ID   TNNC2_BALNU             Reviewed;         151 AA.
AC   P21798;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Troponin C, isoform 2;
OS   Balanus nubilus (Giant acorn barnacle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Cirripedia; Thoracica; Thoracicalcarea; Balanomorpha; Balanoidea;
OC   Balanidae; Balaninae; Balanus.
OX   NCBI_TaxID=6678;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RX   PubMed=1988057; DOI=10.1021/bi00217a017;
RA   Collins J.H., Theibert J.L., Francois J.-M., Ashley C.C., Potter J.D.;
RT   "Amino acid sequences and Ca2(+)-binding properties of two isoforms of
RT   barnacle troponin C.";
RL   Biochemistry 30:702-707(1991).
RN   [2]
RP   SEQUENCE REVISION TO 77.
RX   PubMed=1929438; DOI=10.1016/0003-9861(91)90108-u;
RA   Garone L., Theibert J.L., Miegel A., Maeda Y., Murphy C., Collins J.H.;
RT   "Lobster troponin C: amino acid sequences of three isoforms.";
RL   Arch. Biochem. Biophys. 291:89-91(1991).
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: There are two different troponin C in barnacle.
CC   -!- MISCELLANEOUS: This protein binds two calcium ions.
CC   -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; B38397; B38397.
DR   AlphaFoldDB; P21798; -.
DR   SMR; P21798; -.
DR   iPTMnet; P21798; -.
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   Pfam; PF13833; EF-hand_8; 1.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
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..151
FT                   /note="Troponin C, isoform 2"
FT                   /id="PRO_0000073683"
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          84..119
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          120..151
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         57
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         61
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         133
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         135
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         137
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         139
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         144
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:1988057"
SQ   SEQUENCE   151 AA;  16796 MW;  5B984D4BE5E505A3 CRC64;
     MMDELDKDQI AMLKKAFDGF DHEKKGAINC DVVATILRMM GQAYNAQTLK ELIDEVDADG
     SGMLEFEEFV TLAAKFIIDD DAEAMAKELK EAFRLYDKAG KGYIPTSALK DILKELDETL
     NAEDLDNIIG EIDTDGSGTV DFDEFMEMMT G