P02588 (TNNC2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Troponin C, skeletal muscle

Gene names

Name:

TNNC2

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	163 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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.
Sequence similarities	Belongs to the troponin C family. Contains 4 EF-hand domains.

Ontologies

Keywords
Domain	Repeat
Ligand	Calcium
Molecular function	Muscle protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2 Ref.3

Chain

2 – 163

162

Troponin C, skeletal muscle

PRO_0000073707

Regions

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

Calcium binding

31 – 42

12

1

Calcium binding

67 – 78

12

2

Calcium binding

107 – 118

12

3

Calcium binding

143 – 154

12

4

Amino acid modifications

Modified residue

2

1

Blocked amino end (Ala)

Experimental info

Mutagenesis

131

1

T → I: Decreases calcium affinity.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

163

Helix Strand Turn

Details...

Helix

11 – 14

4

Helix

17 – 30

14

Beta strand

35 – 38

4

Helix

40 – 49

10

Helix

56 – 66

11

Beta strand

72 – 75

4

Helix

76 – 87

12

Helix

92 – 106

15

Beta strand

111 – 114

4

Helix

116 – 124

9

Helix

132 – 142

11

Beta strand

147 – 150

4

Helix

152 – 160

9

Sequences

	Sequence		Length	Mass (Da)
	P02588 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C4E1D9F40FFED3BC	FASTA	163	18,375
	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

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19027 mRNA. Translation: AAA49097.1. Sequence problems.

IPI

IPI00600948.

PIR

TPCHCS. A03015.

RefSeq

NP_990781.1. NM_205450.1.

UniGene

Gga.823.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AVS	X-ray	1.75	A/B	2-91	[»]
1BLQ	NMR	-	A	2-90	[»]
1CTA	NMR	-	A/B	94-126	[»]
1CTD	NMR	-	A/B	94-126	[»]
1EW7	model	-	C	3-162	[»]
1JC2	NMR	-	A	89-163	[»]
1NCX	X-ray	1.80	A	2-162	[»]
1NCY	X-ray	2.10	A	2-162	[»]
1NCZ	X-ray	1.80	A	2-162	[»]
1NPQ	NMR	-	A	2-90	[»]
1PON	NMR	-	A	94-126	[»]
			B	130-162	[»]
1SKT	NMR	-	A	2-91	[»]
1SMG	NMR	-	A	2-90	[»]
1TNP	NMR	-	A	2-90	[»]
1TNQ	NMR	-	A	2-90	[»]
1TNW	NMR	-	A	2-163	[»]
1TNX	NMR	-	A	2-163	[»]
1TOP	X-ray	1.78	A	2-163	[»]
1YTZ	X-ray	3.00	C	2-162	[»]
1YV0	X-ray	7.00	C	2-162	[»]
1ZAC	NMR	-	A	2-91	[»]
2W49	electron microscopy	35.00	0/3/6/9	5-163	[»]
2W4U	electron microscopy	35.00	0/3/6/9	5-163	[»]
4TNC	X-ray	2.00	A	6-163	[»]

ProteinModelPortal

P02588.

SMR

P02588. Positions 2-163.

ModBase

Search...

Protein-protein interaction databases

IntAct

P02588. 2 interactions.

MINT

MINT-252237.

STRING

P02588.

Proteomic databases

PRIDE

P02588.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

396434.

KEGG

gga:396434.

Organism-specific databases

CTD

7125.

Phylogenomic databases

eggNOG

veNOG19363.

GeneTree

ENSGT00560000076590.

HOGENOM

HBG746798.

HOVERGEN

HBG012180.

InParanoid

P02588.

OrthoDB

EOG4Z0B6X.

PhylomeDB

P02588.

Family and domain databases

InterPro

IPR018248. EF-hand.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 2 hits.

KO

K12042.

Pfam

PF00036. efhand. 3 hits.
[Graphical view]

SMART

SM00054. EFh. 4 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TNNC2_CHICK

Accession

Primary (citable) accession number: P02588

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 112 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program