4PHJ,1AJ5,1ALW,1DF0,1DVI,1QXP,1KFX,4PHN


Conserved Protein Domain Family
EFh_PEF_CPNS1_2

?
cd16188: EFh_PEF_CPNS1_2 
Click on image for an interactive view with Cn3D
Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit CAPNS1 and CAPNS2
CAPNS1, also termed calpain small subunit 1 (CSS1), or calcium-activated neutral proteinase small subunit (CANP small subunit), or calcium-dependent protease small subunit (CDPS), or calpain regulatory subunit, is a common 28-kDa regulatory calpain subunit encoded by the calpain small 1 (Capns1, also known as Capn4) gene. It acts as a binding partner to form a heterodimer with the 80 kDa calpain large catalytic subunit and is required in maintaining the activity of calpain. CAPNS1 plays a significant role in tumor progression of human cancer, and functions as a potential therapeutic target in human hepatocellular carcinoma (HCC), nasopharyngeal carcinoma (NPC), glioma, and clear cell renal cell carcinoma (ccRCC). It may be involved in regulating migration and cell survival through binding to the SH3 domain of Ras GTPase-activating protein (RasGAP). It may also modulate Akt/FoxO3A signaling and apoptosis through PP2A. CAPNS1 contains an N-terminal glycine rich domain and a C-terminal PEF-hand domain. CAPNS2, also termed calpain small subunit 2 (CSS2), is a novel tissue-specific 30 kDa calpain small subunit that lacks two oligo-Gly stretches characteristic of the N-terminal Gly-rich domain of CAPNS1. CAPNS2 acts as a chaperone for the calpain large subunit, and appears to be the functional equivalent of CAPNS1. However, CAPNS2 binds the large subunit much more weakly than CAPNS1 and it does not undergo the autolytic conversion typical of CAPNS1.
Statistics
?
PSSM-Id: 320063
View PSSM: cd16188
Aligned: 17 rows
Threshold Bit Score: 310.134
Threshold Setting Gi: 395503780
Created: 13-Feb-2015
Updated: 18-Aug-2016
Structure
?
Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:Ca binding site [ion binding site]
Evidence:
  • Structure:4PHJ; Homo sapiens calpain small subunit 1 binds four Ca2+ ions, through its EF1, EF2, EF3, and EF4 hands.
    View structure with Cn3D

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                    #      #                 #                # #      #                
4PHJ_A         5 QFRRLFAQLAGDDMEVSATELMNILNKVVtrhpDLKTDGFGiDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKRWQAIYK 84
1ALW_A         5 QFRRLFAQLAGDDMEVSATELMNILNKVVtrhpDLKTDGFGiDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKKWQAIYK 84
4PHN_A         5 QFRRLFAQLAGDDMEVSATELMNILNKVVtrhpDLKTDGFGiDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKKWQAIYK 84
gi 2506056    46 QFRRLFTQLAGDDMEVSPTELMNILNKVVtrhpDLKTDGFGlDTCRSMVAVMDSDTTGKLGFEEFKYLWNNIKKWQLVYK 125
gi 45476965   80 RFRQQFTQLAGPDMEVGATDLMNILNKVLskhkDLKTDGFSlDTCRSIVSVMDSDTTGKLGFEEFKYLWNNIKKWQCVYK 159
gi 51873936   59 QFRRLFSQLAGDDMEVSAAELMGILNKVVarhqDLKTDGFSvDSCRSMVAVMDSDSTGKLGFEEFKYLWDNIKKWQGVYK 138
gi 91754190   48 QFRKVFNQLAGDDMEVSPTELMNILNKIIskhgDLKTDGFTiESCRSMVAVMDSDSTGKLGFHEFKHLWNNIKKWQGIYK 127
gi 147904973 164 QFRRLFKQLAGEDMEVNADELKNVLDKVVakhqDLKTSGFSiDTCRSMVAIMDSDGTGKLGFEEFKYLWNNIKKWQCIYK 243
gi 513203183  80 QFRRLFVQLAGDDMEVSATELRNILNKVLsrhqDLKTDGFSlDTCRSMVAVMDTDTNGKLGFEEFKYLWNNIKKWQCAYK 159
gi 543732308  80 RFRRLFAQLAGDDMEVCATELRDILNKVVsrhqDLKTNGFSlDTCRSMVAVMDTDTNGKLGFEEFKYLWNNIKKWQGVYK 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1          # # #      #                               # ##                               
4PHJ_A        85 QFDTDRSGTICSSELPGAFEAAGFhlnehLYNMIIRRYSDESGNMDFDNFISCLVRLDAMFRAFKSLDKDGTGQIQVNIQ 164
1ALW_A        85 QFDVDRSGTIGSSELPGAFEAAGFhlnehLYSMIIRRYSDEGGNMDFDNFISCLVRLDAMFRAFKSLDKDGTGQIQVNIQ 164
4PHN_A        85 QFDVDRSGTIGSSELPGAFEAAGFhlnehLYSMIIRRYSDEGGNMDFDNFISCLVRLDAMFRAFKSLDKDGTGQIQVNIQ 164
gi 2506056   126 RFDTDRSGTIGVQELPGAFEAAGFrlppeLWGVLGRRYGDEGGNLDFDNFISCLVRLDAMFRAFKSLDRDGSGQIRVSLQ 205
gi 45476965  160 QYDRDHSGSLGSSQLRGALQAAGFqlneqLYQMIVRRYANEDGDMDFNNFISCLVRLDAMFRAFKSLDRDRDGLIQVSIK 239
gi 51873936  139 RYDTDRSGTIGRNELPGAFSSAGFqlngqLYEMIVRRYSDENGEMDFDNYICCLVRLDAMFRAFKTLDKDGDGQIKVTIE 218
gi 91754190  128 TYDRDHSGTIGADELPAAFRAAGFpltdqLFQMIIRRYSDESGNMDFDNYIGCLVRLDAMCHAFKTLDKDNDGTIKVNVQ 207
gi 147904973 244 QFDTERSGYINCQALPGALKAAGFdlhdqLHVLLARRYADESGNINFDSFISALVRLDAMYRAFKALDRENTGQVQVRMP 323
gi 513203183 160 RCDTNQSGILERAQLPAALRAAGFqlneqLCQVIMRRYASEDGSMDFNNFISCLVRLDSMFRAFKSLDRNGNGQIKMTIE 239
gi 543732308 160 QYDTNQSGTVGRAQLPDALKAAGFhlneqLCQVIVRRYADEDGSMDFNSFISCLVRLDGMFRAFKSLDRDGNGQIKVTIE 239

                 ....*....
Feature 1                 
4PHJ_A       165 EWLQLTMYS 173
1ALW_A       165 EWLQLTMYS 173
4PHN_A       165 EWLQLTMYS 173
gi 2506056   206 EWLQLTMYS 214
gi 45476965  240 EWLQLTMYS 248
gi 51873936  219 EWLQLTMYS 227
gi 91754190  208 EWLQLTMYS 216
gi 147904973 324 EWLKLTIYS 332
gi 513203183 240 DWLQLTMYS 248
gi 543732308 240 DWLQLTMYS 248

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap