TNNC1_PIG
ID TNNC1_PIG Reviewed; 161 AA.
AC P63317; O14800; P02590; P04463; Q4G1M5;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Troponin C, slow skeletal and cardiac muscles;
DE Short=TN-C;
GN Name=TNNC1; Synonyms=TNNC;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Heart muscle;
RX PubMed=2777752; DOI=10.1093/oxfordjournals.jbchem.a122819;
RA Kobayashi T., Takagi T., Konishi K., Morimoto S., Ohtsuki I.;
RT "Amino acid sequence of porcine cardiac muscle troponin C.";
RL J. Biochem. 106:55-59(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Cheng H.C., Deng C.Y., Wang J.;
RT "Cloning and identification of a new gene TNNC1 in pigs.";
RL Submitted (MAR-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; AY958072; AAY33022.1; -; Genomic_DNA.
DR PIR; JU0035; JU0035.
DR RefSeq; NP_001123715.1; NM_001130243.1.
DR PDB; 7KO4; EM; 8.00 A; V/c=2-161.
DR PDB; 7KO5; EM; 7.80 A; V/c=2-161.
DR PDB; 7KO7; EM; 8.30 A; V/c=2-161.
DR PDB; 7KON; EM; 8.10 A; V/c=2-161.
DR PDB; 7KOR; EM; 7.80 A; V/c=2-161.
DR PDBsum; 7KO4; -.
DR PDBsum; 7KO5; -.
DR PDBsum; 7KO7; -.
DR PDBsum; 7KON; -.
DR PDBsum; 7KOR; -.
DR AlphaFoldDB; P63317; -.
DR BMRB; P63317; -.
DR SMR; P63317; -.
DR STRING; 9823.ENSSSCP00000012193; -.
DR iPTMnet; P63317; -.
DR PaxDb; P63317; -.
DR PeptideAtlas; P63317; -.
DR PRIDE; P63317; -.
DR Ensembl; ENSSSCT00000012521; ENSSSCP00000012193; ENSSSCG00000011441.
DR Ensembl; ENSSSCT00005025801; ENSSSCP00005015625; ENSSSCG00005016411.
DR Ensembl; ENSSSCT00015107220; ENSSSCP00015045257; ENSSSCG00015079078.
DR Ensembl; ENSSSCT00025021119; ENSSSCP00025008685; ENSSSCG00025015750.
DR Ensembl; ENSSSCT00030102516; ENSSSCP00030047293; ENSSSCG00030073168.
DR Ensembl; ENSSSCT00035098214; ENSSSCP00035041468; ENSSSCG00035072554.
DR Ensembl; ENSSSCT00040051401; ENSSSCP00040021332; ENSSSCG00040038293.
DR Ensembl; ENSSSCT00045025066; ENSSSCP00045017315; ENSSSCG00045014719.
DR Ensembl; ENSSSCT00050103559; ENSSSCP00050045315; ENSSSCG00050075504.
DR Ensembl; ENSSSCT00055034141; ENSSSCP00055027124; ENSSSCG00055017398.
DR Ensembl; ENSSSCT00060039098; ENSSSCP00060016589; ENSSSCG00060028932.
DR Ensembl; ENSSSCT00065047256; ENSSSCP00065020331; ENSSSCG00065034718.
DR Ensembl; ENSSSCT00070051140; ENSSSCP00070043256; ENSSSCG00070025573.
DR GeneID; 100156435; -.
DR KEGG; ssc:100156435; -.
DR CTD; 7134; -.
DR VGNC; VGNC:94282; TNNC1.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000153541; -.
DR HOGENOM; CLU_061288_2_5_1; -.
DR InParanoid; P63317; -.
DR OMA; QKSEFRA; -.
DR OrthoDB; 1386217at2759; -.
DR TreeFam; TF318191; -.
DR Reactome; R-SSC-390522; Striated Muscle Contraction.
DR Proteomes; UP000008227; Chromosome 13.
DR Proteomes; UP000314985; Chromosome 13.
DR Bgee; ENSSSCG00000011441; Expressed in heart left ventricle and 33 other tissues.
DR ExpressionAtlas; P63317; baseline and differential.
DR Genevisible; P63317; SS.
DR GO; GO:1990584; C:cardiac Troponin complex; IEA:Ensembl.
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:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0031013; F:troponin I binding; IEA:Ensembl.
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 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; Direct protein sequencing;
KW Metal-binding; Muscle protein; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..161
FT /note="Troponin C, slow skeletal and cardiac muscles"
FT /id="PRO_0000073699"
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:2777752"
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
