MYL11_RABIT
ID MYL11_RABIT Reviewed; 170 AA.
AC P02608;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
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 type 2;
GN Name=MYL11; Synonyms=MYLPF;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2147475; DOI=10.1093/nar/18.22.6687;
RA Maeda K., Mueller-Gerhardt E., Wittinghofer A.;
RT "Sequence of two isoforms of myosin light chain 2 isolated from a rabbit
RT fast skeletal muscle lambda library.";
RL Nucleic Acids Res. 18:6687-6687(1990).
RN [2]
RP PROTEIN SEQUENCE OF 3-170.
RX PubMed=863872; DOI=10.1093/oxfordjournals.jbchem.a131520;
RA Matsuda G., Maita T., Suzuyama Y., Setoguchi M., Umegane T.;
RT "Amino acid sequence of the L-2 light chain of rabbit skeletal muscle
RT myosin.";
RL J. Biochem. 81:809-811(1977).
RN [3]
RP PROTEIN SEQUENCE OF 3-170.
RX PubMed=352892;
RA Matsuda G., Maita T., Suzuyama Y., Setoguchi M., Umegane T.;
RT "The amino acid sequences of the tryptic, chymotryptic and peptic peptides
RT from the L-2 light chain of rabbit skeletal muscle myosin.";
RL Hoppe-Seyler's Z. Physiol. Chem. 359:629-640(1978).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-39 AND 113-146.
RX PubMed=6687628; DOI=10.1038/302718a0;
RA Putney S.D., Herlihy W.C., Schimmel P.R.;
RT "A new troponin T and cDNA clones for 13 different muscle proteins, found
RT by shotgun sequencing.";
RL Nature 302:718-721(1983).
RN [5]
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).
CC -!- FUNCTION: Myosin regulatory subunit that plays an essential role to
CC maintain muscle integrity during early development (By similarity).
CC Plays a role in muscle contraction (By similarity).
CC {ECO:0000250|UniProtKB:O93409, ECO:0000250|UniProtKB:Q96A32}.
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC {ECO:0000305}.
CC -!- PTM: N,N,N-trimethylalanine found in this myosin light chain would not
CC have been detected in the N-terminal tryptic peptide in PubMed:863872
CC and PubMed:352892 because it would remain trimethylated and ninhydrin
CC negative after hydrolysis.
CC -!- MISCELLANEOUS: This chain binds one calcium ion.
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DR EMBL; X54043; CAA37976.1; -; mRNA.
DR EMBL; V00887; CAA24255.1; -; mRNA.
DR EMBL; V00888; CAA24256.1; -; mRNA.
DR PIR; S12691; MORBLD.
DR RefSeq; NP_001076230.1; NM_001082761.1.
DR AlphaFoldDB; P02608; -.
DR SMR; P02608; -.
DR STRING; 9986.ENSOCUP00000015491; -.
DR iPTMnet; P02608; -.
DR GeneID; 100009542; -.
DR KEGG; ocu:100009542; -.
DR CTD; 29895; -.
DR eggNOG; KOG0031; Eukaryota.
DR InParanoid; P02608; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 Calcium; Direct protein sequencing; Metal-binding; Methylation;
KW Motor protein; Muscle protein; Myosin; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..170
FT /note="Myosin regulatory light chain 11"
FT /id="PRO_0000198741"
FT DOMAIN 26..61
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 96..131
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 132..167
FT /note="EF-hand 3"
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 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 50
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:0000269|PubMed:3979397"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97457"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97457"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04466"
SQ SEQUENCE 170 AA; 19027 MW; 1349935FDB900820 CRC64;
MAPKKAKRRA AAEGGSSNVF SMFDQTQIQE FKEAFTVIDQ NRDGIIDKED LRDTFAAMGR
LNVKNEELDA MMKEASGPIN FTVFLTMFGE KLKGADPEDV ITGAFKVLDP EGKGTIKKQF
LEELLTTQCD RFSQEEIKNM WAAFPPDVGG NVDYKNICYV ITHGDAKDQE
