ID   TNNC1_HOMAM             Reviewed;         150 AA.
AC   P29289;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Troponin C, isoform 1;
OS   Homarus americanus (American lobster).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Nephropoidea; Nephropidae; Homarus.
OX   NCBI_TaxID=6706;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC   TISSUE=Abdominal flexor muscle;
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: This protein binds two calcium ions.
CC   -!- MISCELLANEOUS: There are three different troponin C in lobster.
CC   -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR   PIR; S18394; S18394.
DR   AlphaFoldDB; P29289; -.
DR   SMR; P29289; -.
DR   Allergome; 6090; Hom a 6.
DR   iPTMnet; P29289; -.
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; 2.
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..150
FT                   /note="Troponin C, isoform 1"
FT                   /id="PRO_0000073690"
FT   DOMAIN          7..42
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          43..78
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          83..118
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          119..150
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         67
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         132
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         136
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         138
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         143
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:1929438"
SQ   SEQUENCE   150 AA;  16996 MW;  61E38219E31CC867 CRC64;
     MDTLDEDQVQ ALQKAFNSFD TDDKGFITPD TVGVILRMMG VKISDRHLQE VISETDEDGS
     GEIEFEEFAA LAAKFLSEED EEALKKELKE AFRIYDRGGN GYITVHTLKE ILRELDNKLT
     EDNLDSIIEE VDEDGSGTID FNEFMKMMNG