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DP00291: Calsenilin [Isoform 1]FASTA viewXML view

General information
DisProt:DP00291
Name:Calsenilin [Isoform 1]
Synonym(s):CSEN_MOUSE
Kv channel-interacting protein 3
KChIP3
A-type potassium channel modulatory protein 3
DRE-antagonist modulator
DREAM
First appeared in release:Release 3.0 (02/17/2006)
UniProt:Q9QXT8-1
UniGene:Mm.315292
SwissProt: CSEN_MOUSE
TrEMBL:  
NCBI (GI): 73620954
Source organism:Mus musculus (Mouse)
Sequence length:256
Percent disordered:75%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MQRTKEAVKA SDGSLLGDPG RIPLSKRESI KWQRPRFTRQ ALMRCCLIKW ILSSAAPQGS - 60
DSSDSELELS TVRHQPEGLD QLQAQTKFTK KELQSLYRGF KNECPTGLVD EDTFKLIYSQ - 120
FFPQGDATTY AHFLFNAFDA DGNGAIHFED FVVGLSILLR GTVHEKLKWA FNLYDINKDG - 180
CITKEEMLAI MKSIYDMMGR HTYPILREDA PLEHVERFFQ KMDRNQDGVV TIDEFLETCQ - 240
KDENIMNSMQ LFENVI



Functional narrative    

Calcium-dependent transcriptional repressor that binds to the DRE element of genes including PDYN and FOS. Affinity for DNA is reduced upon binding to calcium and enhanced by binding to magnesium. Seems to be involved in nociception. Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Probably modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and probably KCND3 trafficking to the cell surface By similarity. May play a role in the regulation of PSEN2 proteolytic processing and apoptosis. Together with PSEN2 involved in modulation of beta-amyloid formation.

Region 1: 65-256

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 - Molten Globule
Name:DREAM-C
Location:65 - 256
Length:192
Region sequence:

SELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYSQFFPQ
GDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGCITK
EEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVVTIDEFLETCQKDEN
IMNSMQLFENVI

Modification type: Fragment
Mutant
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Protein-DNA binding
Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (305 K; [2H10]dithiothreitol 5 mM; [2H11]Tris (pH 7.4) 10 mM; EDTA 5 mM; H2O/2H2O (5%/95%) 0.3 ml; KCl 50 mM; protein (0.2 to 0.5 mM))
References:
  1. Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. "Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM." J Biol Chem. 2005; 280(18): 18008-14. PubMed: 15746104
Comments:
DREAM-C is a mutant containing residues 65-256 of the full length protein, and contains the mutant residues D150N, E186Q, and E234Q.


Comments


The authors used a natural variant of the protein in which there is an N to S conversion that is associated with certain strains. View natural variations section of UniProt entry.


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