TNNC2_RABIT
ID TNNC2_RABIT Reviewed; 160 AA.
AC P02586;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Troponin C, skeletal muscle;
GN Name=TNNC2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3680204; DOI=10.1016/s0021-9258(18)47742-3;
RA Zot A.S., Potter J.D., Strauss W.L.;
RT "Isolation and sequence of a cDNA clone for rabbit fast skeletal muscle
RT troponin C. Homology with calmodulin and parvalbumin.";
RL J. Biol. Chem. 262:15418-15421(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3277860; DOI=10.1016/0014-5793(88)80576-3;
RA Chen Q., Taljanidisz J., Satyapriya S., Tao T., Gergely J.;
RT "Cloning, sequencing and expression of a full-length rabbit fast skeletal
RT troponin-C cDNA.";
RL FEBS Lett. 228:22-26(1988).
RN [3]
RP PROTEIN SEQUENCE OF 2-160, AND ACETYLATION AT THR-2.
RX PubMed=893419; DOI=10.1016/s0021-9258(17)39964-7;
RA Collins J.H., Greaser M.L., Potter J.D., Horn M.J.;
RT "Determination of the amino acid sequence of troponon C from rabbit
RT skeletal muscle.";
RL J. Biol. Chem. 252:6456-6462(1977).
RN [4]
RP 3D-STRUCTURE MODELING.
RX PubMed=1174567; DOI=10.1016/0005-2795(75)90312-8;
RA Kretsinger R.H., Barry C.D.;
RT "The predicted structure of the calcium-binding component of troponin.";
RL Biochim. Biophys. Acta 405:40-52(1975).
RN [5]
RP STRUCTURE BY NMR OF 122-160.
RX PubMed=2021624; DOI=10.1021/bi00231a031;
RA Kay L.E., Forman-Kay J.D., McCubbin W.D., Kay C.M.;
RT "Solution structure of a polypeptide dimer comprising the fourth Ca(2+)-
RT binding site of troponin C by nuclear magnetic resonance spectroscopy.";
RL Biochemistry 30:4323-4333(1991).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9438870; DOI=10.1016/s0969-2126(97)00315-8;
RA Houdusse A., Love M.L., Dominguez R., Grabarek Z., Cohen C.;
RT "Structures of four Ca2+-bound troponin C at 2.0-A resolution: further
RT insights into the Ca2+-switch in the calmodulin superfamily.";
RL Structure 5:1695-1711(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=10651267;
RX DOI=10.1002/(sici)1097-0134(19991201)37:4<510::aid-prot2>3.0.co;2-t;
RA Soman J., Tao T., Phillips G.N. Jr.;
RT "Conformational variation of calcium-bound troponin C.";
RL Proteins 37:510-511(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF COMPLEX WITH TNI.
RX PubMed=9560191; DOI=10.1073/pnas.95.9.4847;
RA Vassylyev D.G., Takeda S., Wakatsuki S., Maeda K., Maeda Y.;
RT "Crystal structure of troponin C in complex with troponin I fragment at
RT 2.3-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4847-4852(1998).
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 EMBL; J03462; AAA31481.1; -; mRNA.
DR EMBL; Y00760; CAA68729.1; -; mRNA.
DR PIR; A28442; TPRBCS.
DR RefSeq; NP_001076114.1; NM_001082645.1.
DR PDB; 1A2X; X-ray; 2.30 A; A=2-160.
DR PDB; 1TCF; X-ray; 1.90 A; A=2-160.
DR PDB; 1TN4; X-ray; 1.95 A; A=2-160.
DR PDB; 2TN4; X-ray; 2.00 A; A=2-160.
DR PDBsum; 1A2X; -.
DR PDBsum; 1TCF; -.
DR PDBsum; 1TN4; -.
DR PDBsum; 2TN4; -.
DR AlphaFoldDB; P02586; -.
DR BMRB; P02586; -.
DR SMR; P02586; -.
DR BioGRID; 1172361; 3.
DR CORUM; P02586; -.
DR IntAct; P02586; 1.
DR STRING; 9986.ENSOCUP00000020944; -.
DR iPTMnet; P02586; -.
DR PRIDE; P02586; -.
DR GeneID; 100009341; -.
DR KEGG; ocu:100009341; -.
DR CTD; 7125; -.
DR eggNOG; KOG0027; Eukaryota.
DR InParanoid; P02586; -.
DR EvolutionaryTrace; P02586; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0031014; F:troponin T binding; IPI:UniProtKB.
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; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Direct protein sequencing;
KW Metal-binding; Muscle protein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:893419"
FT CHAIN 2..160
FT /note="Troponin C, skeletal muscle"
FT /id="PRO_0000073706"
FT DOMAIN 15..50
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 51..86
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 91..126
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 127..160
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
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 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:893419"
FT CONFLICT 2..3
FT /note="TD -> DT (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:1TCF"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:1TCF"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1TCF"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1TCF"
FT HELIX 53..63
FT /evidence="ECO:0007829|PDB:1TCF"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:1A2X"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1TCF"
FT HELIX 73..103
FT /evidence="ECO:0007829|PDB:1TCF"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:1TN4"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:1TCF"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:1TCF"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1TCF"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:1TCF"
SQ SEQUENCE 160 AA; 18096 MW; 81FED9E732A0F902 CRC64;
MTDQQAEARS YLSEEMIAEF KAAFDMFDAD GGGDISVKEL GTVMRMLGQT PTKEELDAII
EEVDEDGSGT IDFEEFLVMM VRQMKEDAKG KSEEELAECF RIFDRNADGY IDAEELAEIF
RASGEHVTDE EIESLMKDGD KNNDGRIDFD EFLKMMEGVQ
