1H0A,1INZ,1XGW


Conserved Protein Domain Family
ENTH_epsin

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cd03571: ENTH_epsin (this model, PSSM-Id:239627 is obsolete and has been replaced by 340772)
Click on image for an interactive view with Cn3D
ENTH domain, Epsin family; The epsin (Eps15 interactor) N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. A set of proteins previously designated as harboring an ENTH domain in fact contains a highly similar, yet unique module referred to as an AP180 N-terminal homology (ANTH) domain. ENTH and ANTH (E/ANTH) domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. E/ANTH domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the trans-Golgi network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding.
Statistics
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PSSM-Id: 239627
Aligned: 53 rows
Threshold Bit Score: 124.587
Created: 2-Mar-2006
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
Ins(1,4,5)p3PLZF binding
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:Ins(1,4,5)p3 binding site
Evidence:
  • Structure:1H0A; Rattus norvegicus Epsin ENTH binds Ins(1,4,5)p3; contacts at 3.5A
    View structure with Cn3D
  • Comment:Ins(1,4,5)p3 = Inositol 1,4,5-Trisphosphate

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1           #   ##                                 #           #   #                  
1H0A_A     19 EAEIKVREATSNDp-WGPSSSLMSEIADLTYnvvAFSEIMSMIWKRLNDh------gKNWRHVYKAMTLMEYLIKTGSER 91  Norway rat
NP_190238  45 PLQLMTEEATDGEs-CGPNTQTLGSISKAAFefeDYLAIVEVLHKRLAKfd-----kRNWRMAYNSLIVVEHLLTHGPES 118 thale cress
NP_172343  37 AEELLTEEVTGSDh-SSIDSRSMAAITRVSFevdQFQRIVKILRQRMVVfd-----rKEWRGMCNTLSMLNHLLLNGPLS 110 thale cress
AAU44477   34 EAELLVEEVTNGDp-SSPDAKTMTKIAEASFdtvEYWRIVDVLHRKIGKder---eiKNWREAYKAMVLLEFLLMHGPIH 109 thale cress
BAD81760   36 PTQLMTEEATSGDa-SPPNVKTMSLIARQAFeidEYVRISDILHKRFARfd-----rRQWREAYKALLLLEHLLTHGPRS 109 Japanese rice
CAJ04864   22 EYVQIVHDATNDEk-WGPTGPQMDAVCNAYPr--GGPEILNELRTRLNNr------dKSWRPCYKSLLVIDYLARNVDDR 92  Leishmania major
XP_828159  22 EYARLVHEATNEDp-WGPTGEQMDNVCRVFQa--GTVKIMEEIKLRLKNr------dKSWRPCYKALLLLDHLARNVPEV 92  Trypanosoma brucei...
AAS51167   14 PTAAKVRKATDDNefVGASSALISEITILTYsckTLLDVTRVLKKRLSGnank-sshKNAVHILKALTLTNYLIANGSED 92  Ashbya gossypii AT...
NP_013062  14 PTESKVKQATNEDetSGATGTLMNEISILTYspkTVREIIQVIRKRLLLgqnrrnshRNCIQVMKTLTLVSYLMNNGSNE 93  baker's yeast
XP_445852  14 PTELKVRQATDDNelAGATGTLMNEISVLTYskkTLKDVIQVIRKRLSGvnkr-nshRTCLHVLKTLTLVSYLLNNGSND 92  Candida glabrata C...
Feature 1                                                        
1H0A_A     92 VSQQCKENMYAVQtl-kDFQYVDRDGkdQGVNVREKAKQLVALLRDEDRLR 141 Norway rat
NP_190238 119 VSDEFQGDIDVISqm-qTFQQIDEKGfnWGLAVRKKAEKVLKLLEKGELLK 168 thale cress
NP_172343 111 VFSEFQHERAIIEda-iKMEWIDERGfdCGLKVRNIAEKVLRLLEDDMFLK 160 thale cress
AAU44477  110 LPHDFLYDLDHFRfl-sTFQYVDNNGfdWGAQVQKKADQIQTLLLGKEELR 159 thale cress
BAD81760  110 VALEFQRDREVIEqm-vSFQHIDEKGfnWGMTVKSKSERVLRLLERGPFLE 159 Japanese rice
CAJ04864   93 YLPEISALVPIIRtistSFYYTNPKGvdHGVSVRERAKKVADLLSDGLQLR 143 Leishmania major
XP_828159  93 GLPPLCSILPTLQhisqTFYYTGKQGadHGLSVRERAKKLFDLLSDPATLR 143 Trypanosoma brucei TREU927
AAS51167   93 FVQWLQGCAVLLRrl-kDFTTGNERDshMASQIRSFSLSLLELMQNPALLE 142 Ashbya gossypii ATCC 10895
NP_013062  94 FIKWLKGNMILIEil-eDFQVQDPRDerKAEDIQKLSRNVLGLLQDDGLLE 143 baker's yeast
XP_445852  93 FIAWLKSSKYVIEyl-sSFEAQSSSDepMVNQIRFLCNDIITLLEDEELLE 142 Candida glabrata CBS 138

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