MLRT_RABIT
ID MLRT_RABIT Reviewed; 170 AA.
AC P24732;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Myosin regulatory light chain 2, skeletal muscle isoform type 1;
DE AltName: Full=DTNB;
DE AltName: Full=Fast skeletal myosin light chain 2;
DE Short=G2;
DE Short=MLC-2;
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).
CC -!- SUBUNIT: Myosin is a hexamer of 2 heavy chains and 4 light chains.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR EMBL; X54042; CAA37975.1; -; mRNA.
DR PIR; S12855; S12855.
DR PDB; 5H53; EM; 5.20 A; B=25-170.
DR PDBsum; 5H53; -.
DR AlphaFoldDB; P24732; -.
DR SMR; P24732; -.
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 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..170
FT /note="Myosin regulatory light chain 2, skeletal muscle
FT isoform type 1"
FT /id="PRO_0000198742"
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:0000250|UniProtKB:P02608"
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; 19029 MW; 134AA36CC01A2099 CRC64;
MAPKKAKRRA AAEGGSSNVF SMFDQTQIQE FKEAFTVIDQ NRDGIIDKED LRDTFAAMGR
LNVKNEELDA MMKEASGPIN FTVFLTMFGE KLKGADPEDV ITGAFKVLDP EGKGTIKKQF
LEELLITQCD RFSQEEIKNM WAAFSPDVGG NVDYKNICYV ITHGDAKDQE
