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Conserved domains on  [gi|22329424|ref|NP_172343|]
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ENTH/VHS family protein [Arabidopsis thaliana]

Protein Classification

ENTH domain-containing protein( domain architecture ID 10477394)

ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to epsin family protein that may participate in clathrin-mediated endocytosis

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 35-159 6.12e-36

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: 123.44  E-value: 6.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329424    35 VTAEELLTEEVTGSDHSSIDSRSMAAITRVSFEVDQFQRIVKILRQRMVvFDRKEWRGMCNTLSMLNHLLLNGPLSVFSE 114
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLN-DKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 22329424   115 FQHERAIIEDAIKMEWIDERGFDCGLKVRNIAEKVLRLLEDDMFL 159
Cdd:pfam01417  80 LRENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
 
Name Accession Description Interval E-value
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 35-159 6.12e-36

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: 123.44  E-value: 6.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329424    35 VTAEELLTEEVTGSDHSSIDSRSMAAITRVSFEVDQFQRIVKILRQRMVvFDRKEWRGMCNTLSMLNHLLLNGPLSVFSE 114
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLN-DKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 22329424   115 FQHERAIIEDAIKMEWIDERGFDCGLKVRNIAEKVLRLLEDDMFL 159
Cdd:pfam01417  80 LRENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 39-155 2.85e-35

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: 121.47  E-value: 2.85e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329424  39 ELLTEEVTGSDHSSIDSRSMAAITRVSFEVDQFQRIVKILRQRMVVFDrKEWRGMCNTLSMLNHLLLNGPLSVFSEFQHE 118
Cdd:cd03571   2 ELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKG-KNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 22329424 119 RAIIEDAIKMEWIDERGFDCGLKVRNIAEKVLRLLED 155
Cdd:cd03571  81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
70-163 6.64e-28

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 102.71  E-value: 6.64e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329424     70 QFQRIVKILRQRMvvFDRKEWRGMCNTLSMLNHLLLNGPLSVFSEFQHERAIIEDAIKMEWIDERGFDCGLKVRNIAEKV 149
Cdd:smart00273  36 SFAEIMAVLWRRL--NDTKNWRVVYKALILLHYLLRNGSPRVILEALRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYL 113

                           90
                   ....*....|....
gi 22329424    150 LRLLEDDMFLKDER 163
Cdd:smart00273 114 LERLEDDRRLKEER 127
 
Name Accession Description Interval E-value
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 35-159 6.12e-36

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: 123.44  E-value: 6.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329424    35 VTAEELLTEEVTGSDHSSIDSRSMAAITRVSFEVDQFQRIVKILRQRMVvFDRKEWRGMCNTLSMLNHLLLNGPLSVFSE 114
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKRLN-DKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 22329424   115 FQHERAIIEDAIKMEWIDERGFDCGLKVRNIAEKVLRLLEDDMFL 159
Cdd:pfam01417  80 LRENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 39-155 2.85e-35

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: 121.47  E-value: 2.85e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329424  39 ELLTEEVTGSDHSSIDSRSMAAITRVSFEVDQFQRIVKILRQRMVVFDrKEWRGMCNTLSMLNHLLLNGPLSVFSEFQHE 118
Cdd:cd03571   2 ELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKRLNDKG-KNWRHVYKALTLLEYLLKNGSERVVDEFRDN 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 22329424 119 RAIIEDAIKMEWIDERGFDCGLKVRNIAEKVLRLLED 155
Cdd:cd03571  81 LYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
70-163 6.64e-28

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 102.71  E-value: 6.64e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329424     70 QFQRIVKILRQRMvvFDRKEWRGMCNTLSMLNHLLLNGPLSVFSEFQHERAIIEDAIKMEWIDERGFDCGLKVRNIAEKV 149
Cdd:smart00273  36 SFAEIMAVLWRRL--NDTKNWRVVYKALILLHYLLRNGSPRVILEALRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYL 113

                           90
                   ....*....|....
gi 22329424    150 LRLLEDDMFLKDER 163
Cdd:smart00273 114 LERLEDDRRLKEER 127
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 39-166 2.54e-12

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: 61.91  E-value: 2.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329424  39 ELLTEEVTGSDHSSIDSRSMAAITRVSFEVDQFQRIVKILRQRMVvfDR-KEWRGMCNTLSMLNHLLLNGPLSVFSEFQH 117
Cdd:cd16991   6 QVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDMLDKRLN--DKgKNWRHVAKALTVLDYLLHFGSENVVLWAKE 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 22329424 118 ERAIIEDAIKMEWIDERGFDCGLKVRNIAEKVLRLLEDDMFLKDERERN 166
Cdd:cd16991  84 NIYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREERSMR 132
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 58-167 5.86e-11

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: 58.07  E-value: 5.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329424  58 MAAITRVSFEVDQFQRIVKILRQRMVVFDRKEWRGMCNTLSMLNHLLLNGPLSVFSEfqhERAIIEDAIKME---WIDER 134
Cdd:cd16989  21 MQEIARYTFTYEQFPEVMNMLWKRMLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTS---AREHIYDLRSLEnyhFIDEK 97

                        90       100       110
                ....*....|....*....|....*....|...
gi 22329424 135 GFDCGLKVRNIAEKVLRLLEDDMFLKDERERNR 167
Cdd:cd16989  98 GKDQGINVRQKVKEIIELLQDDERLREERKKAK 130
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 44-156 1.59e-10

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: 56.69  E-value: 1.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329424  44 EVTGSDHSSIDSRSMAAITRVSFEVDQFQRIVKILRQRMVVFDRKEWRGMCNTLSMLNHLLLNGPLSVFSEFQHERAIIE 123
Cdd:cd16992   7 EATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEKAGSEWRQIYKALQLLEYLIKNGSERVVDDARGHLTLIK 86

                        90       100       110
                ....*....|....*....|....*....|...
gi 22329424 124 DAIKMEWIDERGFDCGLKVRNIAEKVLRLLEDD 156
Cdd:cd16992  87 MLRSFHYIDDKGKDQGINVRNRAKELIELLSDD 119
 
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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