ID   TNNC_HALRO              Reviewed;         155 AA.
AC   P06706;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Troponin C, body wall muscle;
OS   Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC   Pyuridae; Halocynthia.
OX   NCBI_TaxID=7729;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT VAL-1.
RX   PubMed=6671964; DOI=10.1093/oxfordjournals.jbchem.a134526;
RA   Takagi T., Konishi K.;
RT   "Amino acid sequence of troponin C obtained from ascidian (Halocynthia
RT   roretzi) body wall muscle.";
RL   J. Biochem. 94:1753-1760(1983).
CC   -!- FUNCTION: Troponin is the central regulatory protein of 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   -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR   PIR; A28853; A28853.
DR   AlphaFoldDB; P06706; -.
DR   SMR; P06706; -.
DR   iPTMnet; P06706; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00051; EFh; 2.
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   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF13833; EF-hand_8; 1.
DR   SMART; SM00054; EFh; 4.
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..155
FT                   /note="Troponin C, body wall muscle"
FT                   /id="PRO_0000073689"
FT   DOMAIN          7..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          88..121
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          122..155
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         135
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         137
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         139
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         141
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         146
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         1
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000269|PubMed:6671964"
SQ   SEQUENCE   155 AA;  17749 MW;  B7ED76F2DF693FB4 CRC64;
     VEHLTEDEKS QFRAAFDIFV ADAKDGTISS KELGKVMKML GQNPTEKDLQ EMIEEVDIDG
     SGTIDFEEFC LMMYRQMQAQ EEAKIPEREE KELSEAFRLF DLDGDGIGDE LKAALDGTGE
     NVETWEVDEM MADGDKNHDS QIDYEEWVTM MKFVQ