1A8Y,1SJI


Conserved Protein Domain Family
PDI_b_Calsequestrin_N

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cd03065: PDI_b_Calsequestrin_N 
Click on image for an interactive view with Cn3D
PDIb family, Calsequestrin subfamily, N-terminal TRX-fold domain; Calsequestrin is the major calcium storage protein in the sarcoplasmic reticulum (SR) of skeletal and cardiac muscle. It stores calcium ions in sufficient quantities (up to 20 mM) to allow repetitive contractions and is essential to maintain movement, respiration and heart beat. A missense mutation in human cardiac calsequestrin is associated with catecholamine-induced polymorphic ventricular tachycardia (CPVT), a rare disease characterized by seizures or sudden death in response to physiologic or emotional stress. Calsequestrin is a highly acidic protein with up to 50 calcium binding sites formed simply by the clustering of two or more acidic residues. The monomer contains three redox inactive TRX-fold domains. Calsequestrin is condensed as a linear polymer in the SR lumen and is membrane-anchored through binding with intra-membrane proteins triadin, junctin and ryanodine receptor (RyR) Ca2+ release channel. In addition to its role as a calcium ion buffer, calsequestrin also regulates the activity of the RyR channel, coordinating the release of calcium ions from the SR with the loading of the calcium store. The N-terminal TRX-fold domain (or domain I) mediates front-to-front dimer interaction, an important feature in the formation of calsequestrin polymers.
Statistics
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PSSM-Id: 239363
Aligned: 11 rows
Threshold Bit Score: 166.457
Created: 19-Apr-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
front-to-front
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:front-to-front dimer interface [polypeptide binding site]
Evidence:
  • Structure:1SJI; Canis familiaris cardiac calsequestrin dimer; contacts at 3.5A
    View structure with Cn3D
  • Comment:The front-to-front dimer interface of calsequestrin is formed primarily by residues from the N-terminal TRX-fold domain (or domain I). Polymerization occurs by the formation of additional back-to-back interactions between calsequestrin monomers through residues in the C-terminal TRX-fold domain (or domain III).

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        # # #####                                 #  ## #      #           #            
1A8Y           5 DFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPed-dkASQRQFEMEELILELAAQVLED---KGVGFGLVDSEKD 80  Oryctolagus cun...
1SJI_B         3 NFPTYDGKDRVVSLTEKNFKQVLKKYDVLCLYYHESVss-dkVAQKQFQLKEIVLELVAQVLEH---KDIGFVMVDAKKE 78  dog
AAA48674       5 NFPTYDGKDRVIDLNEKNYKHALKKYDMLCLLFHEPVss-drVSQKQFQMTEMVLELAAQVLEP---RSIGFGMVDSKKD 80  chicken
CAA93667      34 PDLEYDGFDRTEVLTEKNFNRTVFAEDTKSVVFFNDVe----EDDSELDQYECFLQLSAQIMTK---RGYNFYTVNTTKE 106 Caenorhabditis ...
NP_001223     24 NFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVss-dkVTPKQFQLKEIVLELVAQVLEH---KAIGFVMVDAKKE 99  human
AAH41283      45 HFPTYDGKDRVLELGEKNYRQLMKKHKVFCILLQTAPpsgdkIAQRRLHLTDMVLELTAQVLER---KQIGFGLLDPKKN 121 African clawed ...
AAH46947      27 DFPEYDGEDRVININLKNYKAALKKYEVLALLYHEPIed-dkASQRQFEMEELIFELAAQVLED---KGVGFGLVDSEKD 102 African clawed ...
CAE17619      25 DIPEYDGKDRVHELNAKNYKSVMKKYDVMVVYYHEHVgs-skVAQKQFQIEELALELAAQVLADfddEDIGIGLLDEKTD 103 zebrafish
NP_001002682  25 EFPRYDGEDRVLDIDDKNYRKALKKYDMLCLFYHAPPpa-akELQKQLHLTELVLELAAQVLEE---KDIGFGMVDSQKD 100 zebrafish
CAI15276      39 DFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPed-dkASQRQFEMEELILELAAQVLED---KGVGFGLVDSEKD 114 human
BAC86117      25 EIPEYDGKDRVHDLNAKNYKSVMKKYDVMVIYYHAHVes-nkNAQKAFEMEELALELAAQVLDDlddEDIGFGLVDEKKD 103 human
Feature 1                                                     
1A8Y          81 AAVAK-KLGLTEEDSIYVFKEDEVIEYDGEFSADTLVEFLLDVLE 124 Oryctolagus cuniculus
1SJI_B        79 AKLAK-KLGFDEEGSLYVLKGDRTIEFDGEFAADVLVEFLLDLIE 122 dog
AAA48674      81 AKLAK-KLGLVEEGSLYVFKEERLIEFDGELATDVLVEFLLDLLE 124 chicken
CAA93667     107 HRLRKqEEVEKGEDTIHVYKDGYKIEYNGVRDPETFVSWLMDIPD 151 Caenorhabditis elegans
NP_001223    100 AKLAK-KLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIE 143 human
AAH41283     122 SKIAK-KLGCSEEGSLYVFKEDNVIEFDGEMAADVIVDFLLDLIE 165 African clawed frog
AAH46947     103 AAVAK-KLGLDEEDSIYVFKDDEVIEYDGEFAADTLVEFLLDVLE 146 African clawed frog
CAE17619     104 KAVAK-KLGLDEADSIFIFIEDEVIEYDGELAADTLVEFIYDVIE 147 zebrafish
NP_001002682 101 AKVAK-KLGLHEEGSVYIFKDDRVIEFDGLPSADTLVEFLLDLLE 144 zebrafish
CAI15276     115 AAVAK-KLGLTEVDSMYVFKGDEVIEYDGEFSADTIVEFLLDVLE 158 human
BAC86117     104 LSVAK-KLGLDEVESIYIFVDNEIIEYDGELAADTLVEFLYDVIE 147 human

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