TNNC2_HUMAN
ID TNNC2_HUMAN Reviewed; 160 AA.
AC P02585; Q6FH92;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Troponin C, skeletal muscle;
GN Name=TNNC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3166492; DOI=10.1016/0022-2836(88)90145-3;
RA Gahlmann R., Wade R., Gunning R., Kedes L.;
RT "Differential expression of slow and fast skeletal muscle troponin C. Slow
RT skeletal muscle troponin C is expressed in human fibroblasts.";
RL J. Mol. Biol. 201:379-391(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2373703; DOI=10.1016/s0021-9258(19)38376-0;
RA Gahlmann R., Kedes L.;
RT "Cloning, structural analysis, and expression of the human fast twitch
RT skeletal muscle troponin C gene.";
RL J. Biol. Chem. 265:12520-12528(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RA Wu Q.L.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [9]
RP PROTEIN SEQUENCE OF 2-160, AND ACETYLATION AT THR-2.
RC TISSUE=Skeletal muscle;
RX PubMed=978749; DOI=10.1007/bf01730999;
RA Romero-Herrera A.E., Castillo O., Lehmann H.;
RT "Human skeletal muscle proteins. The primary structure of troponin C.";
RL J. Mol. Evol. 8:251-270(1976).
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 -!- INTERACTION:
CC P02585; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-10249681, EBI-1644036;
CC P02585; P19429: TNNI3; NbExp=3; IntAct=EBI-10249681, EBI-704146;
CC P02585; Q6FGX2: TNNI3; NbExp=3; IntAct=EBI-10249681, EBI-10249686;
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; X07898; CAA30737.1; -; mRNA.
DR EMBL; M33772; AAA61197.1; -; Genomic_DNA.
DR EMBL; M33771; AAA61197.1; JOINED; Genomic_DNA.
DR EMBL; M22307; AAA91854.1; -; mRNA.
DR EMBL; AK291323; BAF84012.1; -; mRNA.
DR EMBL; CR541864; CAG46662.1; -; mRNA.
DR EMBL; CR541884; CAG46682.1; -; mRNA.
DR EMBL; CH471077; EAW75803.1; -; Genomic_DNA.
DR EMBL; AL050348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005323; AAH05323.1; -; mRNA.
DR CCDS; CCDS13375.1; -.
DR PIR; A36574; TPHUCS.
DR RefSeq; NP_003270.1; NM_003279.2.
DR PDB; 7KAA; NMR; -; A=1-88.
DR PDBsum; 7KAA; -.
DR AlphaFoldDB; P02585; -.
DR BMRB; P02585; -.
DR SMR; P02585; -.
DR BioGRID; 112980; 65.
DR IntAct; P02585; 7.
DR STRING; 9606.ENSP00000361636; -.
DR ChEMBL; CHEMBL3831282; -.
DR DrugBank; DB01373; Calcium.
DR DrugBank; DB01023; Felodipine.
DR DrugBank; DB04682; Octylphenoxy polyethoxyethanol.
DR iPTMnet; P02585; -.
DR PhosphoSitePlus; P02585; -.
DR BioMuta; TNNC2; -.
DR DMDM; 136043; -.
DR MassIVE; P02585; -.
DR PaxDb; P02585; -.
DR PeptideAtlas; P02585; -.
DR PRIDE; P02585; -.
DR ProteomicsDB; 51535; -.
DR Antibodypedia; 27766; 163 antibodies from 25 providers.
DR DNASU; 7125; -.
DR Ensembl; ENST00000372555.8; ENSP00000361636.3; ENSG00000101470.10.
DR GeneID; 7125; -.
DR KEGG; hsa:7125; -.
DR MANE-Select; ENST00000372555.8; ENSP00000361636.3; NM_003279.3; NP_003270.1.
DR UCSC; uc002xpr.4; human.
DR CTD; 7125; -.
DR DisGeNET; 7125; -.
DR GeneCards; TNNC2; -.
DR HGNC; HGNC:11944; TNNC2.
DR HPA; ENSG00000101470; Group enriched (skeletal muscle, tongue).
DR MIM; 191039; gene.
DR neXtProt; NX_P02585; -.
DR OpenTargets; ENSG00000101470; -.
DR PharmGKB; PA36633; -.
DR VEuPathDB; HostDB:ENSG00000101470; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000153541; -.
DR InParanoid; P02585; -.
DR OMA; QVEARSY; -.
DR OrthoDB; 1386217at2759; -.
DR PhylomeDB; P02585; -.
DR TreeFam; TF318191; -.
DR PathwayCommons; P02585; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; P02585; -.
DR SIGNOR; P02585; -.
DR BioGRID-ORCS; 7125; 14 hits in 1066 CRISPR screens.
DR ChiTaRS; TNNC2; human.
DR GeneWiki; TNNC2; -.
DR GenomeRNAi; 7125; -.
DR Pharos; P02585; Tbio.
DR PRO; PR:P02585; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P02585; protein.
DR Bgee; ENSG00000101470; Expressed in skeletal muscle tissue of rectus abdominis and 116 other tissues.
DR ExpressionAtlas; P02585; baseline and differential.
DR Genevisible; P02585; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005861; C:troponin complex; IDA:UniProtKB.
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; IDA:UniProtKB.
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; 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 3D-structure; Acetylation; Calcium; Direct protein sequencing;
KW Metal-binding; Muscle protein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:978749"
FT CHAIN 2..160
FT /note="Troponin C, skeletal muscle"
FT /id="PRO_0000073703"
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:0000269|PubMed:978749"
FT CONFLICT 2..3
FT /note="TD -> DT (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="E -> G (in Ref. 3; AAA91854)"
FT /evidence="ECO:0000305"
FT HELIX 4..10
FT /evidence="ECO:0007829|PDB:7KAA"
FT HELIX 14..20
FT /evidence="ECO:0007829|PDB:7KAA"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:7KAA"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:7KAA"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:7KAA"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:7KAA"
FT HELIX 73..88
FT /evidence="ECO:0007829|PDB:7KAA"
SQ SEQUENCE 160 AA; 18122 MW; EA93729732A0F916 CRC64;
MTDQQAEARS YLSEEMIAEF KAAFDMFDAD GGGDISVKEL GTVMRMLGQT PTKEELDAII
EEVDEDGSGT IDFEEFLVMM VRQMKEDAKG KSEEELAECF RIFDRNADGY IDPEELAEIF
RASGEHVTDE EIESLMKDGD KNNDGRIDFD EFLKMMEGVQ
