MYL11_CHICK
ID MYL11_CHICK Reviewed; 168 AA.
AC P02609; Q90915;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Myosin regulatory light chain 11;
DE AltName: Full=DTNB;
DE AltName: Full=Fast skeletal myosin light chain 2;
DE Short=MLC-2;
DE AltName: Full=G2;
DE AltName: Full=LC2f;
DE AltName: Full=Myosin light chain 11;
DE AltName: Full=Myosin regulatory light chain 2, skeletal muscle isoform;
GN Name=MYL11; Synonyms=MYLPF, RLC {ECO:0000303|PubMed:15256600};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2580100; DOI=10.1016/0022-2836(85)90229-3;
RA Reinach F.C., Fischman D.A.;
RT "Recombinant DNA approach for defining the primary structure of monoclonal
RT antibody epitopes.";
RL J. Mol. Biol. 181:411-422(1985).
RN [2]
RP PROTEIN SEQUENCE OF 3-168.
RX PubMed=7358336; DOI=10.1515/bchm2.1980.361.1.119;
RA Suzuyama Y., Umegane T., Maita T., Matsuda G.;
RT "The amino acid sequence of the L-2 light chain of chicken skeletal muscle
RT myosin.";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:119-127(1980).
RN [3]
RP METHYLATION AT ALA-2.
RX PubMed=3979397; DOI=10.1111/j.1432-1033.1985.tb08809.x;
RA Henry G.D., Trayer I.P., Brewer S., Levine B.A.;
RT "The widespread distribution of alpha-N-trimethylalanine as the N-terminal
RT amino acid of light chains from vertebrate striated muscle myosins.";
RL Eur. J. Biochem. 148:75-82(1985).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8316857; DOI=10.1126/science.8316857;
RA Rayment I., Rypniewski W.R., Schmidt-Base K., Smith R., Tomchick D.R.,
RA Benning M.M., Winkelmann D.A., Wesenberg G., Holden H.M.;
RT "Three-dimensional structure of myosin subfragment-1: a molecular motor.";
RL Science 261:50-58(1993).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF PHE-103.
RX PubMed=15256600; DOI=10.1073/pnas.0401699101;
RA Sherwood J.J., Waller G.S., Warshaw D.M., Lowey S.;
RT "A point mutation in the regulatory light chain reduces the step size of
RT skeletal muscle myosin.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10973-10978(2004).
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 (PubMed:15256600). {ECO:0000250|UniProtKB:O93409,
CC ECO:0000269|PubMed:15256600}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC {ECO:0000305}.
CC -!- PTM: The N-terminus is blocked. N,N,N-trimethylalanine, found in other
CC myosin light chains would not have been detected in the N-terminal
CC tryptic peptide in PubMed:7358336 because it would remain trimethylated
CC and ninhydrin negative after hydrolysis.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR EMBL; M11030; AAA48980.1; -; mRNA.
DR PIR; I50393; MOCHLS.
DR RefSeq; NP_001185673.1; NM_001198744.1.
DR PDB; 1I84; EM; 20.00 A; U/Z=3-168.
DR PDB; 1M8Q; EM; 70.00 A; B/E/H/Q=21-164.
DR PDB; 1MVW; EM; 70.00 A; B/E/H/K/N/Q=26-164.
DR PDB; 1O18; EM; 70.00 A; E/H/K/N/Q=26-164.
DR PDB; 1O19; EM; 70.00 A; B/E/H/K/N/T=26-164.
DR PDB; 1O1A; EM; 70.00 A; B/E/H/K/N/Q=26-164.
DR PDB; 1O1B; EM; 70.00 A; B/E/H/K=26-164.
DR PDB; 1O1C; EM; 70.00 A; B/E/H/K/Q=26-164.
DR PDB; 1O1D; EM; 70.00 A; B/E/H/K/N/Q=26-164.
DR PDB; 1O1E; EM; 70.00 A; B/E/H/K/N/Q=26-164.
DR PDB; 1O1F; EM; 70.00 A; B/E/H/K=26-164.
DR PDB; 1O1G; EM; 70.00 A; B/E/H/K/N/Q=26-164.
DR PDB; 2MYS; X-ray; 2.80 A; B=3-168.
DR PDB; 2W4A; EM; 35.00 A; B=16-165.
DR PDB; 2W4G; EM; 35.00 A; B=16-165.
DR PDB; 2W4H; EM; 35.00 A; B=16-165.
DR PDBsum; 1I84; -.
DR PDBsum; 1M8Q; -.
DR PDBsum; 1MVW; -.
DR PDBsum; 1O18; -.
DR PDBsum; 1O19; -.
DR PDBsum; 1O1A; -.
DR PDBsum; 1O1B; -.
DR PDBsum; 1O1C; -.
DR PDBsum; 1O1D; -.
DR PDBsum; 1O1E; -.
DR PDBsum; 1O1F; -.
DR PDBsum; 1O1G; -.
DR PDBsum; 2MYS; -.
DR PDBsum; 2W4A; -.
DR PDBsum; 2W4G; -.
DR PDBsum; 2W4H; -.
DR AlphaFoldDB; P02609; -.
DR SMR; P02609; -.
DR iPTMnet; P02609; -.
DR GeneID; 776775; -.
DR KEGG; gga:776775; -.
DR CTD; 29895; -.
DR VEuPathDB; HostDB:geneid_776775; -.
DR InParanoid; P02609; -.
DR PhylomeDB; P02609; -.
DR BRENDA; 5.6.1.8; 1306.
DR EvolutionaryTrace; P02609; -.
DR PRO; PR:P02609; -.
DR Proteomes; UP000000539; Unplaced.
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:0006936; P:muscle contraction; IMP:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:UniProtKB.
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; Direct protein sequencing; Metal-binding;
KW Methylation; Motor protein; Muscle protein; Myosin; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..168
FT /note="Myosin regulatory light chain 11"
FT /id="PRO_0000019308"
FT DOMAIN 24..59
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 94..129
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 130..165
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
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:0000305|PubMed:3979397"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MUTAGEN 103
FT /note="F->L: Results in 50% reduction in actin filament
FT velocity."
FT /evidence="ECO:0000269|PubMed:15256600"
FT CONFLICT 61
FT /note="V -> L (in Ref. 1; AAA48980)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="F -> L (in Ref. 1; AAA48980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 18839 MW; FF5913861D2795F1 CRC64;
MAPKKAKRRA AEGSSNVFSM FDQTQIQEFK EAFTVIDQNR DGIIDKDDLR ETFAAMGRLN
VKNEELDAMI KEASGPINFT VFLTMFGEKL KGADPEDVIM GAFKVLDPDG KGSIKKSFLE
ELLTTQCDRF TPEEIKNMWA AFPPDVAGNV DYKNICYVIT HGEDKEGE
