1H0A,5LP0,1EDU,1INZ


Conserved Protein Domain Family
ENTH_Epsin

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cd16990: ENTH_Epsin 
Click on image for an interactive view with Cn3D
Epsin N-Terminal Homology (ENTH) domain of Epsin family
Members of the epsin family play an important role as accessory proteins in clathrin-mediated endocytosis. They are important factors in clathrin-coated vesicle (CCV) generation. They contribute to membrane deformation and play a key function as adaptor proteins, coupling various components of clathrin-mediated uptake. They also have an important role in selecting and recognizing cargo. Three isoforms have been identified in mammals, epsin-1 to -3, and these are conserved in vertebrates. Epsin-1 is highly enriched and represents the dominant isoform in the brain. It is required for proper synaptic vesicle retrieval and modulates the endocytic capacity of synaptic vesicles. Epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. The ENTH domain is highly similar to the N-terminal region of the AP180 N-Terminal Homology (ANTH_N) domain. ENTH and ANTH_N domains are structurally similar to the VHS domain and are composed of a superhelix of eight alpha helices. ENTH domains bind both, inositol phospholipids with preference for PtdIns(4,5)P2, 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 CCVs. ENTH and ANTH (E/ANTH)-containing 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: 340787
Aligned: 37 rows
Threshold Bit Score: 229.164
Created: 28-May-2015
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
phosphoinosit..
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:phosphoinositide binding site [chemical binding site]
Evidence:
  • Structure:1H0A; Rattus norvegicus Epsin ENTH binds Ins(1,4,5)p3; contacts at 4.0A
  • Comment:based on the binding of Rattus norvegicus Epsin ENTH domain to inositol 1,4,5-trisphosphate
  • Comment:ENTH domains bind phosphoinositides (PtdInsPs), usually with a preference for PdtIns(4,5)P2, although not all ENTH domains show this preference.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1              #   ##                                #     #   #                         
1H0A_A        19 EAEIKVREATSNDpWGPSSSLMSEIADLTYNvVAFSEIMSMIWKRLNDHgKNWRHVYKAMTLMEYLIKTGSERVSQQCKE 98  Norway rat
T24447       150 DAQVKVREATSNDpWGPSTALMSEIADLTHNpMAFTEIMSIVWKRLNDSgKNWRHVYKSLVLLDFLIKCGHEKVAQQCRE 229 nematode
AAH75256      19 EAEVKVREATSNDpWGPSTSLMSEISLMTHHaEAFPEVMIMIWKRLNDSgKNWRHVYKALTLLDYLIKNGSKKVVEECNE 98  western clawed ...
CBY11445      19 EVEIKVREATSNDpWGPSSSIMAEIADLTYNmTAFPEIMGIIWKRVSDTgKNWRHVYKSLVLLDYLVKTGAERVQNQCKE 98  Oikopleura dioica
KJE94598      20 PIEIKVRTATSNDpWGAPNALLSEIADATYNfEQFPQIMNMVWKRMNDDgKNWRHIYKSMLLLEYLIKNGSERVAASAKD 99  Capsaspora owcz...
Q8IYW4        16 DAEIKVREATSNDpWGPSSSLMLDISDLTFNtISLSEIMNMLWHRLNDHgKNWRHVYKSLTLMDYLIKNGSKKVIQHCRE 95  human
EFO88299      19 AHQIKTREATSNDsWGPSKSIMCELAELTHSpMAFTRIMPIIWKRMNESgKKWRHVYKSLVLLEYLVKAGHDMVVEECTE 98  Caenorhabditis ...
CCD81309      16 DAERKVREATSNDpWGPSSTLMAEIADKTHNvMAFTEIMQMIWRRLNDKsKNWRHVYKALVLLEYLSKTGSDKVATQCRE 95  Schistosoma man...
NP_001122248  19 EAEVKVREATSNDpWGPSSSQMSDISDLTYNvVACNEILAMLWKRLNDD-KNWRHVYKALTLLEYLLKTGSDRVPQQSVE 97  zebrafish
EMP41838      16 DSEVKVREATSNDpWGPSSSLMLEISDLTYNtVSLLEIMNMIWHRMNDQgKNWRHVYKSLMLLDYLIKNGSKKVIQHCRE 95  green sea turtle
Feature 1                                                     
1H0A_A        99 NMYAVQTlKDFQYVDRDGk-DQGVNVREKAKQLVALLRDEDRLRE 142 Norway rat
T24447       230 NVFTIETlKDFQHVEDNR--DQGLNIREKAKQITSLLSDDERLKN 272 nematode
AAH75256      99 NIHSVQTlKDFQFLDRDGk-DQGINVREKAKQIVSLLKDEERLKQ 142 western clawed frog
CBY11445      99 NIYSIQTlKDFQYVDNRDykDHGKNVRERATQLVSLLKDEERLRN 143 Oikopleura dioica
KJE94598     100 QLITITTlKDFQYIDKENk-DQGVNIRERAKQLASLLNDPERLKE 143 Capsaspora owczarzaki ATCC 30864
Q8IYW4        96 GFCNLQTlKDFQHIDEAGk-DQGYYIREKSKQVITLLMDEPLLCK 139 human
EFO88299      99 NLYLIDTlKDFQYIEKYQ--DVGMNVRETAKKICSLLSDDELLKK 141 Caenorhabditis remanei
CCD81309      96 NIHSIETlRDFECVEDGK--DRGKNVREKARHLSTLLRDEERLHE 138 Schistosoma mansoni
NP_001122248  98 NIHIIKAlSEYRFTDKDGk-DQGVNVREKAKIVMVLIEDEEKRKE 141 zebrafish
EMP41838      96 GLFNIQTlKDFHYIDEAGk-DQGYHIREKSKQVSALLTDDQLLHN 139 green sea turtle

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