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MLR_PATSP
ID   MLR_PATSP               Reviewed;         153 AA.
AC   P02613;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Myosin regulatory light chain;
DE   AltName: Full=EDTA light chain;
OS   Patinopecten sp. (Scallop).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Patinopecten; unclassified Patinopecten.
OX   NCBI_TaxID=6574;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Kendrick-Jones J., Jakes R.;
RL   (In) Riecker G., Weber A., Goodwin J. (eds.);
RL   Myocardial failure (International Boehringer Mannheim Symposium), pp.28-40,
RL   Springer-Verlag, Berlin and New York (1977).
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   PIR; A03046; MOSWLE.
DR   AlphaFoldDB; P02613; -.
DR   SMR; P02613; -.
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   Calcium; Direct protein sequencing; Metal-binding; Motor protein;
KW   Muscle protein; Myosin; Repeat.
FT   CHAIN           1..153
FT                   /note="Myosin regulatory light chain"
FT                   /id="PRO_0000198754"
FT   DOMAIN          15..50
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          81..116
FT                   /note="EF-hand 2"
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         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
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   MOD_RES         1
FT                   /note="Blocked amino end (Ala)"
SQ   SEQUENCE   153 AA;  17207 MW;  CD55D28BBFDF8CC2 CRC64;
     ADKAASGVLT KLPQKQIQEM KEAFSMIDVD RDGFVSKDDI KAISEQLGRT PDDKELTAML
     KEAPGPLNFT MFLSDKLSGT DSEETIRNAF AMFDEQENKK LNIEYIKDLL EDMGNNFNKD
     EMRMTFKEAP VEGGKFDYVK FTAMIKGSGE DEA
 
 
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