MLR_TODPA
ID MLR_TODPA Reviewed; 153 AA.
AC P08052;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Myosin regulatory light chain LC-2, mantle muscle;
DE Short=RLC;
OS Todarodes pacificus (Japanese flying squid) (Ommastrephes pacificus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Oegopsina; Ommastrephidae; Todarodes.
OX NCBI_TaxID=6637;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3436964; DOI=10.1093/oxfordjournals.jbchem.a122153;
RA Maita T., Tanaka H., Konno K., Matsuda G.;
RT "Amino acid sequence of the regulatory light chain of squid mantle muscle
RT myosin.";
RL J. Biochem. 102:1151-1157(1987).
CC -!- FUNCTION: In molluscan muscle, calcium regulation is associated with
CC myosin rather than with actin. Muscle myosin contains two types of
CC light chains: the catalytic light chain, essential for ATPase activity,
CC and the regulatory light chain, a calcium-binding protein responsible
CC for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity.
CC -!- MISCELLANEOUS: This chain binds calcium.
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DR PIR; A41510; A41510.
DR PDB; 3I5F; X-ray; 3.10 A; B=1-153.
DR PDB; 3I5G; X-ray; 2.60 A; B=1-153.
DR PDB; 3I5H; X-ray; 3.40 A; B=1-153.
DR PDB; 3I5I; X-ray; 3.30 A; B=1-153.
DR PDBsum; 3I5F; -.
DR PDBsum; 3I5G; -.
DR PDBsum; 3I5H; -.
DR PDBsum; 3I5I; -.
DR AlphaFoldDB; P08052; -.
DR SMR; P08052; -.
DR EvolutionaryTrace; P08052; -.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Metal-binding;
KW Motor protein; Muscle protein; Myosin; Repeat.
FT CHAIN 1..153
FT /note="Myosin regulatory light chain LC-2, mantle muscle"
FT /id="PRO_0000198757"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 82..117
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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 MOD_RES 1
FT /note="Blocked amino end (Ala)"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:3I5G"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3I5F"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:3I5G"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:3I5G"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3I5G"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:3I5G"
FT TURN 73..80
FT /evidence="ECO:0007829|PDB:3I5G"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:3I5G"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3I5F"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:3I5G"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:3I5G"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:3I5G"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:3I5G"
SQ SEQUENCE 153 AA; 17558 MW; 2FBE6E02F8FB9F4E CRC64;
AEEAPRRVKL SQRQMQELKE AFTMIDQDRD GFIGMEDLKD MFSSLGRVPP DDELNAMLKE
CPGQLNFTAF LTLFGEKVSG TDPEDALRNA FSMFDEDGQG FIPEDYLKDL LENMGDNFSK
EEIKNVWKDA PLKNKQFNYN KMVDIKGKAE DED