MLE_ARGIR
ID MLE_ARGIR Reviewed; 157 AA.
AC P07291;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Myosin essential light chain, striated adductor muscle;
DE Short=E-LC;
DE AltName: Full=Sulfhydryl light chain;
DE Short=SHLC;
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 PROTEIN SEQUENCE OF 2-157.
RX PubMed=3801438; DOI=10.1021/bi00371a056;
RA Collins J.H., Jakes R., Kendrick-Jones J., Leszyk J., Barouch W.,
RA Theibert J.L., Spiegel J., Szent-Gyorgyi A.G.;
RT "Amino acid sequence of myosin essential light chain from the scallop
RT Aquipecten irradians.";
RL Biochemistry 25:7651-7656(1986).
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.
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DR EMBL; M17201; AAA27714.1; -; mRNA.
DR PIR; A25183; A25183.
DR PDB; 1B7T; X-ray; 2.50 A; Z=2-157.
DR PDB; 1DFK; X-ray; 4.20 A; Z=4-155.
DR PDB; 1DFL; X-ray; 4.20 A; X/Z=4-155.
DR PDB; 1KK7; X-ray; 3.20 A; Z=2-157.
DR PDB; 1KK8; X-ray; 2.30 A; C=2-155.
DR PDB; 1KQM; X-ray; 3.00 A; C=2-157.
DR PDB; 1KWO; X-ray; 3.80 A; C=2-157.
DR PDB; 1L2O; X-ray; 2.80 A; C=2-157.
DR PDB; 1QVI; X-ray; 2.54 A; Z=2-157.
DR PDB; 1S5G; X-ray; 3.10 A; Z=2-157.
DR PDB; 1SCM; X-ray; 2.80 A; C=5-153.
DR PDB; 1SR6; X-ray; 2.75 A; C=2-157.
DR PDB; 1WDC; X-ray; 2.00 A; C=2-157.
DR PDB; 2W4T; EM; 35.00 A; Z=5-155.
DR PDB; 2W4V; EM; 35.00 A; Z=5-155.
DR PDB; 2W4W; EM; 35.00 A; Z=5-155.
DR PDB; 3JTD; X-ray; 2.57 A; C=2-156.
DR PDB; 3JVT; X-ray; 2.10 A; C=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; P07291; -.
DR SMR; P07291; -.
DR EvolutionaryTrace; P07291; -.
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; IPR002048; EF_hand_dom.
DR InterPro; IPR029655; Mlc1.
DR PANTHER; PTHR23048:SF33; PTHR23048:SF33; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Motor protein; Muscle protein;
KW Myosin; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3801438"
FT CHAIN 2..157
FT /note="Myosin essential light chain, striated adductor
FT muscle"
FT /id="PRO_0000198718"
FT DOMAIN 7..44
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 HELIX 6..22
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:3JVT"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1QVI"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:1WDC"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1WDC"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:1WDC"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:3JVT"
SQ SEQUENCE 157 AA; 17748 MW; C34640DDE2A27386 CRC64;
MPKLSQDEID DLKDVFELFD FWDGRDGAVD AFKLGDVCRC LGINPRNEDV FAVGGTHKMG
EKSLPFEEFL PAYEGLMDCE QGTFADYMEA FKTFDREGQG FISGAELRHV LTALGERLSD
EDVDEIIKLT DLQEDLEGNV KYEDFVKKVM AGPYPDK
