Conserved Protein Domain Family
EFh_UTRO

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cd16247: EFh_UTRO 
EF-hand-like motif found in utrophin
Utrophin, also termed dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homologue that increases dystrophic muscle function and reduces pathology. It is broadly expressed at both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with the dystroglycans (DGs) and the sarcoglycan-dystroglycans, sarcoglycans and sarcospan (SG-SSPN) subcomplex. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, Utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs) and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs.
Statistics
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PSSM-Id: 320005
View PSSM: cd16247
Aligned: 5 rows
Threshold Bit Score: 332.246
Threshold Setting Gi: 632953847
Created: 12-Nov-2014
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Feature 1:EF-hand-like motif [structural motif]
Evidence:
  • Comment:The EF-like motifs don't contain the canonical pattern of calcium binding residues.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1         ########################################                                        
gi 215274104 2882 ELSTTNEIFKQHKLNQNDQLLSVPDVINCLTTTYDGLEQMhkdlvnVPLCVDMCLNWLLNVYDTGRTGKIRVQSLKIGLM 2961
gi 82261301  2604 DLNVAQNTFKQHKLTNNSQLLSVPDIINCLTSIYDGLEQEhkdlvnVPLCVDMCLNWLLNVYDTGRSGKIRVLSMKIGLL 2683
gi 82070270    40 DLTTTHSVFKQHELNQNNQLLSVPEVINVLTTIYDGLEQKhkelvnVPLCVEMCLNWLLNVYDTGRTGKLRVLSLKIGLM 119
gi 632953847 3099 DLNTAHSIFEQHKLTQNEQLLNVTEVINCLTTIYDGLEQShkdlvnVPLCVDMCLNWLLNVFDTGRSGKIRVLSLKIGLM 3178
gi 678132243    7 DLNTTSEVFKQHKLSQNDQLIGVQDVISCLTTIYSGLEEKhkdmvnVPLCVDMCLNWLLNVYDSGRTGKIRVQSLKIGLM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                         
gi 215274104 2962 SlskglLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQlgevaafggsniEPSVRSCFQQNNNKPEISVKEFIDW 3041
gi 82261301  2684 SlckghLEEKYKYLFSQVASAGDTCDQRQLGLLLHEAIQIPRQlgevaafggsniEPSVRSCFQHVNNKVELEPRQFVDW 2763
gi 82070270   120 ClskglLEEKYRHLFKEVCGAGDTCDQRQLSLMLHDAIQIPRQlgevaafggsniEPSVRSCFQHAQNKPEIDVNHFIEW 199
gi 632953847 3179 SlskglLEEKYKNLFKQVAGPNAQCDQRGLSHLLHDAIQIPRQlgevasfggsniEPSVRSCFQHAQNKTEIDVKLFVEW 3258
gi 678132243   87 SlskglLEEKYRYLFKEVAGPTEMCDQRQLGLLLHDAIQIPRQlgevaafggsniEPSVRSCFQQNHNKPEITVKQFIDW 166

                  ..
Feature 1           
gi 215274104 3042 MH 3043
gi 82261301  2764 MR 2765
gi 82070270   200 MR 201
gi 632953847 3259 MR 3260
gi 678132243  167 MR 168

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