MYL11_RAT
ID MYL11_RAT Reviewed; 169 AA.
AC P04466;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Myosin regulatory light chain 11;
DE AltName: Full=DTNB;
DE AltName: Full=Fast skeletal myosin light chain 2;
DE Short=G2;
DE Short=MLC-2;
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|RGD:3141};
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 [GENOMIC DNA].
RX PubMed=6091059; DOI=10.1093/nar/12.18.7175;
RA Nudel U., Calvo J.M., Shani M., Levy Z.;
RT "The nucleotide sequence of a rat myosin light chain 2 gene.";
RL Nucleic Acids Res. 12:7175-7186(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 70-169.
RX PubMed=6179945; DOI=10.1016/s0021-9258(18)33935-8;
RA Garfinkel L.I., Periasamy M., Nadal-Ginard B.;
RT "Cloning and characterization of cDNA sequences corresponding to myosin
RT light chains 1, 2, and 3, troponin-C, troponin-T, alpha-tropomyosin, and
RT alpha-actin.";
RL J. Biol. Chem. 257:11078-11086(1982).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; THR-35; SER-75 AND
RP THR-101, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Myosin regulatory subunit that plays an essential to maintain
CC muscle integrity during early development (By similarity). Plays a role
CC in muscle contraction (By similarity). {ECO:0000250|UniProtKB:O93409,
CC ECO:0000250|UniProtKB:Q96A32}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR EMBL; X00975; CAA25480.1; -; Genomic_DNA.
DR EMBL; J00754; AAA41660.1; -; mRNA.
DR PIR; A03041; MORTL2.
DR RefSeq; NP_036737.1; NM_012605.2.
DR AlphaFoldDB; P04466; -.
DR SMR; P04466; -.
DR IntAct; P04466; 1.
DR STRING; 10116.ENSRNOP00000023944; -.
DR iPTMnet; P04466; -.
DR PhosphoSitePlus; P04466; -.
DR PaxDb; P04466; -.
DR PRIDE; P04466; -.
DR Ensembl; ENSRNOT00000023944; ENSRNOP00000023944; ENSRNOG00000017645.
DR GeneID; 24584; -.
DR KEGG; rno:24584; -.
DR UCSC; RGD:3141; rat.
DR CTD; 29895; -.
DR RGD; 3141; Mylpf.
DR eggNOG; KOG0031; Eukaryota.
DR GeneTree; ENSGT00940000159038; -.
DR HOGENOM; CLU_061288_9_0_1; -.
DR InParanoid; P04466; -.
DR OMA; EDVKNMW; -.
DR OrthoDB; 1435392at2759; -.
DR PhylomeDB; P04466; -.
DR TreeFam; TF314218; -.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR PRO; PR:P04466; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017645; Expressed in quadriceps femoris and 18 other tissues.
DR Genevisible; P04466; RN.
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; ISO:RGD.
DR GO; GO:0006955; P:immune response; IEP:RGD.
DR GO; GO:0006936; P:muscle contraction; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
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 Calcium; Metal-binding; Methylation; Motor protein; Muscle protein; Myosin;
KW 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_0000198743"
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:0000250|UniProtKB:P97457"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97457"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 169 AA; 18969 MW; 22C0BEB268C0318A CRC64;
MAPKKAKRRA AAEGSSNVFS MFDQTQIQEF KEAFTVIDQN RDGIIDKEDL RDTFAAMGRL
NVKNEELDAM MKEASGPINF TVFLTMFGEK LKGADPEDVI TGAFKVLDPE GKGTIKKQFL
EELLTTQCDR FSQEEIKNMW AAFPPDVGGN VDYKNICYVI THGDAKDQE
