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Troponin C, slow skeletal and cardiac muscles (TN-C)

 TNNC1_BOVIN             Reviewed;         161 AA.
P63315; O14800; P02590; P04463; Q3SZB2;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
28-MAR-2018, entry version 93.
RecName: Full=Troponin C, slow skeletal and cardiac muscles;
Short=TN-C;
Name=TNNC1; Synonyms=TNNC;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
TISSUE=Heart muscle;
PubMed=1252434; DOI=10.1021/bi00650a033;
van Eerd J.-P., Takahashi K.;
"Determination of the complete amino acid sequence of bovine cardiac
troponin C.";
Biochemistry 15:1171-1180(1976).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Heart ventricle;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Troponin is the central regulatory protein of striated
muscle contraction. Tn consists of three components: Tn-I which is
the inhibitor of actomyosin ATPase, Tn-T which contains the
binding site for tropomyosin and Tn-C. The binding of calcium to
Tn-C abolishes the inhibitory action of Tn on actin filaments.
-!- MISCELLANEOUS: Cardiac muscle Tn-C can bind 3 calcium ions per
molecule. Domain I does not bind calcium.
-!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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EMBL; BC102995; AAI02996.1; -; mRNA.
PIR; A03018; TPBOCC.
RefSeq; NP_001029523.1; NM_001034351.2.
UniGene; Bt.49083; -.
DisProt; DP00249; -.
ProteinModelPortal; P63315; -.
SMR; P63315; -.
STRING; 9913.ENSBTAP00000055780; -.
iPTMnet; P63315; -.
PaxDb; P63315; -.
PRIDE; P63315; -.
Ensembl; ENSBTAT00000062950; ENSBTAP00000055780; ENSBTAG00000045757.
GeneID; 509486; -.
KEGG; bta:509486; -.
CTD; 7134; -.
VGNC; VGNC:36189; TNNC1.
eggNOG; KOG0027; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000118901; -.
HOVERGEN; HBG012180; -.
InParanoid; P63315; -.
KO; K05865; -.
OMA; MNDIYKA; -.
OrthoDB; EOG091G0QHM; -.
TreeFam; TF318191; -.
Reactome; R-BTA-390522; Striated Muscle Contraction.
Proteomes; UP000009136; Chromosome 22.
Bgee; ENSBTAG00000045757; -.
GO; GO:0097512; C:cardiac myofibril; IDA:CAFA.
GO; GO:1990584; C:cardiac Troponin complex; IDA:CAFA.
GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
GO; GO:0005509; F:calcium ion binding; IDA:AgBase.
GO; GO:0048306; F:calcium-dependent protein binding; IDA:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0031013; F:troponin I binding; IPI:CAFA.
GO; GO:0031014; F:troponin T binding; IEA:Ensembl.
GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
GO; GO:0043462; P:regulation of ATPase activity; IEA:Ensembl.
GO; GO:0006937; P:regulation of muscle contraction; IBA:GO_Central.
GO; GO:0032972; P:regulation of muscle filament sliding speed; IEA:Ensembl.
GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
CDD; cd00051; EFh; 2.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 1.
Pfam; PF13833; EF-hand_8; 1.
SMART; SM00054; EFh; 4.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 3.
PROSITE; PS50222; EF_HAND_2; 4.
1: Evidence at protein level;
Acetylation; Calcium; Complete proteome; Direct protein sequencing;
Metal-binding; Muscle protein; Phosphoprotein; Reference proteome;
Repeat.
CHAIN 1 161 Troponin C, slow skeletal and cardiac
muscles.
/FTId=PRO_0000073696.
DOMAIN 16 51 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 52 87 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 92 127 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 128 161 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 65 76 1.
CA_BIND 105 116 2.
CA_BIND 141 152 3.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:1252434}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000250|UniProtKB:P19123}.
SEQUENCE 161 AA; 18417 MW; 5FB0BC46D503A243 CRC64;
MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ NPTPEELQEM
IDEVDEDGSG TVDFDEFLVM MVRCMKDDSK GKSEEELSDL FRMFDKNADG YIDLEELKIM
LQATGETITE DDIEELMKDG DKNNDGRIDY DEFLEFMKGV E


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