TNNC1_BOVIN
ID TNNC1_BOVIN Reviewed; 161 AA.
AC P63315; O14800; P02590; P04463; Q3SZB2;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Troponin C, slow skeletal and cardiac muscles;
DE Short=TN-C;
GN Name=TNNC1; Synonyms=TNNC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Heart muscle;
RX PubMed=1252434; DOI=10.1021/bi00650a033;
RA van Eerd J.-P., Takahashi K.;
RT "Determination of the complete amino acid sequence of bovine cardiac
RT troponin C.";
RL Biochemistry 15:1171-1180(1976).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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: Cardiac 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; BC102995; AAI02996.1; -; mRNA.
DR PIR; A03018; TPBOCC.
DR RefSeq; NP_001029523.1; NM_001034351.2.
DR AlphaFoldDB; P63315; -.
DR BMRB; P63315; -.
DR SMR; P63315; -.
DR STRING; 9913.ENSBTAP00000055780; -.
DR iPTMnet; P63315; -.
DR PaxDb; P63315; -.
DR Ensembl; ENSBTAT00000062950; ENSBTAP00000055780; ENSBTAG00000045757.
DR GeneID; 509486; -.
DR KEGG; bta:509486; -.
DR CTD; 7134; -.
DR VEuPathDB; HostDB:ENSBTAG00000045757; -.
DR VGNC; VGNC:36189; TNNC1.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000153541; -.
DR HOGENOM; CLU_061288_2_5_1; -.
DR InParanoid; P63315; -.
DR OMA; QKSEFRA; -.
DR OrthoDB; 1386217at2759; -.
DR TreeFam; TF318191; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000045757; Expressed in tongue muscle and 93 other tissues.
DR ExpressionAtlas; P63315; baseline and differential.
DR GO; GO:0097512; C:cardiac myofibril; IDA:CAFA.
DR GO; GO:1990584; C:cardiac Troponin complex; IDA:CAFA.
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; IDA:AgBase.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0031013; F:troponin I binding; IPI:CAFA.
DR GO; GO:0031014; F:troponin T binding; IEA:Ensembl.
DR GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; IEA:Ensembl.
DR GO; GO:0006937; P:regulation of muscle contraction; IBA:GO_Central.
DR GO; GO:0032972; P:regulation of muscle filament sliding speed; IEA:Ensembl.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
DR CDD; cd00051; EFh; 2.
DR DisProt; DP00249; -.
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 Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW Muscle protein; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..161
FT /note="Troponin C, slow skeletal and cardiac muscles"
FT /id="PRO_0000073696"
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:0000269|PubMed:1252434"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19123"
SQ SEQUENCE 161 AA; 18417 MW; 5FB0BC46D503A243 CRC64;
MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ NPTPEELQEM
IDEVDEDGSG TVDFDEFLVM MVRCMKDDSK GKSEEELSDL FRMFDKNADG YIDLEELKIM
LQATGETITE DDIEELMKDG DKNNDGRIDY DEFLEFMKGV E
