TNNC2_MOUSE
ID TNNC2_MOUSE Reviewed; 160 AA.
AC P20801;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Troponin C, skeletal muscle;
DE AltName: Full=STNC;
GN Name=Tnnc2; Synonyms=Tncs;
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].
RC STRAIN=BALB/cJ;
RX PubMed=2394755; DOI=10.1016/s0021-9258(18)55492-2;
RA Parmacek M.S., Bengur A.R., Vora A.J., Leiden J.M.;
RT "The structure and regulation of expression of the murine fast skeletal
RT troponin C gene. Identification of a developmentally regulated, muscle-
RT specific transcriptional enhancer.";
RL J. Biol. Chem. 265:15970-15976(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
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 -!- TISSUE SPECIFICITY: Fast skeletal muscle.
CC -!- MISCELLANEOUS: Skeletal muscle troponin C binds four calcium ions.
CC -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR EMBL; M57590; AAA37642.1; -; Genomic_DNA.
DR EMBL; BC024390; AAH24390.1; -; mRNA.
DR CCDS; CCDS17056.1; -.
DR PIR; A38383; A38383.
DR RefSeq; NP_033420.1; NM_009394.2.
DR AlphaFoldDB; P20801; -.
DR BMRB; P20801; -.
DR SMR; P20801; -.
DR BioGRID; 204239; 1.
DR IntAct; P20801; 1.
DR MINT; P20801; -.
DR STRING; 10090.ENSMUSP00000099384; -.
DR iPTMnet; P20801; -.
DR PhosphoSitePlus; P20801; -.
DR SWISS-2DPAGE; P20801; -.
DR MaxQB; P20801; -.
DR PaxDb; P20801; -.
DR PeptideAtlas; P20801; -.
DR PRIDE; P20801; -.
DR ProteomicsDB; 259601; -.
DR Antibodypedia; 27766; 163 antibodies from 25 providers.
DR DNASU; 21925; -.
DR Ensembl; ENSMUST00000103095; ENSMUSP00000099384; ENSMUSG00000017300.
DR GeneID; 21925; -.
DR KEGG; mmu:21925; -.
DR UCSC; uc008nvz.1; mouse.
DR CTD; 7125; -.
DR MGI; MGI:98780; Tnnc2.
DR VEuPathDB; HostDB:ENSMUSG00000017300; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000153541; -.
DR HOGENOM; CLU_061288_2_5_1; -.
DR InParanoid; P20801; -.
DR OMA; QVEARSY; -.
DR OrthoDB; 1386217at2759; -.
DR PhylomeDB; P20801; -.
DR TreeFam; TF318191; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 21925; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Tnnc2; mouse.
DR PRO; PR:P20801; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P20801; protein.
DR Bgee; ENSMUSG00000017300; Expressed in intercostal muscle and 139 other tissues.
DR Genevisible; P20801; MM.
DR GO; GO:0005861; C:troponin complex; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
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; ISO:MGI.
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; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Metal-binding; Muscle protein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02585"
FT CHAIN 2..160
FT /note="Troponin C, skeletal muscle"
FT /id="PRO_0000073704"
FT DOMAIN 15..50
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 51..86
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 91..126
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 127..160
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P02585"
SQ SEQUENCE 160 AA; 18110 MW; 9AE469E732A0F903 CRC64;
MTDQQAEARS YLSEEMIAEF KAAFDMFDAD GGGDISVKEL GTVMRMLGQT PTKEELDAII
EEVDEDGSGT IDFEEFLVMM VRQMKEDAKG KSEEELAECF RIFDRNADGY IDAEELAEIF
RASGEHVTEE EIESLMKDGD KNNDGRIDFD EFLKMMEGVQ
