ID   MYL9_HUMAN              Reviewed;         172 AA.
AC   P24844; E1P5T6; Q9BQL9; Q9BUF9; Q9H136;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Myosin regulatory light polypeptide 9;
DE   AltName: Full=20 kDa myosin light chain;
DE            Short=LC20;
DE   AltName: Full=MLC-2C;
DE   AltName: Full=Myosin RLC;
DE   AltName: Full=Myosin regulatory light chain 2, smooth muscle isoform;
DE   AltName: Full=Myosin regulatory light chain 9;
DE   AltName: Full=Myosin regulatory light chain MRLC1;
GN   Name=MYL9; Synonyms=MLC2, MRLC1, MYRL2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND FUNCTION.
RC   TISSUE=Umbilical artery;
RX   PubMed=2526655; DOI=10.1021/bi00435a059;
RA   Kumar C.C., Mohan S.R., Zavodny P.J., Narula S.K., Leibowitz P.J.;
RT   "Characterization and differential expression of human vascular smooth
RT   muscle myosin light chain 2 isoform in nonmuscle cells.";
RL   Biochemistry 28:4027-4035(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Pan J.Y., Li S., Silberstein D.S.;
RT   "Splice variant of regulatory myosin light chain, short version.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-19 AND
RP   SER-20, AND FUNCTION.
RX   PubMed=11942626; DOI=10.1247/csf.26.677;
RA   Iwasaki T., Murata-Hori M., Ishitobi S., Hosoya H.;
RT   "Diphosphorylated MRLC is required for organization of stress fibers in
RT   interphase cells and the contractile ring in dividing cells.";
RL   Cell Struct. Funct. 26:677-683(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Uterus;
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   [7]
RP   PHOSPHORYLATION AT SER-20.
RX   PubMed=18854160; DOI=10.1016/j.cell.2008.09.018;
RA   Tan I., Yong J., Dong J.M., Lim L., Leung T.;
RT   "A tripartite complex containing MRCK modulates lamellar actomyosin
RT   retrograde flow.";
RL   Cell 135:123-136(2008).
RN   [8]
RP   PHOSPHORYLATION AT SER-20.
RX   PubMed=21072057; DOI=10.1038/cdd.2010.140;
RA   Gabet A.S., Coulon S., Fricot A., Vandekerckhove J., Chang Y., Ribeil J.A.,
RA   Lordier L., Zermati Y., Asnafi V., Belaid Z., Debili N., Vainchenker W.,
RA   Varet B., Hermine O., Courtois G.;
RT   "Caspase-activated ROCK-1 allows erythroblast terminal maturation
RT   independently of cytokine-induced Rho signaling.";
RL   Cell Death Differ. 18:678-689(2011).
RN   [9]
RP   PHOSPHORYLATION AT THR-19 AND SER-20.
RX   PubMed=21457715; DOI=10.1016/j.febslet.2011.03.054;
RA   Tan I., Lai J., Yong J., Li S.F., Leung T.;
RT   "Chelerythrine perturbs lamellar actomyosin filaments by selective
RT   inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase.";
RL   FEBS Lett. 585:1260-1268(2011).
RN   [10]
RP   PHOSPHORYLATION AT SER-20 BY DAPK1; DAPK2 AND ZIPK/DAPK3.
RX   PubMed=21408167; DOI=10.1371/journal.pone.0017344;
RA   Shoval Y., Berissi H., Kimchi A., Pietrokovski S.;
RT   "New modularity of DAP-kinases: alternative splicing of the DRP-1 gene
RT   produces a ZIPk-like isoform.";
RL   PLoS ONE 6:E17344-E17344(2011).
RN   [11]
RP   INVOLVEMENT IN MMIHS4.
RX   PubMed=29453416; DOI=10.1038/s41431-017-0055-5;
RA   Moreno C.A., Sobreira N., Pugh E., Zhang P., Steel G., Torres F.R.,
RA   Cavalcanti D.P.;
RT   "Homozygous deletion in MYL9 expands the molecular basis of megacystis-
RT   microcolon-intestinal hypoperistalsis syndrome.";
RL   Eur. J. Hum. Genet. 26:669-675(2018).
RN   [12]
RP   INVOLVEMENT IN MMIHS4.
RX   PubMed=33031641; DOI=10.1002/mgg3.1516;
RA   Kandler J.L., Sklirou E., Woerner A., Walsh L., Cox E., Xue Y.;
RT   "Compound heterozygous loss of function variants in MYL9 in a child with
RT   megacystis-microcolon-intestinal hypoperistalsis syndrome.";
RL   Mol. Genet. Genomic Med. 8:e1516-e1516(2020).
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 (PubMed:11942626, PubMed:2526655). In
CC       myoblasts, may regulate PIEZO1-dependent cortical actomyosin assembly
CC       involved in myotube formation (By similarity).
CC       {ECO:0000250|UniProtKB:Q9CQ19, ECO:0000269|PubMed:11942626,
CC       ECO:0000269|PubMed:2526655}.
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   -!- INTERACTION:
CC       P24844-2; A6NI15: MSGN1; NbExp=3; IntAct=EBI-13066228, EBI-11991020;
CC       P24844-2; Q99757: TXN2; NbExp=3; IntAct=EBI-13066228, EBI-2932492;
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P24844-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P24844-2; Sequence=VSP_042834;
CC   -!- TISSUE SPECIFICITY: Smooth muscle tissues and in some, but not all,
CC       nonmuscle cells. {ECO:0000269|PubMed:2526655}.
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:0000269|PubMed:11942626,
CC       ECO:0000269|PubMed:21457715}.
CC   -!- DISEASE: Megacystis-microcolon-intestinal hypoperistalsis syndrome 4
CC       (MMIHS4) [MIM:619365]: A form of megacystis-microcolon-intestinal
CC       hypoperistalsis syndrome, a congenital visceral myopathy primarily
CC       affecting females, and characterized by loss of smooth muscle
CC       contraction in the bladder and intestine. Affected individuals present
CC       at birth with functional obstruction of intestine, microcolon, dilation
CC       of bladder, and secondary hydronephrosis. The majority of cases have a
CC       fatal outcome due to malnutrition and sepsis, followed by multiorgan
CC       failure. MMIHS4 inheritance is autosomal recessive.
CC       {ECO:0000269|PubMed:29453416, ECO:0000269|PubMed:33031641}. Note=The
CC       disease may be caused by variants affecting the gene represented in
CC       this entry.
CC   -!- MISCELLANEOUS: This chain binds calcium.
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DR   EMBL; J02854; AAA59852.1; -; mRNA.
DR   EMBL; AF176043; AAQ13654.1; -; mRNA.
DR   EMBL; D82057; BAB88917.1; -; mRNA.
DR   EMBL; AL050318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW76129.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76131.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76132.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76133.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW76134.1; -; Genomic_DNA.
DR   EMBL; BC002648; AAH02648.1; -; mRNA.
DR   CCDS; CCDS13276.1; -. [P24844-1]
DR   CCDS; CCDS13277.1; -. [P24844-2]
DR   PIR; A32031; A32031.
DR   RefSeq; NP_006088.2; NM_006097.4. [P24844-1]
DR   RefSeq; NP_852667.1; NM_181526.2. [P24844-2]
DR   AlphaFoldDB; P24844; -.
DR   SMR; P24844; -.
DR   BioGRID; 115670; 61.
DR   DIP; DIP-60525N; -.
DR   IntAct; P24844; 24.
DR   MINT; P24844; -.
DR   STRING; 9606.ENSP00000279022; -.
DR   GlyGen; P24844; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P24844; -.
DR   MetOSite; P24844; -.
DR   PhosphoSitePlus; P24844; -.
DR   BioMuta; MYL9; -.
DR   DMDM; 20141521; -.
DR   OGP; P24844; -.
DR   EPD; P24844; -.
DR   jPOST; P24844; -.
DR   MassIVE; P24844; -.
DR   MaxQB; P24844; -.
DR   PaxDb; 9606-ENSP00000279022; -.
DR   PeptideAtlas; P24844; -.
DR   ProteomicsDB; 54231; -. [P24844-1]
DR   ProteomicsDB; 54232; -. [P24844-2]
DR   Pumba; P24844; -.
DR   TopDownProteomics; P24844-1; -. [P24844-1]
DR   Antibodypedia; 11734; 547 antibodies from 35 providers.
DR   DNASU; 10398; -.
DR   Ensembl; ENST00000279022.7; ENSP00000279022.2; ENSG00000101335.10. [P24844-1]
DR   Ensembl; ENST00000346786.2; ENSP00000217313.2; ENSG00000101335.10. [P24844-2]
DR   GeneID; 10398; -.
DR   KEGG; hsa:10398; -.
DR   MANE-Select; ENST00000279022.7; ENSP00000279022.2; NM_006097.5; NP_006088.2.
DR   UCSC; uc002xfl.3; human. [P24844-1]
DR   AGR; HGNC:15754; -.
DR   CTD; 10398; -.
DR   DisGeNET; 10398; -.
DR   GeneCards; MYL9; -.
DR   HGNC; HGNC:15754; MYL9.
DR   HPA; ENSG00000101335; Tissue enhanced (intestine).
DR   MalaCards; MYL9; -.
DR   MIM; 609905; gene.
DR   MIM; 619365; phenotype.
DR   neXtProt; NX_P24844; -.
DR   OpenTargets; ENSG00000101335; -.
DR   PharmGKB; PA31387; -.
DR   VEuPathDB; HostDB:ENSG00000101335; -.
DR   eggNOG; KOG0031; Eukaryota.
DR   GeneTree; ENSGT00940000155458; -.
DR   HOGENOM; CLU_061288_9_3_1; -.
DR   InParanoid; P24844; -.
DR   OMA; GFVDHED; -.
DR   OrthoDB; 312751at2759; -.
DR   PhylomeDB; P24844; -.
DR   TreeFam; TF314218; -.
DR   PathwayCommons; P24844; -.
DR   Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
DR   Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR   Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR   Reactome; R-HSA-5625900; RHO GTPases activate CIT.
DR   Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
DR   Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
DR   Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   SignaLink; P24844; -.
DR   SIGNOR; P24844; -.
DR   BioGRID-ORCS; 10398; 15 hits in 1150 CRISPR screens.
DR   ChiTaRS; MYL9; human.
DR   GeneWiki; MYL9; -.
DR   GenomeRNAi; 10398; -.
DR   Pharos; P24844; Tbio.
DR   PRO; PR:P24844; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P24844; Protein.
DR   Bgee; ENSG00000101335; Expressed in popliteal artery and 182 other cell types or tissues.
DR   ExpressionAtlas; P24844; baseline and differential.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005859; C:muscle myosin complex; TAS:ProtInc.
DR   GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR   GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR   GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0032036; F:myosin heavy chain binding; IEA:Ensembl.
DR   GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR   GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR   GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR   GO; GO:0006937; P:regulation of muscle contraction; TAS:ProtInc.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR23049; MYOSIN REGULATORY LIGHT CHAIN 2; 1.
DR   PANTHER; PTHR23049:SF66; MYOSIN REGULATORY LIGHT POLYPEPTIDE 9; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   Genevisible; P24844; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Calcium; Cytoplasm; Cytoskeleton;
KW   Metal-binding; Motor protein; Muscle protein; Myosin; Phosphoprotein;
KW   Reference proteome; 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_0000198735"
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:0000269|PubMed:11942626,
FT                   ECO:0000269|PubMed:21457715"
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:11942626,
FT                   ECO:0000269|PubMed:18854160, ECO:0000269|PubMed:21072057,
FT                   ECO:0000269|PubMed:21408167, ECO:0000269|PubMed:21457715"
FT   VAR_SEQ         62..115
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT                   /id="VSP_042834"
FT   CONFLICT        10
FT                   /note="T -> A (in Ref. 1; AAA59852)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="I -> Y (in Ref. 1; AAA59852)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114
FT                   /note="A -> S (in Ref. 1; AAA59852)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="E -> K (in Ref. 1; AAA59852)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="I -> V (in Ref. 1; AAA59852)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="D -> H (in Ref. 1; AAA59852)"
FT                   /evidence="ECO:0000305"
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
//