TNNC1_CHICK
ID TNNC1_CHICK Reviewed; 161 AA.
AC P09860;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Troponin C, slow skeletal and cardiac muscles;
DE Short=TN-C;
GN Name=TNNC1;
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].
RC TISSUE=Slow skeletal muscle;
RX PubMed=3037328; DOI=10.1128/mcb.7.4.1549-1553.1987;
RA Putkey J.A., Carroll S.L., Means A.R.;
RT "The nontranscribed chicken calmodulin pseudogene cross-hybridizes with
RT mRNA from the slow-muscle troponin C gene.";
RL Mol. Cell. Biol. 7:1549-1553(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart muscle;
RX PubMed=2805242; DOI=10.1161/01.res.65.5.1241;
RA Toyota N., Shimada Y., Bader D.;
RT "Molecular cloning and expression of chicken cardiac troponin C.";
RL Circ. Res. 65:1241-1246(1989).
RN [3]
RP STRUCTURE BY NMR OF 1-89.
RX PubMed=9218458; DOI=10.1074/jbc.272.29.18216;
RA Sia S.K., Li M.X., Spyracopoulos L., Gagne S.M., Liu W., Putkey J.A.,
RA Sykes B.D.;
RT "Structure of cardiac muscle troponin C unexpectedly reveals a closed
RT regulatory domain.";
RL J. Biol. Chem. 272:18216-18221(1997).
RN [4]
RP STRUCTURE BY NMR OF 81-161.
RX PubMed=10387077; DOI=10.1021/bi9902642;
RA Gasmi-Seabrook G.M., Howarth J.W., Finley N., Abusamhadneh E.,
RA Gaponenko V., Brito R.M., Solaro R.J., Rosevear P.R.;
RT "Solution structures of the C-terminal domain of cardiac troponin C free
RT and bound to the N-terminal domain of cardiac troponin I.";
RL Biochemistry 38:8313-8322(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: Slow skeletal muscle Tn-C can bind 3 calcium ions per
CC molecule. Domain I does not bind calcium.
CC -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR EMBL; M16024; AAA48654.1; -; mRNA.
DR EMBL; D13037; BAA02369.1; -; mRNA.
DR PIR; A27204; A27204.
DR RefSeq; NP_990464.1; NM_205133.1.
DR PDB; 1AJ4; NMR; -; A=3-161.
DR PDB; 1DTL; X-ray; 2.15 A; A=1-161.
DR PDB; 1FI5; NMR; -; A=81-161.
DR PDB; 1LA0; NMR; -; A=1-161.
DR PDB; 1SBJ; NMR; -; A=81-161.
DR PDB; 1SCV; NMR; -; A=81-161.
DR PDB; 2CTN; NMR; -; A=3-89.
DR PDB; 3CTN; NMR; -; A=86-161.
DR PDBsum; 1AJ4; -.
DR PDBsum; 1DTL; -.
DR PDBsum; 1FI5; -.
DR PDBsum; 1LA0; -.
DR PDBsum; 1SBJ; -.
DR PDBsum; 1SCV; -.
DR PDBsum; 2CTN; -.
DR PDBsum; 3CTN; -.
DR AlphaFoldDB; P09860; -.
DR BMRB; P09860; -.
DR SMR; P09860; -.
DR BioGRID; 676302; 1.
DR STRING; 9031.ENSGALP00000002212; -.
DR PaxDb; P09860; -.
DR Ensembl; ENSGALT00000102795; ENSGALP00000072451; ENSGALG00000001459.
DR GeneID; 396032; -.
DR KEGG; gga:396032; -.
DR CTD; 7134; -.
DR VEuPathDB; HostDB:geneid_396032; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000153541; -.
DR HOGENOM; CLU_061288_2_5_1; -.
DR InParanoid; P09860; -.
DR OMA; QKSEFRA; -.
DR OrthoDB; 1386217at2759; -.
DR PhylomeDB; P09860; -.
DR TreeFam; TF318191; -.
DR EvolutionaryTrace; P09860; -.
DR PRO; PR:P09860; -.
DR Proteomes; UP000000539; Chromosome 12.
DR Bgee; ENSGALG00000001459; Expressed in heart and 14 other tissues.
DR ExpressionAtlas; P09860; baseline and differential.
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; ISS:AgBase.
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; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Metal-binding; Muscle protein;
KW Reference proteome; Repeat.
FT CHAIN 1..161
FT /note="Troponin C, slow skeletal and cardiac muscles"
FT /id="PRO_0000073701"
FT DOMAIN 16..51
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 52..87
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 92..127
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 128..161
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
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 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 141
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="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:1DTL"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:1DTL"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1DTL"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1DTL"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:1DTL"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:1DTL"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:1DTL"
FT HELIX 74..85
FT /evidence="ECO:0007829|PDB:1DTL"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1AJ4"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:1DTL"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:1DTL"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:1DTL"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:1DTL"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1FI5"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:1DTL"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3CTN"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1DTL"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:1DTL"
SQ SEQUENCE 161 AA; 18431 MW; 426BBC46D117B247 CRC64;
MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ NPTPEELQEM
IDEVDEDGSG TVDFDEFLVM MVRCMKDDSK GKTEEELSDL FRMFDKNADG YIDLEELKIM
LQATGETITE DDIEELMKDG DKNNDGRIDY DEFLEFMKGV E
