[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2963002 [NCBI, ExPASy, EBI, Israel, Japan] Reinach F.C., Karlsson R.; "Cloning, expression, and site-directed mutagenesis of chicken skeletal muscle troponin C."; J. Biol. Chem. 263:2371-2376(1988).
[2]	PROTEIN SEQUENCE OF 2-163. PubMed=1908459 [NCBI, ExPASy, EBI, Israel, Japan] Golosinska K., Pearlstone J.R., Borgford T., Oikawa K., Kay C.M., Carpenter M.R., Smillie L.B.; "Determination of and corrections to sequences of turkey and chicken troponins-C. Effects of Thr-130 to Ile mutation on Ca2+ affinity."; J. Biol. Chem. 266:15797-15809(1991).
[3]	PRELIMINARY PROTEIN SEQUENCE OF 2-163. DOI=10.1016/0014-5793(76)80769-7; PubMed=992069 [NCBI, ExPASy, EBI, Israel, Japan] Wilkinson J.M.; "The amino acid sequence of troponin C from chicken skeletal muscle."; FEBS Lett. 70:254-256(1976).
[4]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). PubMed=3969570 [NCBI, ExPASy, EBI, Israel, Japan] Sundaralingam M., Bergstrom R., Strasburg G., Rao S.T., Raychowdhory P., Greaser M.L., Wang B.C.; "Molecular structure of troponin C from chicken skeletal muscle at 3-A resolution."; Science 227:945-948(1985).
[5]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). PubMed=3338985 [NCBI, ExPASy, EBI, Israel, Japan] Satyshur K.A., Rao S.T., Pyzalska D., Drendel W., Greaser M.L., Sundaralingam M.; "Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution."; J. Biol. Chem. 263:1628-1647(1988).
[6]	X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS). DOI=10.1107/S090744499300798X; PubMed=15299475 [NCBI, ExPASy, EBI, Israel, Japan] Satyshur K.A., Pyzalska D., Rao S.T., Greaser M.L., Sundaralingam M.; "Structure of chicken skeletal muscle troponin C at 1.78-A resolution."; Acta Crystallogr. D 50:40-49(1994).
[7]	X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). DOI=10.1006/jmbi.1997.1257; PubMed=9367759 [NCBI, ExPASy, EBI, Israel, Japan] Strynadka N.C., Cherney M., Sielecki A.R., Li M.X., Smillie L.B., James M.N.G.; "Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75-A resolution."; J. Mol. Biol. 273:238-255(1997).
[8]	STRUCTURE BY NMR OF 94-127. DOI=10.1021/bi00155a009; PubMed=1390738 [NCBI, ExPASy, EBI, Israel, Japan] Shaw G.S., Hodges R.S., Sykes B.D.; "Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy."; Biochemistry 31:9572-9580(1992).
[9]	STRUCTURE BY NMR. DOI=10.1021/bi00049a010; PubMed=8519752 [NCBI, ExPASy, EBI, Israel, Japan] Slupsky C.M., Sykes B.D.; "NMR solution structure of calcium-saturated skeletal muscle troponin C."; Biochemistry 34:15953-15964(1995).
[10]	STRUCTURE BY NMR. DOI=10.1021/bi982936e; PubMed=10231519 [NCBI, ExPASy, EBI, Israel, Japan] Tsuda S., Miura A., Gagne S.M., Spyracopoulos L., Sykes B.D.; "Low-temperature-induced structural changes in the Apo regulatory domain of skeletal muscle troponin C."; Biochemistry 38:5693-5700(1999).

Comments

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: Skeletal muscle troponin C binds four calcium ions.
SIMILARITY: Belongs to the troponin C family.
SIMILARITY: Contains 4 EF-hand domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M19027; AAA49097.1; ALT_SEQ; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A03015; TPCHCS.

NP_990781.1; -.

3D structure databases

PDB

1AVS; X-ray; 1.75 A; A/B=1-91.	[ExPASy / RCSB / EBI]
1BLQ; NMR; -; A=1-91.	[ExPASy / RCSB / EBI]
1EW7; Model; -; C=3-162.	[ExPASy / RCSB / EBI]
1JC2; NMR; -; A=89-163.	[ExPASy / RCSB / EBI]
1NCX; X-ray; 1.80 A; A=1-163.	[ExPASy / RCSB / EBI]
1NCY; X-ray; 2.10 A; A=1-163.	[ExPASy / RCSB / EBI]
1NCZ; X-ray; 1.80 A; A=1-163.	[ExPASy / RCSB / EBI]
1NPQ; NMR; -; A=1-91.	[ExPASy / RCSB / EBI]
1PON; NMR; -; A=94-127, B=130-163.	[ExPASy / RCSB / EBI]
1SKT; NMR; -; A=1-91.	[ExPASy / RCSB / EBI]
1SMG; NMR; -; A=1-91.	[ExPASy / RCSB / EBI]
1TNP; NMR; -; A=1-91.	[ExPASy / RCSB / EBI]
1TNQ; NMR; -; A=1-91.	[ExPASy / RCSB / EBI]
1TNW; NMR; -; A=1-163.	[ExPASy / RCSB / EBI]
1TNX; NMR; -; A=1-163.	[ExPASy / RCSB / EBI]
1TOP; X-ray; 1.78 A; A=1-163.	[ExPASy / RCSB / EBI]
1YTZ; X-ray; 3.00 A; C=1-163.	[ExPASy / RCSB / EBI]
1YV0; X-ray; 7.00 A; C=1-163.	[ExPASy / RCSB / EBI]
1ZAC; NMR; -; A=1-91.	[ExPASy / RCSB / EBI]
4TNC; X-ray; 2.00 A; A=6-163.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AVS; -.
1BLQ; -.
1EW7; -.
1JC2; -.
1NCX; -.
1NCY; -.
1NCZ; -.
1NPQ; -.
1PON; -.
1SKT; -.
1SMG; -.
1TNP; -.
1TNQ; -.
1TNW; -.
1TNX; -.
1TOP; -.
1YTZ; -.
1YV0; -.
1ZAC; -.
4TNC; -.

ModBase

P02588.

Family and domain databases

InterPro

IPR011992; EF-Hand_type.
IPR002048; EF_hand_Ca_bd.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.238.10; EF-Hand_type; 1.

Pfam

PF00036; efhand; 4.
Pfam graphical view of domain structure.

ProDom

PD000012; EF-hand; 2.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00054; EFh; 4.
SMART graphical view of domain structure.

PROSITE

PS00018; EF_HAND_1; 4.
PS50222; EF_HAND_2; 4.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSGALG00000006835; Gallus gallus. [Contig view]

GeneID

396434; -.

KEGG

gga:396434; -.

Phylogenomic databases

HOGENOM

P02588; -.

HOVERGEN

P02588; -.

Other

LinkHub

P02588; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Direct protein sequencing; Muscle protein; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 163`	`162`	`Troponin C, skeletal muscle.`	`PRO_0000073707`
`DOMAIN`	`18 53`	`36`	`EF-hand 1.`
`DOMAIN`	`54 89`	`36`	`EF-hand 2.`
`DOMAIN`	`94 129`	`36`	`EF-hand 3.`
`DOMAIN`	`130 163`	`34`	`EF-hand 4.`
`CA_BIND`	`31 42`	`12`	`1.`
`CA_BIND`	`67 78`	`12`	`2.`
`CA_BIND`	`107 118`	`12`	`3.`
`CA_BIND`	`143 154`	`12`	`4.`
`MOD_RES`	`2 2`		`Blocked amino end (Ala).`
`MUTAGEN`	`131 131`		`T->I: Decreases calcium affinity.`
`HELIX`	`11 14`	`4`
`HELIX`	`17 30`	`14`
`STRAND`	`35 38`	`4`
`HELIX`	`40 49`	`10`
`HELIX`	`56 66`	`11`
`STRAND`	`72 75`	`4`
`HELIX`	`76 87`	`12`
`HELIX`	`92 106`	`15`
`STRAND`	`111 114`	`4`
`HELIX`	`116 124`	`9`
`HELIX`	`132 142`	`11`
`STRAND`	`147 150`	`4`
`HELIX`	`152 160`	`9`

Sequence information

Length: 163 AA [This is the length of the unprocessed precursor]

Molecular weight: 18375 Da [This is the MW of the unprocessed precursor]

CRC64: C4E1D9F40FFED3BC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASMTDQQAE ARAFLSEEMI AEFKAAFDMF DADGGGDIST KELGTVMRML GQNPTKEELD 

        70         80         90        100        110        120 
AIIEEVDEDG SGTIDFEEFL VMMVRQMKED AKGKSEEELA NCFRIFDKNA DGFIDIEELG 

       130        140        150        160 
EILRATGEHV TEEDIEDLMK DSDKNNDGRI DFDEFLKMME GVQ

P02588 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools