1EF1,3U8Z,2YVC,2D2Q,1J19,2EMT,1GC6,2ZPY,1SGH


Conserved Protein Domain Family
FERM_C_ERM

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cd13194: FERM_C_ERM 
Click on image for an interactive view with Cn3D
FERM domain C-lobe/F3 of the ERM family
The ERM family includes ezrin, radixin, moesin and merlin. They are composed of a N-terminal FERM (ERM) domain (also called N-ERMAD (N-terminal ERM association domain)), a coiled coil region (CRR), and a C-terminal domain CERMAD (C-terminal ERM association domain) which has an F-actin-binding site (ABD). Two actin-binding sites have been identified in the middle and N-terminal domains. Merlin is structurally similar to the ERM proteins, but instead of an actin-binding domain (ABD), it contains a C-terminal domain (CTD), just like the proteins from the 4.1 family. Activated ezrin, radixin and moesin are thought to be involved in the linking of actin filaments to CD43, CD44, ICAM1-3 cell adhesion molecules, various membrane channels and receptors, such as the Na+/H+ exchanger-3 (NHE3), cystic fibrosis transmembrane conductance regulator (CFTR), and the beta2-adrenergic receptor. The ERM proteins exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain of ERM is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.
Statistics
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PSSM-Id: 270015
View PSSM: cd13194
Aligned: 37 rows
Threshold Bit Score: 155.124
Threshold Setting Gi: 198423742
Created: 6-Dec-2011
Updated: 22-Oct-2014
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:phosphoinositide binding site [chemical binding site]
Evidence:
  • Structure:1GC6; Mouse Radixin FERM F3 binds inositol-(1,4, 5)-trisphosphate (IP3), contacts at 4A
    View structure with Cn3D
  • Comment:These residues differ from PIP2 binding sites identified by in vitro studies

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
1EF1_A       197 XYGVNYFSIKNkkGSELWLGVDALGLNIYEqnDRLTPKIGFPWSEIRNISFNDKKFVIKPIDk----------------- 259
1GC6_A       200 MYGVNYFEIKNkkGTELWLGVDALGLNIYEhdDKLTPKIGFPWSEIRNISFNDKKFVIKPIDk----------------- 262
gi 17553374  210 MYGILYYPICNnkETDLHLGISAQGLGIYKgvNRITPRPFFSWSEIKNIQFKNRKFHMKTVD------------------ 271
gi 133778420 206 MFGVSLFKIKNnkGSELCLGINAVSVNVYEpdNQLLPIVSFQWSELADMSFSDNKFVIKQSSlptirsgtlrrgatmses 285
gi 198423742 214 MSGVQYFKIKDgnGADLWLGIDAKSVSMYPynDQLHPTKSYQWSELADMSYYGNKFVIKQTTrpnntntigrrfn-lgas 292
gi 167515612 225 QFAMLRYDIKNknGTPLVLGVSPRGLYVFRlnNMQKPVVTFSWAECSELAFADKKFTICVHDk----------------- 287
gi 255760088 318 MYGVNYFPITNknKTKLWLGVTSVGLNIYDerDKLTPKTTFQWNEIRHVSFDDKKFTIRLVDa----------------- 380
gi 386783915 145 MFGVNYFNIKNkkGSELLLGVDALGLSIYKqdNKLTPTIGFPWSEIKNVSYSNKKFTIKSSDk----------------- 207
gi 326429935 205 MYGVNYFPIKNkrGTLLWLGVDALGLNIYKsnDKLTPSISFPWSEIKTVSYNDRKFVIKPLDk----------------- 267
gi 91077028  192 MYGVTFFKIKNrkGTDVLLGVNALGLDIYKpeDKLNPQISFPWAEIKNLKFKDRKFVIKPTDk----------------- 254
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
Feature 1                              #   #              
1EF1_A       260 -------kAPDFVFYAPRLRINKRILALCXGNHELYXRRRK 293
1GC6_A       263 -------kAPDFVFYAPRLRINKRILALCMGNHELYMRRRK 296
gi 17553374  272 --------KSTISFRSRETSIDSSILDLCIGTHNLYLRRRQ 304
gi 133778420 286 senselqqNKDFVFFTDEPGVNKIILDLCRGNHDLFMKRRK 326
gi 198423742 293 tsnlnvnaPEDIVFLVDDPEVNKLILDLCRGNHDLFMQRRR 333
gi 167515612 288 -------aTKDFSVFFNRAKTCQRILDMCVGYHSLYVQTVH 321
gi 255760088 381 -------kVSNFIFYSQDLHINKMILDLCKGNHDLYMRRRK 414
gi 386783915 208 -------nSSNFVFFTDHSRINKTILHMSMGNHDLYLKRRK 241
gi 326429935 268 -------hAVDLVFFSTDPSVNKTILQLCIGNHELYLKRRE 301
gi 91077028  255 -------tSQDFVFFTSEPRMSKMILNLGIGNHSLYVKRRK 288

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