ID   TNNC_MIZYE              Reviewed;         152 AA.
AC   P35622;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Troponin C;
DE            Short=TN-C;
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, AND ACETYLATION AT THR-1.
RC   TISSUE=Striated adductor muscle;
RX   PubMed=8106387; DOI=10.1016/s0021-9258(17)41885-0;
RA   Nishita K., Tanaka H., Ojima T.;
RT   "Amino acid sequence of troponin C from scallop striated adductor muscle.";
RL   J. Biol. Chem. 269:3464-3468(1994).
CC   -!- FUNCTION: Troponin is the central regulatory protein of striated muscle
CC       contraction. Tn consists of three components: Tn-I which is the
CC       inhibitor of actomyosin ATPase, Tn-T which contains the binding site
CC       for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the
CC       inhibitory action of Tn on actin filaments.
CC   -!- MISCELLANEOUS: This protein binds one calcium ion per molecule.
CC   -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR   PIR; A53051; A53051.
DR   AlphaFoldDB; P35622; -.
DR   SMR; P35622; -.
DR   iPTMnet; P35622; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW   Muscle protein; Repeat.
FT   CHAIN           1..152
FT                   /note="Troponin C"
FT                   /id="PRO_0000073693"
FT   DOMAIN          9..44
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          45..80
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          82..117
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          118..152
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         131
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         133
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         135
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         137
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         1
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000269|PubMed:8106387"
SQ   SEQUENCE   152 AA;  17411 MW;  D6B9936EA7E41BEE CRC64;
     TEEFRASEKQ ILDAKQAFCN VDKKKEGTVS CKDLGAIFKS LGLLVKDDKI KDWSDEMDEE
     ATGRLNCDAW IQLFERKLKE DLDERELKEA FRVLDKEKKG VIKVDVLRWI LSSLGDELTE
     EEIENMIAET DTDGSGTVDY EEFKCLMMSS DA