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Conserved domains on  [gi|340780479|pdb|3ONK|A]
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Chain A, Epsin-3

Protein Classification

ENTH domain-containing protein( domain architecture ID 13017050)

ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to Saccharomyces cerevisiae epsin-3 involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles

CATH:  1.25.40.90
Gene Ontology:  GO:0030276|GO:1901981|GO:0006897|GO:0005543|GO:0072659
PubMed:  27466364|14657269|12742163|22748146|11911874|29774507
SCOP:  4001355

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 12-132 4.18e-74

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-3 (Ent3 or Ent3p), and similar proteins. Ent3 is an adaptor proteins at the Trans-Golgi Network (TGN); it cooperates with yeast SNARE Vti1p to regulate transport from the TGN to the prevacuolar endosome. Ent3 facilitates the interaction between Gga2p with both the endosomal syntaxin Pep12p and clathrin in the GGA-dependent transport to the late endosome. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. 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 clathrin-coated vesicles. Similar to mammalian epsinR, The ENTH domain of Ent3 binds to the yeast SNARE Vti1p; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. 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.


:

Pssm-ID: 340789  Cd Length: 121  Bit Score: 216.94  E-value: 4.18e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A       12 MEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFTEKAGSEWRQIYKALQLLDYLIKHGSERFIDDTRN 91
Cdd:cd16992   1 MESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEKAGSEWRQIYKALQLLEYLIKNGSERVVDDARG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
3ONK_A       92 SINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNK 132
Cdd:cd16992  81 HLTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK 121
 
Name Accession Description Interval E-value
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 12-132 4.18e-74

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-3 (Ent3 or Ent3p), and similar proteins. Ent3 is an adaptor proteins at the Trans-Golgi Network (TGN); it cooperates with yeast SNARE Vti1p to regulate transport from the TGN to the prevacuolar endosome. Ent3 facilitates the interaction between Gga2p with both the endosomal syntaxin Pep12p and clathrin in the GGA-dependent transport to the late endosome. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. 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 clathrin-coated vesicles. Similar to mammalian epsinR, The ENTH domain of Ent3 binds to the yeast SNARE Vti1p; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. 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.


Pssm-ID: 340789  Cd Length: 121  Bit Score: 216.94  E-value: 4.18e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A       12 MEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFTEKAGSEWRQIYKALQLLDYLIKHGSERFIDDTRN 91
Cdd:cd16992   1 MESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEKAGSEWRQIYKALQLLEYLIKNGSERVVDDARG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
3ONK_A       92 SINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNK 132
Cdd:cd16992  81 HLTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK 121
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 9-133 2.05e-62

ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown.


Pssm-ID: 426255  Cd Length: 124  Bit Score: 187.38  E-value: 2.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A          9 YTEMEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFtEKAGSEWRQIYKALQLLDYLIKHGSERFIDD 88
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRL-NDKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
3ONK_A         89 TRNSINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNKI 133
Cdd:pfam01417  80 LRENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
10-137 4.41e-47

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 148.93  E-value: 4.41e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A          10 TEMEGKVREATNNEPWGASSTLMDQISQGTYNFRE-REEILSMIFRRFTEKAgsEWRQIYKALQLLDYLIKHGSERFIDD 88
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSsFAEIMAVLWRRLNDTK--NWRVVYKALILLHYLLRNGSPRVILE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
3ONK_A          89 TRNSINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNKIRAER 137
Cdd:smart00273  79 ALRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
 
Name Accession Description Interval E-value
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 12-132 4.18e-74

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-3 (Ent3 or Ent3p), and similar proteins. Ent3 is an adaptor proteins at the Trans-Golgi Network (TGN); it cooperates with yeast SNARE Vti1p to regulate transport from the TGN to the prevacuolar endosome. Ent3 facilitates the interaction between Gga2p with both the endosomal syntaxin Pep12p and clathrin in the GGA-dependent transport to the late endosome. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. 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 clathrin-coated vesicles. Similar to mammalian epsinR, The ENTH domain of Ent3 binds to the yeast SNARE Vti1p; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. 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.


Pssm-ID: 340789  Cd Length: 121  Bit Score: 216.94  E-value: 4.18e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A       12 MEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFTEKAGSEWRQIYKALQLLDYLIKHGSERFIDDTRN 91
Cdd:cd16992   1 MESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEKAGSEWRQIYKALQLLEYLIKNGSERVVDDARG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
3ONK_A       92 SINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNK 132
Cdd:cd16992  81 HLTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK 121
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 9-133 2.05e-62

ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in endocytosis and cytoskeletal machinery. The function of the ENTH domain is unknown.


Pssm-ID: 426255  Cd Length: 124  Bit Score: 187.38  E-value: 2.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A          9 YTEMEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFtEKAGSEWRQIYKALQLLDYLIKHGSERFIDD 88
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRL-NDKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
3ONK_A         89 TRNSINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNKI 133
Cdd:pfam01417  80 LRENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 12-141 4.08e-57

Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein (EpsinR) is also called clathrin interactor 1 (Clint), enthoprotin, or epsin-4. It is a clathrin-coated vesicle (CCV) protein that binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). It contains 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 clathrin-coated vesicles. The ENTH domain of human epsinR binds directly to the helical bundle domain of the mouse SNARE Vti1b; soluble NSF attachment protein receptors (SNAREs) are type II transmembrane proteins that have critical roles in providing the specificity and energy for transport-vesicle fusion. Specific ENTH domains may also function as protein cargo selection/recognition modules. 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.


Pssm-ID: 340786  Cd Length: 130  Bit Score: 174.40  E-value: 4.08e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A       12 MEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFTEKAGSEWRQIYKALQLLDYLIKHGSERFIDDTRN 91
Cdd:cd16989   1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRMLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
3ONK_A       92 SINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNKIRAERKKAR 141
Cdd:cd16989  81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREERKKAK 130
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 12-129 8.40e-55

Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. 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, contributing 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. 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.


Pssm-ID: 340772  Cd Length: 117  Bit Score: 168.08  E-value: 8.40e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A       12 MEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFTEKaGSEWRQIYKALQLLDYLIKHGSERFIDDTRN 91
Cdd:cd03571   1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDK-GKNWRHVYKALTLLEYLLKNGSERVVDEFRD 79

                        90       100       110
                ....*....|....*....|....*....|....*...
3ONK_A       92 SINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSD 129
Cdd:cd03571  80 NLYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
10-137 4.41e-47

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 148.93  E-value: 4.41e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A          10 TEMEGKVREATNNEPWGASSTLMDQISQGTYNFRE-REEILSMIFRRFTEKAgsEWRQIYKALQLLDYLIKHGSERFIDD 88
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEKSsFAEIMAVLWRRLNDTK--NWRVVYKALILLHYLLRNGSPRVILE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
3ONK_A          89 TRNSINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNKIRAER 137
Cdd:smart00273  79 ALRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 11-134 9.94e-45

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.


Pssm-ID: 340787  Cd Length: 124  Bit Score: 142.88  E-value: 9.94e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A       11 EMEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFTEKaGSEWRQIYKALQLLDYLIKHGSERFIDDTR 90
Cdd:cd16990   1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDH-GKNWRHVYKALTLLEYLIKTGSERVAQQCK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3ONK_A       91 NSINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNKIR 134
Cdd:cd16990  80 ENIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLK 123
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 9-138 3.53e-43

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This subfamily is composed of the two orthologs of epsin in Saccharomyces cerevisiae, Epsin-1 (Ent1 or Ent1p) and Epsin-2 (Ent2 or Ent2p), and similar proteins. Yeast single epsin knockouts, either Ent1 and Ent2, are viable while the double knockout is not. Yeast epsins are required for endocytosis and localization of actin. Ent2 also plays a signaling role during cell division. The ENTH domain of Ent2 interacts with the septin organizing, Cdc42 GTPase activating protein, Bem3, leading to increased cytokinesis failure when overexpressed. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. 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 clathrin-coated vesicles. 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.


Pssm-ID: 340788  Cd Length: 132  Bit Score: 138.95  E-value: 3.53e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A        9 YTEMEGKVREATNNEPWGASSTLMDQISQGTYNFREREEILSMIFRRFTEKaGSEWRQIYKALQLLDYLIKHGSERFIDD 88
Cdd:cd16991   2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLNDK-GKNWRHVAKALTVLDYLLHFGSENVVLW 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
3ONK_A       89 TRNSINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDNKIRAERK 138
Cdd:cd16991  81 AKENIYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREERS 130
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 13-129 2.22e-17

VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a VHS, CID, ENTH, or ANTH domain. The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It is located at the N-termini of proteins involved in intracellular membrane trafficking. The CTD-Interacting Domain (CID) is present in several RNA-processing factors and binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase II (RNAP II or Pol II). The epsin 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. VHS, ENTH, and ANTH domains are structurally similar and are composed of a superhelix of eight alpha helices. ENTH and ANTH (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 domain-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.


Pssm-ID: 340764  Cd Length: 115  Bit Score: 72.84  E-value: 2.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A       13 EGKVREATNNEPWGASSTLMDQISQGTYNFRER-EEILSMIFRRFTekaGSEWRQIYKALQLLDYLIKHGSERFIDDTRN 91
Cdd:cd00197   2 EKTVEKATSNENMGPDWPLIMEICDLINETNVGpKEAVDAIKKRIN---NKNPHVVLKALTLLEYCVKNCGERFHQEVAS 78

                        90       100       110
                ....*....|....*....|....*....|....*...
3ONK_A       92 SINLIRILEtFHYIDSQGRDQGINVRTRVKALIELLSD 129
Cdd:cd00197  79 NDFAVELLK-FDKSGLLGDDVSTNVREKAIELVQLWAS 115
ENTH_Ent4 cd16994
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 ...
 13-131 3.71e-17

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 (Ent4 or Ent4p) has been reported to be involved in the Trans-Golgi Network (TGN)-to-vacuole sorting of Arn1p, a transporter for the uptake of ferrichrome, an important nutritional source of iron. Yeast epsins contain an Epsin N-Terminal Homology (ENTH) domain, an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. 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 clathrin-coated vesicles. 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.


Pssm-ID: 340791  Cd Length: 126  Bit Score: 72.33  E-value: 3.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A       13 EGKVREATN-NEPWGASSTLMDQISQGTYNFREREEILSMIFRRFTEKAGS----EWRQIYKALQLLDYLIKHGSERFID 87
Cdd:cd16994   2 ELKVKQATDdNETSGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSKKsshkNCVHILKTLTLISYLINNGSNEFIA 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
3ONK_A       88 DTRNSINLIRILETFHYIDSQGRDQGINVRTRVKALIELLSDDN 131
Cdd:cd16994  82 WLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDE 125
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 19-103 6.31e-04

ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal Homology) domain family is composed of Adaptor Protein 180 (AP180), Clathrin Assembly Lymphoid Myeloid Leukemia protein (CALM), and similar proteins. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. ANTH-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that the ANTH domain is a universal component of the machinery for clathrin-mediated membrane budding. The ANTH domain is a unique module whose N-terminal half is structurally similar to the Epsin N-Terminal Homology (ENTH) and Vps27/Hrs/STAM (VHS) domains, containing a superhelix of eight alpha helices. In addition, it contains a coiled-coil C-terminal half with strutural similarity to spectrin repeats. It binds phosphoinositide PtdIns(4,5)P2 at a short conserved motif K[X]9[K/R][H/Y] between helices 1 and 2. This model describes the N-terminal region of ANTH domains.


Pssm-ID: 340767  Cd Length: 120  Bit Score: 37.25  E-value: 6.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A       19 ATNNEPWGASSTLMDQISQGTYNFRER---EEILSMIFRRFTekaGSEWRQIYKALQLLDYLIKHGSERFIDDTRNSINL 95
Cdd:cd03564   8 ATNHDEVPPKEKHVRKLLLATSNGGGRadvAYIVHALAKRLH---KKNWIVVLKTLIVIHRLLREGSPSFLEELLRYSGH 84


                ....*...
3ONK_A       96 IRILETFH 103
Cdd:cd03564  85 IFNLSNFK 92
VHS cd03561
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ...
 12-125 6.16e-03

VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It has a superhelical structure similar to that of the ARM (Armadillo) repeats and is present at the N-termini of proteins involved in intracellular membrane trafficking. There are four general groups of VHS domain containing proteins based on their association with other domains. The first group consists of proteins of the STAM/EAST/Hbp family, which has the domain composition of VHS-SH3-ITAM. The second consists of proteins with a FYVE domain C-terminal to VHS. The third consists of GGA proteins with a domain composition of VHS-GAT (GGA and TOM)-GAE (Gamma-Adaptin Ear) domain. The fourth consists of proteins with a VHS domain alone or with domains other than those mentioned above. In GGA proteins, VHS domains are involved in cargo recognition in trans-Golgi, thereby having a general membrane targeting/cargo recognition role in vesicular trafficking.


Pssm-ID: 340765  Cd Length: 131  Bit Score: 34.93  E-value: 6.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3ONK_A       12 MEGKVREATN----NEPWGASSTLMDQISQGTYNfreREEILSMIFRRFTEKAGsewRQIYKALQLLDYLIK------H- 80
Cdd:cd03561   1 VEELVEKATSesltEPDWALNLEICDLVNSDPAQ---AKDAVRALRKRLQSKNP---KVQLLALTLLETLVKncgapfHs 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
3ONK_A       81 --GSERFIDDtrnsinLIRILEtfhyidsqGRDQGINVRTRVKALIE 125
Cdd:cd03561  75 evASRDFLQE------LVKLVK--------KKKTSPEVREKALALIQ 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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