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MLRC_MIZYE
ID   MLRC_MIZYE              Reviewed;         156 AA.
AC   P05944;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Myosin regulatory light chain, striated adductor muscle;
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Mizuhopecten.
OX   NCBI_TaxID=6573;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6706905; DOI=10.1093/oxfordjournals.jbchem.a134581;
RA   Maita T., Konno K., Ojima T., Matsuda G.;
RT   "Amino acid sequences of the regulatory light chains of striated adductor
RT   muscle myosins from Ezo giant scallop and Akazara scallop.";
RL   J. Biochem. 95:167-177(1984).
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; A28863; A28863.
DR   AlphaFoldDB; P05944; -.
DR   SMR; P05944; -.
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; PF00036; EF-hand_1; 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..156
FT                   /note="Myosin regulatory light chain, striated adductor
FT                   muscle"
FT                   /id="PRO_0000198750"
FT   DOMAIN          15..50
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          84..119
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   156 AA;  17527 MW;  475124DA9D7657FF CRC64;
     ADKAASGVLT KLPQKQIQEM KEAFSMIDVD RDGFVNKDDL KAISEQLGRT PDDKELTAML
     KEAPGPLNFT MFLSIFSDKL SGTDTEETLR NAFAMFDELD TKKLNIEYIK DLLENMGDNF
     TKDEMRMTFK EAPVTGGKFD YVKFTAMIKG SGEEEA
 
 
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