DP00166: Troponin I, cardiac muscleFASTA viewXML view

General information
DisProt:DP00166
Name:Troponin I, cardiac muscle
Synonym(s):TNNI3_HUMAN
Cardiac troponin I
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P19429
UniGene:Hs.709179
SwissProt: TNNI3_HUMAN
TrEMBL:  
NCBI (GI): 136213
Source organism:Homo sapiens (Human)
Sequence length:210
Percent disordered:42%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MADGSSDAAR EPRPAPAPIR RRSSNYRAYA TEPHAKKKSK ISASRKLQLK TLLLQIAKQE - 60
LEREAEERRG EKGRALSTRC QPLELAGLGF AELQDLCRQL HARVDKVDEE RYDIEAKVTK - 120
NITEIADLTQ KIFDLRGKFK RPTLRRVRIS ADAMMQALLG ARAKESLDLR AHLKQVKKED - 180
TEKENREVGD WRKNIDALSG MEGRKKKFES



Functional narrative    

Troponin I is a member of a complex known as Troponin, which monitors calcium levels in the muscle and initiates muscle contractions. This component works with Troponin C and T, as well as actin and tropomyosin. Troponin I functions within the subunit as an inhibitor, directly regulating the binding of calcium to Troponin C. As a member of both the EF-hand and troponin I families, Troponin I has been linked to several cardiac disorders including hypertrophic cardiomyopathy and restrictive cardiomyopathy.

Region 1: 31-34 Region 2: 66-89 Region 3: 137-148 Region 5: 189-191 Region 4: 163-210 Region 6: 192-210

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered - Extended
Name: 
Location:31 - 34
Length:4
Region sequence:

TEPH

Modification type: Complex
Engineered
Fragment
Mutant
PDB: 1J1D:C, 1J1E:C
Structural/functional type: Function arises from the disordered state
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (293 K; pH: 8; CaCl2 5 mM; glycerol (15%); LiCl 0.1 M; PEG 3350 (20%); protein 10 mg/ml; Tris-HCl 50 mM)

References:
  1. Takeda S, Yamashita A, Maeda K, Maeda Y. "Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form." Nature. 2003; 424(6944): 35-41. PubMed: 12840750

Comments:
 



Region 2
Type:Disordered - Extended
Name: 
Location:66 - 89
Length:24
Region sequence:

EERRGEKGRALSTRCQPLELAGLG

Modification type: Complex
Engineered
Fragment
Mutant
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Entropic chain
Molecular assembly
Functional subclasses: Flexible linkers/spacers
Protein-protein binding
Detection methods:
  1. X-ray crystallography (293 K; pH: 8; CaCl2 5 mM; glycerol (15%); LiCl 0.1 M; PEG3350 (20%); protein 10 mg/ml; Tris-HCl 50 mM)

References:
  1. Takeda S, Yamashita A, Maeda K, Maeda Y. "Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form." Nature. 2003; 424(6944): 35-41. PubMed: 12840750

Comments:
This disordered region becomes ordered when in complex with Troponin T.




Region 3
Type:Disordered - Extended
Name:TnI Inhibitory Region
Location:137 - 148
Length:12
Region sequence:

GKFKRPTLRRVR

Modification type: Complex
Engineered
Fragment
Mutant
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Entropic chain
Molecular recognition effectors
Functional subclasses: Flexible linkers/spacers
Protein-protein binding
Detection methods:
  1. X-ray crystallography (293 K; pH: 8; CaCl2 5 mM; glycerol (15%); LiCl 0.1 M; PEG3350 (20%); protein 10 mg/ml; Tris-HCl 50 mM)

References:
  1. Takeda S, Yamashita A, Maeda K, Maeda Y. "Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form." Nature. 2003; 424(6944): 35-41. PubMed: 12840750

Comments:
This disordered region is thought to be the binding sites for actin and tropomyosin.




Region 4
Type:Disordered - Extended
Name:C-Terminus
Location:163 - 210
Length:48
Region sequence:

AKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES

Modification type: Complex
Engineered
Fragment
Mutant
PDB: 1J1E:C
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Molecular assembly
Entropic chain
Functional subclasses: Flexible linkers/spacers
Protein-protein binding
Detection methods:
  1. X-ray crystallography (293 K; pH: 8; CaCl2 5 mM; glycerol (15%); LiCl 0.1 M; PEG3350 (20%); protein 10 mg/ml; Tris-HCl 50 mM)

References:
  1. Takeda S, Yamashita A, Maeda K, Maeda Y. "Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form." Nature. 2003; 424(6944): 35-41. PubMed: 12840750

Comments:
Residues 163-191 were disordered in one of the two Troponin I molecules that were obtained through crystallization.




Region 5
Type:Disordered - Extended
Name: 
Location:189 - 191
Length:3
Region sequence:

GDW

Modification type: Complex
Engineered
Fragment
Mutant
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Molecular assembly
Entropic chain
Functional subclasses: Flexible linkers/spacers
Protein-protein binding
Detection methods:
  1. X-ray crystallography (293 K; pH: 8; CaCl2 5 mM; glycerol (15%); LiCl 0.1 M; PEG3350 (20%); Tris-HCl 50 mM)

References:
  1. Takeda S, Yamashita A, Maeda K, Maeda Y. "Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form." Nature. 2003; 424(6944): 35-41. PubMed: 12840750

Comments:
This disordered region undergoes a conformational change when interacting with other Troponin moledules.




Region 6
Type:Disordered - Extended
Name:C-terminus
Location:192 - 210
Length:19
Region sequence:

RKNIDALSGMEGRKKKFES

Modification type: Complex
Engineered
Fragment
Mutant
PDB: 1J1E:F
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (293 K; pH: 8; CaCl2 5 mM; glycerol (15%); LiCl 0.1 M; PEG3350 (20%); protein 10 mg/ml; Tris-HCl 50 mM)

References:
  1. Takeda S, Yamashita A, Maeda K, Maeda Y. "Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form." Nature. 2003; 424(6944): 35-41. PubMed: 12840750

Comments:
 


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