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Conserved domains on  [gi|398365867|ref|NP_010437|]
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Ent5p [Saccharomyces cerevisiae S288C]

Protein Classification

ENTH domain-containing protein( domain architecture ID 13017129)

ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to Saccharomyces cerevisiae epsin-5 involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles

Gene Ontology:  GO:0030276|GO:0080025|GO:0006897
PubMed:  14657269

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 33-190 3.84e-102

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-5 (Ent5 or Ent5p), and similar proteins. Ent5 is required, together with Ent3 and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. It is also required for protein transport from the Trans-Golgi Network (TGN) to the vacuole. 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: 340790  Cd Length: 158  Bit Score: 299.76  E-value: 3.84e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867  33 YQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEWRVVLKCLVVI 112
Cdd:cd16993    1 YQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEWRVVLKCLIVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365867 113 EFLLLNVDTGDELNQIRSCLLTHKHILTREIAQFKVKFSNDGKMEIHERGIRKKGELILQYLEDSQFLKKERAKNKKN 190
Cdd:cd16993   81 EFLLLNVDTGDELNQVLSCLLNHKHIFTREIAQYKVKFSNDGKMEIHERGIQKKCELILQLIEDSDFLRQERAKNKKN 158
 
Name Accession Description Interval E-value
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 33-190 3.84e-102

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-5 (Ent5 or Ent5p), and similar proteins. Ent5 is required, together with Ent3 and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. It is also required for protein transport from the Trans-Golgi Network (TGN) to the vacuole. 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: 340790  Cd Length: 158  Bit Score: 299.76  E-value: 3.84e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867  33 YQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEWRVVLKCLVVI 112
Cdd:cd16993    1 YQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEWRVVLKCLIVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365867 113 EFLLLNVDTGDELNQIRSCLLTHKHILTREIAQFKVKFSNDGKMEIHERGIRKKGELILQYLEDSQFLKKERAKNKKN 190
Cdd:cd16993   81 EFLLLNVDTGDELNQVLSCLLNHKHIFTREIAQYKVKFSNDGKMEIHERGIQKKCELILQLIEDSDFLRQERAKNKKN 158
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 30-180 1.07e-27

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: 106.10  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867   30 YEPYQIDIRRATNTDAWGPTPKHLAKVLRNRYQ-VPLYLMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKC 108
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNyVEFPEIMKMLWKRLNDK-------------------GKNWRHIYKA 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365867  109 LVVIEFLLLNvdtGDElnQIRSCLLTHKHILTReIAQFKVkFSNDGKMEIHErgIRKKGELILQYLEDSQFL 180
Cdd:pfam01417  62 LTLLEYLLKN---GSE--RVVDDLRENIYIIRT-LTDFHY-IDENGKDQGIN--VRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
32-184 1.30e-27

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 105.79  E-value: 1.30e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867    32 PYQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPlylmteYTLKRLVDHIATRPKNLYekarkdyvnygsEWRVVLKCLVV 111
Cdd:smart00273   2 DLEVKVRKATNNDEWGPKGKHLREIIQGTHNEK------SSFAEIMAVLWRRLNDTK------------NWRVVYKALIL 63

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365867   112 IEFLLLNvdtGDElNQIRSCLLTHKHILTREIAQFKvkfsnDGKMEIHERGIRKKGELILQYLEDSQFLKKER 184
Cdd:smart00273  64 LHYLLRN---GSP-RVILEALRNRNRILNLSDFQDI-----DSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
 
Name Accession Description Interval E-value
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 33-190 3.84e-102

Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is composed of one of two epsinR orthologs present in Saccharomyces cerevisiae, Epsin-5 (Ent5 or Ent5p), and similar proteins. Ent5 is required, together with Ent3 and Vps27p for ubiquitin-dependent protein sorting into the multivesicular body. It is also required for protein transport from the Trans-Golgi Network (TGN) to the vacuole. 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: 340790  Cd Length: 158  Bit Score: 299.76  E-value: 3.84e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867  33 YQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEWRVVLKCLVVI 112
Cdd:cd16993    1 YQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEWRVVLKCLIVI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398365867 113 EFLLLNVDTGDELNQIRSCLLTHKHILTREIAQFKVKFSNDGKMEIHERGIRKKGELILQYLEDSQFLKKERAKNKKN 190
Cdd:cd16993   81 EFLLLNVDTGDELNQVLSCLLNHKHIFTREIAQYKVKFSNDGKMEIHERGIQKKCELILQLIEDSDFLRQERAKNKKN 158
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 30-180 1.07e-27

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: 106.10  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867   30 YEPYQIDIRRATNTDAWGPTPKHLAKVLRNRYQ-VPLYLMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKC 108
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNyVEFPEIMKMLWKRLNDK-------------------GKNWRHIYKA 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398365867  109 LVVIEFLLLNvdtGDElnQIRSCLLTHKHILTReIAQFKVkFSNDGKMEIHErgIRKKGELILQYLEDSQFL 180
Cdd:pfam01417  62 LTLLEYLLKN---GSE--RVVDDLRENIYIIRT-LTDFHY-IDENGKDQGIN--VRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
32-184 1.30e-27

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 105.79  E-value: 1.30e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867    32 PYQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPlylmteYTLKRLVDHIATRPKNLYekarkdyvnygsEWRVVLKCLVV 111
Cdd:smart00273   2 DLEVKVRKATNNDEWGPKGKHLREIIQGTHNEK------SSFAEIMAVLWRRLNDTK------------NWRVVYKALIL 63

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398365867   112 IEFLLLNvdtGDElNQIRSCLLTHKHILTREIAQFKvkfsnDGKMEIHERGIRKKGELILQYLEDSQFLKKER 184
Cdd:smart00273  64 LHYLLRN---GSP-RVILEALRNRNRILNLSDFQDI-----DSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 33-176 4.77e-21

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: 87.57  E-value: 4.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867  33 YQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLY-LMTEYTLKRLVDHiatrpknlyekarkdyvnyGSEWRVVLKCLVV 111
Cdd:cd03571    1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYqRIMKVLWKRLNDK-------------------GKNWRHVYKALTL 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398365867 112 IEFLLLNvdtGDElnQIRSCLLTHKHILtREIAQFKVKfsnDGKMEIHERGIRKKGELILQYLED 176
Cdd:cd03571   62 LEYLLKN---GSE--RVVDEFRDNLYLI-RTLQDFQYV---DENGDDQGINVREKAKQIVALLED 117
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 30-118 2.01e-05

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: 43.80  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867  30 YEPYQIDIRRATNTDAWGPTPKHLAKVLRNRY-QVPLYLMTEYTLKRLVDHiatrPKNlyekarkdyvnygseWRVVLKC 108
Cdd:cd16991    2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYdQHDFVEIMDMLDKRLNDK----GKN---------------WRHVAKA 62

                         90
                 ....*....|
gi 398365867 109 LVVIEFLLLN 118
Cdd:cd16991   63 LTVLDYLLHF 72
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 34-188 2.53e-05

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: 43.43  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867  34 QIDIRRATNTDAWGPTPKHLAKVLRnryqvplylMTeYTLKRLVDHIATRPKNLYEKARKDyvnygseWRVVLKCLVVIE 113
Cdd:cd16989    2 ESKVREATNDDPWGPTGQLMQEIAR---------YT-FTYEQFPEVMNMLWKRMLKDNKKN-------WRRVYKSLLLLD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365867 114 FLLLN------VDTGDELNQIRScLLTHKHIltreiaqfkvkfsnDGKMEIHERGIRKKGELILQYLEDSQFLKKERAKN 187
Cdd:cd16989   65 YLLKNgservvTSAREHIYDLRS-LENYHFI--------------DEKGKDQGINVRQKVKEIIELLQDDERLREERKKA 129


                 .
gi 398365867 188 K 188
Cdd:cd16989  130 K 130
 
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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