DP00132: Calsequestrin-1FASTA viewXML view

General information
DisProt:DP00132
Name:Calsequestrin-1
Synonym(s):CASQ1_RABIT
Calsequestrin, skeletal muscle isoform
Aspartactin
Laminin-binding protein
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P07221
UniGene:Ocu.6275
SwissProt: CASQ1_RABIT
TrEMBL:  
NCBI (GI): 115537
Source organism:Oryctolagus cuniculus (Rabbit)
Sequence length:395
Percent disordered:100%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MNAADRMGAR VALLLLLVLG SPQSGVHGEE GLDFPEYDGV DRVINVNAKN YKNVFKKYEV - 60
LALLYHEPPE DDKASQRQFE MEELILELAA QVLEDKGVGF GLVDSEKDAA VAKKLGLTEE - 120
DSIYVFKEDE VIEYDGEFSA DTLVEFLLDV LEDPVELIEG ERELQAFENI EDEIKLIGYF - 180
KNKDSEHYKA FKEAAEEFHP YIPFFATFDS KVAKKLTLKL NEIDFYEAFM EEPVTIPDKP - 240
NSEEEIVNFV EEHRRSTLRK LKPESMYETW EDDMDGIHIV AFAEEADPDG YEFLEILKSV - 300
AQDNTDNPDL SIIWIDPDDF PLLVPYWEKT FDIDLSAPQI GVVNVTDADS VWMEMDDEED - 360
LPSAEELEDW LEDVLEGEIN TEDDDDEDDD DDDDD



Functional narrative    

Calsequestrin is present in skeletal muscle and functions by binding and storing calcium for use by the muscles cells. Calsequestrin interacts with calcium and laminin predominantly, however, it has also been shown to interact with potassium, strontium, terbium, zinc, and protons. Located in the sarcoplasmic reticulum of fast skeletal muscle cells and a member of the calsequestrin protein family, this protein is believed to be intrinsically disordered. However, under certain conditions, such as in the presence of calcium, this protein undergoes a conformational change and becomes highly ordered.

Region 2: 1-4 Region 3: 328-333 Region 4: 352-367 Region 1: 1-395

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:1 - 395
Length:395
Region sequence:

MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEV
LALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEE
DSIYVFKEDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYF
KNKDSEHYKAFKEAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKP
NSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGYEFLEILKSV
AQDNTDNPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEED
LPSAEELEDWLEDVLEGEINTEDDDDEDDDDDDDD

Modification type: Isoform
Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, near-UV (pH: 7.5; )

  2. Nuclear magnetic resonance (NMR) (278 K; pH: 7.5; )

  3. Analytical ultracentrifugation

  4. SDS-PAGE gel, Aberrant mobility on (pH: 7.5; )
References:
  1. Aaron BM, Oikawa K, Reithmeier RA, Sykes BD. "Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy." J Biol Chem. 1984; 259(19): 11876-81. PubMed: 6480588

  2. Cozens B, Reithmeier RA. "Size and shape of rabbit skeletal muscle calsequestrin." J Biol Chem. 1984; 259(10): 6248-52. PubMed: 6725251

  3. Ostwald TJ, MacLennan DH, Dorrington KJ. "Effects of cation binding on the conformation of calsequestrin and the high affinity calcium-binding protein of sarcoplasmic reticulum." J Biol Chem. 1974; 249(18): 5867-71. PubMed: 4472093
Comments:
 



Region 2
Type:Disordered
Name: 
Location:1 - 4
Length:4
Region sequence:

MNAA

Modification type: Isoform
Native
PDB: 1A8Y:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Unknown
Functional subclasses: Protein-protein binding
Substrate/ligand binding
Detection methods:
  1. X-ray crystallography (277 K; pH: 6.5; )
References:
  1. Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH. "Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum." Nat Struct Biol. 1998; 5(6): 476-83. PubMed: 9628486
Comments:
 



Region 3
Type:Disordered
Name: 
Location:328 - 333
Length:6
Region sequence:

EKTFDI

Modification type: Isoform
Native
PDB: 1A8Y:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Unknown
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. X-ray crystallography (277 K; pH: 6.5; )
References:
  1. Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH. "Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum." Nat Struct Biol. 1998; 5(6): 476-83. PubMed: 9628486
Comments:
 



Region 4
Type:Disordered
Name: 
Location:352 - 367
Length:16
Region sequence:

WMEMDDEEDLPSAEEL

Modification type: Isoform
Native
PDB: 1A8Y:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Unknown
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. X-ray crystallography (277 K; pH: 6.5; )
References:
  1. Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH. "Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum." Nat Struct Biol. 1998; 5(6): 476-83. PubMed: 9628486
Comments:
 


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