TNNC2_MELGA
ID TNNC2_MELGA Reviewed; 162 AA.
AC P10246;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Troponin C, skeletal muscle;
GN Name=TNNC2;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1908459; DOI=10.1016/s0021-9258(18)98479-6;
RA Golosinska K., Pearlstone J.R., Borgford T., Oikawa K., Kay C.M.,
RA Carpenter M.R., Smillie L.B.;
RT "Determination of and corrections to sequences of turkey and chicken
RT troponins-C. Effects of Thr-130 to Ile mutation on Ca2+ affinity.";
RL J. Biol. Chem. 266:15797-15809(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=3210231; DOI=10.1016/0022-2836(88)90208-2;
RA Herzberg O., James M.N.G.;
RT "Refined crystal structure of troponin C from turkey skeletal muscle at
RT 2.0-A resolution.";
RL J. Mol. Biol. 203:761-779(1988).
RN [3]
RP STRUCTURE BY NMR OF 12-87.
RX PubMed=8461307; DOI=10.1021/bi00064a033;
RA Findlay W.A., Sykes B.D.;
RT "1H-NMR resonance assignments, secondary structure, and global fold of the
RT TR1C fragment of turkey skeletal troponin C in the calcium-free state.";
RL Biochemistry 32:3461-3467(1993).
RN [4]
RP STRUCTURE BY NMR OF 12-87.
RX PubMed=8120037; DOI=10.2210/pdb1trf/pdb;
RA Findlay W.A., Soenninchen F.D., Sykes B.D.;
RT "Solution structure of the TR1C fragment of skeletal muscle troponin-C.";
RL J. Biol. Chem. 269:6773-6778(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: Skeletal muscle troponin C binds four calcium ions.
CC -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR PIR; A40803; A40803.
DR PDB; 1TRF; NMR; -; A=12-87.
DR PDB; 5TNC; X-ray; 2.00 A; A=2-162.
DR PDBsum; 1TRF; -.
DR PDBsum; 5TNC; -.
DR AlphaFoldDB; P10246; -.
DR BMRB; P10246; -.
DR SMR; P10246; -.
DR HOGENOM; CLU_061288_2_5_1; -.
DR InParanoid; P10246; -.
DR OMA; VETWEVD; -.
DR EvolutionaryTrace; P10246; -.
DR Proteomes; UP000001645; Unplaced.
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; 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; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Metal-binding;
KW Muscle protein; Reference proteome; Repeat.
FT CHAIN 1..162
FT /note="Troponin C, skeletal muscle"
FT /id="PRO_0000073708"
FT DOMAIN 17..52
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 53..88
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 93..128
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 129..162
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:5TNC"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:5TNC"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:5TNC"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5TNC"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5TNC"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5TNC"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:5TNC"
FT HELIX 55..65
FT /evidence="ECO:0007829|PDB:5TNC"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5TNC"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5TNC"
FT HELIX 75..105
FT /evidence="ECO:0007829|PDB:5TNC"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:5TNC"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5TNC"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:5TNC"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:5TNC"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:5TNC"
SQ SEQUENCE 162 AA; 18284 MW; 8B35C5B5B58E7A46 CRC64;
PSMTDQQAEA RAFLSEEMIA EFKAAFDMFD ADGGGDISTK ELGTVMRMLG QNPTKEELDA
IIEEVDEDGS GTIDFEEFLV MMVRQMKEDA KGKSEEELAN CFRIFDKNAD GFIDIEELGE
ILRATGEHVT EEEIEDLMKD SDKNNDGRID FDEFLKMMEG VQ
