MLR_ARGIR
ID MLR_ARGIR Reviewed; 157 AA.
AC P13543;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Myosin regulatory light chain, striated adductor muscle;
DE Short=R-LC;
OS Argopecten irradians (Bay scallop) (Aequipecten irradians).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC Argopecten.
OX NCBI_TaxID=31199;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2440882; DOI=10.1016/s0021-9258(18)60925-1;
RA Goodwin E.B., Szent-Gyorgyi A.G., Leinwand L.A.;
RT "Cloning and characterization of the scallop essential and regulatory
RT myosin light chain cDNAs.";
RL J. Biol. Chem. 262:11052-11056(1987).
RN [2]
RP SEQUENCE REVISION, AND MUTAGENESIS.
RX PubMed=2146399; DOI=10.1016/s0022-2836(05)80062-2;
RA Goodwin E.B., Leinwand L.A., Szent-Gyorgyi A.G.;
RT "Regulation of scallop myosin by mutant regulatory light chains.";
RL J. Mol. Biol. 216:85-93(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8127365; DOI=10.1038/368306a0;
RA Xie X., Harrison D.H., Schlichting I., Sweet R.M., Kalabokis V.N.,
RA Szent-Gyorgyi A.G., Cohen C.;
RT "Structure of the regulatory domain of scallop myosin at 2.8-A
RT resolution.";
RL Nature 368:306-312(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8805510; DOI=10.1016/s0969-2126(96)00006-8;
RA Houdusse A., Cohen C.;
RT "Structure of the regulatory domain of scallop myosin at 2-A resolution:
RT implications for regulation.";
RL Structure 4:21-32(1996).
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 EMBL; M17208; AAA27715.1; ALT_SEQ; mRNA.
DR PIR; B29786; B29786.
DR PDB; 1B7T; X-ray; 2.50 A; Y=2-157.
DR PDB; 1DFK; X-ray; 4.20 A; Y=13-151.
DR PDB; 1DFL; X-ray; 4.20 A; W/Y=13-151.
DR PDB; 1KK7; X-ray; 3.20 A; Y=2-157.
DR PDB; 1KK8; X-ray; 2.30 A; B=14-152.
DR PDB; 1KQM; X-ray; 3.00 A; B=2-157.
DR PDB; 1KWO; X-ray; 3.80 A; B=2-157.
DR PDB; 1L2O; X-ray; 2.80 A; B=2-157.
DR PDB; 1QVI; X-ray; 2.54 A; Y=2-157.
DR PDB; 1S5G; X-ray; 3.10 A; Y=2-157.
DR PDB; 1SCM; X-ray; 2.80 A; B=13-157.
DR PDB; 1SR6; X-ray; 2.75 A; B=2-157.
DR PDB; 1WDC; X-ray; 2.00 A; B=2-157.
DR PDB; 2W4T; EM; 35.00 A; Y=16-151.
DR PDB; 2W4V; EM; 35.00 A; Y=16-151.
DR PDB; 2W4W; EM; 35.00 A; Y=16-151.
DR PDB; 3JTD; X-ray; 2.57 A; B=2-157.
DR PDB; 3JVT; X-ray; 2.10 A; B=2-157.
DR PDBsum; 1B7T; -.
DR PDBsum; 1DFK; -.
DR PDBsum; 1DFL; -.
DR PDBsum; 1KK7; -.
DR PDBsum; 1KK8; -.
DR PDBsum; 1KQM; -.
DR PDBsum; 1KWO; -.
DR PDBsum; 1L2O; -.
DR PDBsum; 1QVI; -.
DR PDBsum; 1S5G; -.
DR PDBsum; 1SCM; -.
DR PDBsum; 1SR6; -.
DR PDBsum; 1WDC; -.
DR PDBsum; 2W4T; -.
DR PDBsum; 2W4V; -.
DR PDBsum; 2W4W; -.
DR PDBsum; 3JTD; -.
DR PDBsum; 3JVT; -.
DR AlphaFoldDB; P13543; -.
DR SMR; P13543; -.
DR EvolutionaryTrace; P13543; -.
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; Metal-binding; Motor protein; Muscle protein;
KW Myosin; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..157
FT /note="Myosin regulatory light chain, striated adductor
FT muscle"
FT /id="PRO_0000198751"
FT DOMAIN 16..51
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 85..120
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 33
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 STRAND 8..10
FT /evidence="ECO:0007829|PDB:3JVT"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:1WDC"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3JTD"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1QVI"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1B7T"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:3JVT"
SQ SEQUENCE 157 AA; 17671 MW; 243CE69DB02A7772 CRC64;
MADKAASGVL TKLPQKQIQE MKEAFSMIDV DRDGFVSKED IKAISEQLGR APDDKELTAM
LKEAPGPLNF TMFLSIFSDK LSGTDSEETI RNAFAMFDEQ ETKKLNIEYI KDLLENMGDN
FNKDEMRMTF KEAPVEGGKF DYVKFTAMIK GSGEEEA
