ID   TNNC_TODPA              Reviewed;         148 AA.
AC   Q9BLG0;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Troponin C;
DE            Short=TN-C;
OS   Todarodes pacificus (Japanese flying squid) (Ommastrephes pacificus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Teuthida; Oegopsina; Ommastrephidae; Todarodes.
OX   NCBI_TaxID=6637 {ECO:0000312|EMBL:BAB40597.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-138.
RC   TISSUE=Mantle muscle;
RX   PubMed=11435133; DOI=10.1016/s1096-4959(01)00397-9;
RA   Ojima T., Ohta T., Nishita K.;
RT   "Amino acid sequence of squid troponin C.";
RL   Comp. Biochem. Physiol. 129B:787-796(2001).
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.
CC       {ECO:0000269|PubMed:11435133}.
CC   -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR   EMBL; AB049962; BAB40597.1; -; mRNA.
DR   AlphaFoldDB; Q9BLG0; -.
DR   SMR; Q9BLG0; -.
DR   GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
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; 2.
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   Calcium; Direct protein sequencing; Metal-binding; Muscle protein; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11435133"
FT   CHAIN           2..148
FT                   /note="Troponin C"
FT                   /id="PRO_0000073695"
FT   DOMAIN          8..43
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          44..79
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          81..116
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          117..148
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         130
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         132
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         136
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         141
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ   SEQUENCE   148 AA;  17136 MW;  2B7063302FDE28BF CRC64;
     MPVVISEKQF NDAHQAFKLH DKKDEGAVSN KELTNLFKSL ALHVSDDKLQ QWVDEMDEDA
     TGVIRWEKFK ILFERKVQED EDERELRSAF RVLDKNNQGV IDVEDLRWIL KSLGDDLNDD
     EIQDMINETD TDGSGTVDYE EFSALMLG