TNNC2_CHICK
ID TNNC2_CHICK Reviewed; 163 AA.
AC P02588;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Troponin C, skeletal muscle;
GN Name=TNNC2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2963002; DOI=10.1016/s0021-9258(18)69216-6;
RA Reinach F.C., Karlsson R.;
RT "Cloning, expression, and site-directed mutagenesis of chicken skeletal
RT muscle troponin C.";
RL J. Biol. Chem. 263:2371-2376(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-163.
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 [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-163.
RX PubMed=992069; DOI=10.1016/0014-5793(76)80769-7;
RA Wilkinson J.M.;
RT "The amino acid sequence of troponin C from chicken skeletal muscle.";
RL FEBS Lett. 70:254-256(1976).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=3969570; DOI=10.1126/science.3969570;
RA Sundaralingam M., Bergstrom R., Strasburg G., Rao S.T., Raychowdhory P.,
RA Greaser M.L., Wang B.C.;
RT "Molecular structure of troponin C from chicken skeletal muscle at 3-A
RT resolution.";
RL Science 227:945-948(1985).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=3338985; DOI=10.1016/s0021-9258(19)77925-3;
RA Satyshur K.A., Rao S.T., Pyzalska D., Drendel W., Greaser M.L.,
RA Sundaralingam M.;
RT "Refined structure of chicken skeletal muscle troponin C in the two-calcium
RT state at 2-A resolution.";
RL J. Biol. Chem. 263:1628-1647(1988).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS).
RX PubMed=15299475; DOI=10.1107/s090744499300798x;
RA Satyshur K.A., Pyzalska D., Rao S.T., Greaser M.L., Sundaralingam M.;
RT "Structure of chicken skeletal muscle troponin C at 1.78-A resolution.";
RL Acta Crystallogr. D 50:40-49(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RX PubMed=9367759; DOI=10.1006/jmbi.1997.1257;
RA Strynadka N.C., Cherney M., Sielecki A.R., Li M.X., Smillie L.B.,
RA James M.N.G.;
RT "Structural details of a calcium-induced molecular switch: X-ray
RT crystallographic analysis of the calcium-saturated N-terminal domain of
RT troponin C at 1.75-A resolution.";
RL J. Mol. Biol. 273:238-255(1997).
RN [8]
RP STRUCTURE BY NMR OF 94-127.
RX PubMed=1390738; DOI=10.1021/bi00155a009;
RA Shaw G.S., Hodges R.S., Sykes B.D.;
RT "Determination of the solution structure of a synthetic two-site calcium-
RT binding homodimeric protein domain by NMR spectroscopy.";
RL Biochemistry 31:9572-9580(1992).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=8519752; DOI=10.1021/bi00049a010;
RA Slupsky C.M., Sykes B.D.;
RT "NMR solution structure of calcium-saturated skeletal muscle troponin C.";
RL Biochemistry 34:15953-15964(1995).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=10231519; DOI=10.1021/bi982936e;
RA Tsuda S., Miura A., Gagne S.M., Spyracopoulos L., Sykes B.D.;
RT "Low-temperature-induced structural changes in the Apo regulatory domain of
RT skeletal muscle troponin C.";
RL Biochemistry 38:5693-5700(1999).
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; M19027; AAA49097.1; ALT_SEQ; mRNA.
DR PIR; A03015; TPCHCS.
DR RefSeq; NP_990781.1; NM_205450.2.
DR PDB; 1AVS; X-ray; 1.75 A; A/B=2-91.
DR PDB; 1BLQ; NMR; -; A=2-91.
DR PDB; 1CTA; NMR; -; A/B=94-127.
DR PDB; 1CTD; NMR; -; A/B=94-127.
DR PDB; 1JC2; NMR; -; A=89-163.
DR PDB; 1NCX; X-ray; 1.80 A; A=2-163.
DR PDB; 1NCY; X-ray; 2.10 A; A=2-163.
DR PDB; 1NCZ; X-ray; 1.80 A; A=2-163.
DR PDB; 1NPQ; NMR; -; A=2-91.
DR PDB; 1PON; NMR; -; A=94-127, B=130-163.
DR PDB; 1SKT; NMR; -; A=2-91.
DR PDB; 1SMG; NMR; -; A=2-91.
DR PDB; 1TNP; NMR; -; A=2-91.
DR PDB; 1TNQ; NMR; -; A=2-91.
DR PDB; 1TNW; NMR; -; A=2-163.
DR PDB; 1TNX; NMR; -; A=2-163.
DR PDB; 1TOP; X-ray; 1.78 A; A=2-163.
DR PDB; 1YTZ; X-ray; 3.00 A; C=2-163.
DR PDB; 1YV0; X-ray; 7.00 A; C=2-163.
DR PDB; 1ZAC; NMR; -; A=2-91.
DR PDB; 2W49; EM; 35.00 A; 0/3/6/9=5-163.
DR PDB; 2W4U; EM; 35.00 A; 0/3/6/9=5-163.
DR PDB; 4TNC; X-ray; 2.00 A; A=3-163.
DR PDBsum; 1AVS; -.
DR PDBsum; 1BLQ; -.
DR PDBsum; 1CTA; -.
DR PDBsum; 1CTD; -.
DR PDBsum; 1JC2; -.
DR PDBsum; 1NCX; -.
DR PDBsum; 1NCY; -.
DR PDBsum; 1NCZ; -.
DR PDBsum; 1NPQ; -.
DR PDBsum; 1PON; -.
DR PDBsum; 1SKT; -.
DR PDBsum; 1SMG; -.
DR PDBsum; 1TNP; -.
DR PDBsum; 1TNQ; -.
DR PDBsum; 1TNW; -.
DR PDBsum; 1TNX; -.
DR PDBsum; 1TOP; -.
DR PDBsum; 1YTZ; -.
DR PDBsum; 1YV0; -.
DR PDBsum; 1ZAC; -.
DR PDBsum; 2W49; -.
DR PDBsum; 2W4U; -.
DR PDBsum; 4TNC; -.
DR AlphaFoldDB; P02588; -.
DR BMRB; P02588; -.
DR SMR; P02588; -.
DR IntAct; P02588; 3.
DR MINT; P02588; -.
DR STRING; 9031.ENSGALP00000011046; -.
DR PaxDb; P02588; -.
DR Ensembl; ENSGALT00000011060; ENSGALP00000011046; ENSGALG00000006835.
DR GeneID; 396434; -.
DR KEGG; gga:396434; -.
DR CTD; 7125; -.
DR VEuPathDB; HostDB:geneid_396434; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000153541; -.
DR HOGENOM; CLU_061288_2_5_1; -.
DR InParanoid; P02588; -.
DR OMA; VETWEVD; -.
DR OrthoDB; 1386217at2759; -.
DR PhylomeDB; P02588; -.
DR EvolutionaryTrace; P02588; -.
DR PRO; PR:P02588; -.
DR Proteomes; UP000000539; Chromosome 20.
DR Bgee; ENSGALG00000006835; Expressed in skeletal muscle tissue and 4 other tissues.
DR GO; GO:0005861; C:troponin complex; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0006937; P:regulation of muscle contraction; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1908459"
FT CHAIN 2..163
FT /note="Troponin C, skeletal muscle"
FT /id="PRO_0000073707"
FT DOMAIN 18..53
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 54..89
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 94..129
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 130..163
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 42
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 154
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="Blocked amino end (Ala)"
FT MUTAGEN 131
FT /note="T->I: Decreases calcium affinity."
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:1AVS"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:1AVS"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1BLQ"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1AVS"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:1AVS"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:1AVS"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1NPQ"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1AVS"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:1AVS"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:1TNW"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:1CTA"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1NCX"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:1TOP"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:1TOP"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:1TOP"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1JC2"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1TOP"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:1TOP"
SQ SEQUENCE 163 AA; 18375 MW; C4E1D9F40FFED3BC CRC64;
MASMTDQQAE ARAFLSEEMI AEFKAAFDMF DADGGGDIST KELGTVMRML GQNPTKEELD
AIIEEVDEDG SGTIDFEEFL VMMVRQMKED AKGKSEEELA NCFRIFDKNA DGFIDIEELG
EILRATGEHV TEEDIEDLMK DSDKNNDGRI DFDEFLKMME GVQ
