID MYL9_PIG Reviewed; 172 AA.
AC P29269;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Myosin regulatory light polypeptide 9;
DE AltName: Full=20 kDa myosin light chain;
DE Short=LC20;
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND ACETYLATION AT SER-2.
RC TISSUE=Aorta;
RX PubMed=1490997; DOI=10.1093/oxfordjournals.jbchem.a123917;
RA Watanabe M., Hasegawa Y., Katoh T., Morita F.;
RT "Amino acid sequence of the 20-kDa regulatory light chain of porcine aorta
RT media smooth muscle myosin.";
RL J. Biochem. 112:431-432(1992).
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:1490997}.
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 PIR; JX0232; JX0232.
DR RefSeq; NP_001231401.1; NM_001244472.1.
DR AlphaFoldDB; P29269; -.
DR SMR; P29269; -.
DR STRING; 9823.ENSSSCP00000026757; -.
DR iPTMnet; P29269; -.
DR PaxDb; P29269; -.
DR PeptideAtlas; P29269; -.
DR PRIDE; P29269; -.
DR Ensembl; ENSSSCT00000038183; ENSSSCP00000039784; ENSSSCG00000036402.
DR Ensembl; ENSSSCT00005061353; ENSSSCP00005037938; ENSSSCG00005038395.
DR Ensembl; ENSSSCT00005061390; ENSSSCP00005037964; ENSSSCG00005038395.
DR Ensembl; ENSSSCT00015087839; ENSSSCP00015035811; ENSSSCG00015065383.
DR Ensembl; ENSSSCT00025035917; ENSSSCP00025014999; ENSSSCG00025026472.
DR Ensembl; ENSSSCT00030048806; ENSSSCP00030022051; ENSSSCG00030035177.
DR Ensembl; ENSSSCT00040067901; ENSSSCP00040028855; ENSSSCG00040050327.
DR Ensembl; ENSSSCT00045013997; ENSSSCP00045009684; ENSSSCG00045008329.
DR Ensembl; ENSSSCT00050083928; ENSSSCP00050036018; ENSSSCG00050061604.
DR Ensembl; ENSSSCT00055057826; ENSSSCP00055046274; ENSSSCG00055029127.
DR Ensembl; ENSSSCT00060105423; ENSSSCP00060046331; ENSSSCG00060076756.
DR Ensembl; ENSSSCT00065090066; ENSSSCP00065039398; ENSSSCG00065065581.
DR GeneID; 100157760; -.
DR KEGG; ssc:100157760; -.
DR CTD; 10398; -.
DR VGNC; VGNC:95651; MYL9.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000155458; -.
DR HOGENOM; CLU_061288_9_3_1; -.
DR InParanoid; P29269; -.
DR OMA; FECFDEN; -.
DR OrthoDB; 1435392at2759; -.
DR TreeFam; TF314218; -.
DR Reactome; R-SSC-445355; Smooth Muscle Contraction.
DR Reactome; R-SSC-5627123; RHO GTPases activate PAKs.
DR Proteomes; UP000008227; Chromosome 17.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000036402; Expressed in stomach and 39 other tissues.
DR ExpressionAtlas; P29269; baseline and differential.
DR Genevisible; P29269; SS.
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; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0032036; F:myosin heavy chain binding; IBA:GO_Central.
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; Direct protein sequencing;
KW Metal-binding; Motor protein; Muscle protein; Myosin; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1490997"
FT CHAIN 2..172
FT /note="Myosin regulatory light polypeptide 9"
FT /id="PRO_0000198737"
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:0000269|PubMed:1490997"
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; 19827 MW; 4C9839E85154CDA8 CRC64;
MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS
LGKNPTDEYL EGMMSEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEASGFIHE
DHLRELLTTM GDRFTDEEVD EMYREAPIDK KGNFNYVEFT RILKHGAKDK DD
