TNNC1_MOUSE
ID TNNC1_MOUSE Reviewed; 161 AA.
AC P19123;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Troponin C, slow skeletal and cardiac muscles;
DE Short=TN-C;
GN Name=Tnnc1; Synonyms=Tncc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2753913; DOI=10.1016/s0021-9258(18)51617-3;
RA Parmacek M.S., Leiden J.M.;
RT "Structure and expression of the murine slow/cardiac troponin C gene.";
RL J. Biol. Chem. 264:13217-13225(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; J04971; AAA37492.1; -; Genomic_DNA.
DR EMBL; M29793; AAA37493.1; -; mRNA.
DR EMBL; BC061172; AAH61172.1; -; mRNA.
DR CCDS; CCDS36854.1; -.
DR PIR; A32620; A32620.
DR RefSeq; NP_033419.1; NM_009393.2.
DR PDB; 6KLT; EM; 12.00 A; A=13-158.
DR PDB; 6KLU; EM; 12.00 A; A=2-158.
DR PDBsum; 6KLT; -.
DR PDBsum; 6KLU; -.
DR AlphaFoldDB; P19123; -.
DR BMRB; P19123; -.
DR SMR; P19123; -.
DR BioGRID; 204238; 2.
DR ComplexPortal; CPX-16; Cardiac Troponin complex.
DR IntAct; P19123; 4.
DR MINT; P19123; -.
DR STRING; 10090.ENSMUSP00000131991; -.
DR iPTMnet; P19123; -.
DR PhosphoSitePlus; P19123; -.
DR CPTAC; non-CPTAC-4066; -.
DR MaxQB; P19123; -.
DR PaxDb; P19123; -.
DR PeptideAtlas; P19123; -.
DR PRIDE; P19123; -.
DR ProteomicsDB; 258939; -.
DR Antibodypedia; 3730; 453 antibodies from 34 providers.
DR DNASU; 21924; -.
DR Ensembl; ENSMUST00000169169; ENSMUSP00000131991; ENSMUSG00000091898.
DR GeneID; 21924; -.
DR KEGG; mmu:21924; -.
DR UCSC; uc007sxd.1; mouse.
DR CTD; 7134; -.
DR MGI; MGI:98779; Tnnc1.
DR VEuPathDB; HostDB:ENSMUSG00000091898; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000153541; -.
DR HOGENOM; CLU_061288_2_5_1; -.
DR InParanoid; P19123; -.
DR OMA; QKSEFRA; -.
DR OrthoDB; 1386217at2759; -.
DR PhylomeDB; P19123; -.
DR TreeFam; TF318191; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 21924; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tnnc1; mouse.
DR PRO; PR:P19123; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P19123; protein.
DR Bgee; ENSMUSG00000091898; Expressed in interventricular septum and 183 other tissues.
DR ExpressionAtlas; P19123; baseline and differential.
DR Genevisible; P19123; MM.
DR GO; GO:1990584; C:cardiac Troponin complex; ISO:MGI.
DR GO; GO:0043292; C:contractile fiber; ISO:MGI.
DR GO; GO:0005861; C:troponin complex; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISS:AgBase.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0031013; F:troponin I binding; ISO:MGI.
DR GO; GO:0031014; F:troponin T binding; ISO:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR GO; GO:0002086; P:diaphragm contraction; ISO:MGI.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; IDA:BHF-UCL.
DR GO; GO:0006937; P:regulation of muscle contraction; ISO:MGI.
DR GO; GO:0032972; P:regulation of muscle filament sliding speed; IMP:BHF-UCL.
DR GO; GO:0010038; P:response to metal ion; ISO:MGI.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR GO; GO:0014883; P:transition between fast and slow fiber; IDA:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:MGI.
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 Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..161
FT /note="Troponin C, slow skeletal and cardiac muscles"
FT /id="PRO_0000073698"
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|UniProtKB:P63315"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 161 AA; 18421 MW; 34DCC903C157A312 CRC64;
MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ NPTPEELQEM
IDEVDEDGSG TVDFDEFLVM MVRCMKDDSK GKSEEELSDL FRMFDKNADG YIDLDELKMM
LQATGETITE DDIEELMKDG DKNNDGRIDY DEFLEFMKGV E
