MYL11_MOUSE
ID MYL11_MOUSE Reviewed; 169 AA.
AC P97457;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Myosin regulatory light chain 11;
DE AltName: Full=Fast skeletal myosin light chain 2;
DE AltName: Full=MLC2F;
DE AltName: Full=Myosin light chain 11;
DE AltName: Full=Myosin regulatory light chain 2, skeletal muscle isoform;
GN Name=Myl11; Synonyms=Mylpf {ECO:0000312|MGI:MGI:97273};
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 [MRNA].
RC TISSUE=Embryo;
RA Park K.W., Park W.J.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8777429;
RA Palermo J., Gulick J., Ng W., Grupp I.L., Grupp G., Robbins J.;
RT "Remodeling the mammalian heart using transgenesis.";
RL Cell. Mol. Biol. Res. 41:501-509(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary 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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17356007; DOI=10.1096/fj.06-7538com;
RA Wang Y., Szczesna-Cordary D., Craig R., Diaz-Perez Z., Guzman G.,
RA Miller T., Potter J.D.;
RT "Fast skeletal muscle regulatory light chain is required for fast and slow
RT skeletal muscle development.";
RL FASEB J. 21:2205-2214(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Lung;
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).
CC -!- FUNCTION: Myosin regulatory subunit that plays an essential role to
CC maintain muscle integrity during early development (PubMed:17356007).
CC Plays a role in regulation of muscle contraction (By similarity).
CC {ECO:0000250|UniProtKB:O93409, ECO:0000269|PubMed:17356007}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice completely lack skeletal muscle
CC and die immediately after birth because of respiratory failure.
CC {ECO:0000269|PubMed:17356007}.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR EMBL; U77943; AAB19118.1; -; mRNA.
DR EMBL; BC055869; AAH55869.1; -; mRNA.
DR CCDS; CCDS40140.1; -.
DR RefSeq; NP_058034.1; NM_016754.5.
DR PDB; 7NEP; EM; 10.20 A; R/S=21-164.
DR PDB; 7QIO; EM; 9.00 A; P/Q=1-169.
DR PDBsum; 7NEP; -.
DR PDBsum; 7QIO; -.
DR AlphaFoldDB; P97457; -.
DR SMR; P97457; -.
DR BioGRID; 201660; 5.
DR IntAct; P97457; 2.
DR MINT; P97457; -.
DR STRING; 10090.ENSMUSP00000032910; -.
DR iPTMnet; P97457; -.
DR PhosphoSitePlus; P97457; -.
DR SWISS-2DPAGE; P97457; -.
DR UCD-2DPAGE; P97457; -.
DR PaxDb; P97457; -.
DR PeptideAtlas; P97457; -.
DR PRIDE; P97457; -.
DR ProteomicsDB; 295916; -.
DR Antibodypedia; 13671; 182 antibodies from 29 providers.
DR DNASU; 17907; -.
DR Ensembl; ENSMUST00000032910; ENSMUSP00000032910; ENSMUSG00000030672.
DR GeneID; 17907; -.
DR KEGG; mmu:17907; -.
DR UCSC; uc009jup.1; mouse.
DR CTD; 29895; -.
DR MGI; MGI:97273; Mylpf.
DR VEuPathDB; HostDB:ENSMUSG00000030672; -.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000159038; -.
DR HOGENOM; CLU_061288_9_0_1; -.
DR InParanoid; P97457; -.
DR OMA; EDVKNMW; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P97457; -.
DR TreeFam; TF314218; -.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR BioGRID-ORCS; 17907; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Mylpf; mouse.
DR PRO; PR:P97457; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P97457; protein.
DR Bgee; ENSMUSG00000030672; Expressed in temporalis muscle and 201 other tissues.
DR ExpressionAtlas; P97457; baseline and differential.
DR Genevisible; P97457; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0008307; F:structural constituent of muscle; IMP:BHF-UCL.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; ISO:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:BHF-UCL.
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; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; Methylation; Motor protein;
KW Muscle protein; Myosin; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02608"
FT CHAIN 2..169
FT /note="Myosin regulatory light chain 11"
FT /id="PRO_0000019310"
FT DOMAIN 25..60
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 95..130
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 131..166
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02608"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
SQ SEQUENCE 169 AA; 18955 MW; 06E4E1126D3A6DB0 CRC64;
MAPKKAKRRA GAEGSSNVFS MFDQTQIQEF KEAFTVIDQN RDGIIDKEDL RDTFAAMGRL
NVKNEELDAM MKEASGPINF TVFLTMFGEK LKGADPEDVI TGAFKVLDPE GKGTIKKQFL
EELLTTQCDR FSQEEIKNMW AAFPPDVGGN VDYKNICYVI THGDAKDQE
