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Conserved domains on  [gi|1390249135|ref|NP_001350413|]
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clathrin interactor 1 isoform 3 [Mus musculus]

Protein Classification

clathrin interactor 1( domain architecture ID 13016578)

clathrin interactor 1 (Clint1) binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and may have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes

Gene Symbol:  CLINT1
Gene Ontology:  GO:0006897|GO:0005543|GO:0030276
PubMed:  12429846|10567358

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 24-149 2.37e-99

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: 297.67  E-value: 2.37e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  24 IESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSARE 103
Cdd:cd16989     1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRMLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1390249135 104 HIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREER 149
Cdd:cd16989    81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREER 126
 
Name Accession Description Interval E-value
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 24-149 2.37e-99

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: 297.67  E-value: 2.37e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  24 IESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSARE 103
Cdd:cd16989     1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRMLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1390249135 104 HIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREER 149
Cdd:cd16989    81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREER 126
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 21-145 3.10e-65

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: 209.34  E-value: 3.10e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  21 YSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRmLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTS 100
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKR-LNDKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1390249135 101 AREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRL 145
Cdd:pfam01417  80 LRENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
22-149 5.77e-50

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 168.96  E-value: 5.77e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135   22 SEIESKVREATNDDPWGPSGQLMGEIAKATFMY-EQFPELMNMLWSRMLkdNKKNWRRVYKSLLLLAYLIRNGSERVVTS 100
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLN--DTKNWRVVYKALILLHYLLRNGSPRVILE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1390249135  101 AREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREER 149
Cdd:smart00273  79 ALRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
 
Name Accession Description Interval E-value
ENTH_EpsinR cd16989
Epsin N-Terminal Homology (ENTH) domain of Epsin-related protein; Epsin-related protein ...
 24-149 2.37e-99

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: 297.67  E-value: 2.37e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  24 IESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSARE 103
Cdd:cd16989     1 IESKVREATNDDPWGPTGQLMQEIARYTFTYEQFPEVMNMLWKRMLKDNKKNWRRVYKSLLLLDYLLKNGSERVVTSARE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1390249135 104 HIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREER 149
Cdd:cd16989    81 HIYDLRSLENYHFIDEKGKDQGINVRQKVKEIIELLQDDERLREER 126
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 21-145 3.10e-65

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: 209.34  E-value: 3.10e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  21 YSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRmLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTS 100
Cdd:pfam01417   1 YSETELKVREATNNDPWGPSGTLMDEIARLTYNYVEFPEIMKMLWKR-LNDKGKNWRHIYKALTLLEYLLKNGSERVVDD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1390249135 101 AREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRL 145
Cdd:pfam01417  80 LRENIYIIRTLTDFHYIDENGKDQGINVRKKAKEILNLLEDDELL 124
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 24-141 1.57e-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: 183.49  E-value: 1.57e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  24 IESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRmLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSARE 103
Cdd:cd03571     1 LELLVREATSNEPWGPTGSQLAEIAQATFDYDDYQRIMKVLWKR-LNDKGKNWRHVYKALTLLEYLLKNGSERVVDEFRD 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1390249135 104 HIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQD 141
Cdd:cd03571    80 NLYLIRTLQDFQYVDENGDDQGINVREKAKQIVALLED 117
ENTH_Epsin cd16990
Epsin N-Terminal Homology (ENTH) domain of Epsin family; Members of the epsin family play an ...
 23-147 7.82e-55

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: 181.78  E-value: 7.82e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  23 EIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRmLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAR 102
Cdd:cd16990     1 EAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKR-LNDHGKNWRHVYKALTLLEYLIKTGSERVAQQCK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1390249135 103 EHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLRE 147
Cdd:cd16990    80 ENIFAIQTLKDFQYIDRDGKDQGVNVREKAKQLVSLLKDDERLKN 124
ENTH_Ent3 cd16992
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent3 and similar proteins; This subfamily is ...
 25-144 3.89e-53

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: 177.26  E-value: 3.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  25 ESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREH 104
Cdd:cd16992     2 ESKVREATNNDPWGASSTLMQEIAQGTYNYQQFNEIMPMIYKRFTEKAGSEWRQIYKALQLLEYLIKNGSERVVDDARGH 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1390249135 105 IYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDR 144
Cdd:cd16992    82 LTLIKMLRSFHYIDDKGKDQGINVRNRAKELIELLSDDEK 121
ENTH_Ent1_Ent2 cd16991
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent1, Ent2, and similar proteins; This ...
 21-149 6.53e-53

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: 177.08  E-value: 6.53e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  21 YSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLwSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTS 100
Cdd:cd16991     2 YSSTQVKVRNATSNDPWGPSGDEMAEIAELTYDQHDFVEIMDML-DKRLNDKGKNWRHVAKALTVLDYLLHFGSENVVLW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1390249135 101 AREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREER 149
Cdd:cd16991    81 AKENIYIIKTLREFQYIDDEGKDQGQNVRVKAKELTSLLLDDERLREER 129
ENTH smart00273
Epsin N-terminal homology (ENTH) domain;
22-149 5.77e-50

Epsin N-terminal homology (ENTH) domain;


Pssm-ID: 214594  Cd Length: 127  Bit Score: 168.96  E-value: 5.77e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135   22 SEIESKVREATNDDPWGPSGQLMGEIAKATFMY-EQFPELMNMLWSRMLkdNKKNWRRVYKSLLLLAYLIRNGSERVVTS 100
Cdd:smart00273   1 SDLEVKVRKATNNDEWGPKGKHLREIIQGTHNEkSSFAEIMAVLWRRLN--DTKNWRVVYKALILLHYLLRNGSPRVILE 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1390249135  101 AREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREER 149
Cdd:smart00273  79 ALRNRNRILNLSDFQDIDSRGKDQGANIRTYAKYLLERLEDDRRLKEER 127
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 25-137 4.28e-19

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: 83.24  E-value: 4.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  25 ESKVREATNDDPWGPSGQLMGEIAKATF-MYEQFPELMNMLWSRMlkdNKKNWRRVYKSLLLLAYLIRNGSERVVTSARE 103
Cdd:cd00197     2 EKTVEKATSNENMGPDWPLIMEICDLINeTNVGPKEAVDAIKKRI---NNKNPHVVLKALTLLEYCVKNCGERFHQEVAS 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1390249135 104 HIYDLRSLeNYHFVDEHGKDQGINIRQKVKELVE 137
Cdd:cd00197    79 NDFAVELL-KFDKSGLLGDDVSTNVREKAIELVQ 111
ENTH_Ent4 cd16994
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent4 and similar proteins; Yeast Epsin-4 ...
 25-143 1.47e-15

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: 73.48  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  25 ESKVREATNDDPW-GPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRR----VYKSLLLLAYLIRNGSERVVT 99
Cdd:cd16994     2 ELKVKQATDDNETsGATGTLMNEISVLTYSPKTLKEITQVLKKRLSGNSKKSSHKncvhILKTLTLISYLINNGSNEFIA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1390249135 100 SAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDD 143
Cdd:cd16994    82 WLRSNLYLIERLKDFEVQDNRDLPMANQIRSLSQDICELINDDE 125
ENTH_Ent5 cd16993
Epsin N-Terminal Homology (ENTH) domain of Yeast Ent5 and similar proteins; This subfamily is ...
 28-150 2.52e-06

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: 47.84  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  28 VREATNDDPWGPSGQLMGEIAKATF---MYEQFPELMNMLWSRMLKDNKK--------------NWRRVYKSLLLLAYLI 90
Cdd:cd16993     5 IRRATNTDAWGPTPKHLAKVLRNRYqvpLYLMTEYTLKRLVDHIATRPKNlyekarkdyvnygsEWRVVLKCLIVIEFLL 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1390249135  91 RNGSE-----RVVTSAREHIYDL-RSLENYHF-VDEHGKDQGIN--IRQKVKELVEFAQDDDRLREERK 150
Cdd:cd16993    85 LNVDTgdelnQVLSCLLNHKHIFtREIAQYKVkFSNDGKMEIHErgIQKKCELILQLIEDSDFLRQERA 153
ANTH_N_YAP180 cd16988
ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly ...
 47-134 6.69e-06

ANTH (AP180 N-Terminal Homology) domain, N-terminal region, of yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins; This subfamily includes yeast clathrin coat assembly protein AP180 (YAP180) and similar proteins. There are two YAP180 proteins in Saccharomyces cerevisiae, AP180A (yAP180A or YAP1801) and AP180B (yAP180B or YAP1802). They are involved in endocytosis and clathrin cage assembly. ANTH domains bind both inositol phospholipids and proteins, and contribute to the nucleation and formation of clathrin coats on membranes. 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 of plant clathrin coat assembly protein AP180 and similar proteins.


Pssm-ID: 340785  Cd Length: 117  Bit Score: 45.25  E-value: 6.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  47 IAKATFMYEQ-FPELMNMLWSRmLKDNkkNWRRVYKSLLLLAYLIRNGSERVVT---SAREHIYDLRSLENYHFvdeHGK 122
Cdd:cd16988    24 ILLATYSSDAsFGEIVRALSRR-LRDN--SWTVVFKSLIVLHLMIREGETDDVLlyyLSRPDFLDLRKIRNGSS---AGS 97

                          90
                  ....*....|....*....
gi 1390249135 123 DQGINIR-------QKVKE 134
Cdd:cd16988    98 GQLQNIQryaaylkERVKE 116
ANTH_N cd03564
ANTH (AP180 N-Terminal Homology) domain family, N-terminal region; The ANTH (AP180 N-Terminal ...
 31-115 9.44e-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: 39.18  E-value: 9.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  31 ATNDDPWGPSGQLMGEIAKATFM---YEQFPELMNMLWSRMlkdNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYD 107
Cdd:cd03564     8 ATNHDEVPPKEKHVRKLLLATSNgggRADVAYIVHALAKRL---HKKNWIVVLKTLIVIHRLLREGSPSFLEELLRYSGH 84


                  ....*...
gi 1390249135 108 LRSLENYH 115
Cdd:cd03564    85 IFNLSNFK 92
ANTH pfam07651
ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the ...
 23-137 1.91e-03

ANTH domain; AP180 is an endocytotic accessory proteins that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats.


Pssm-ID: 400137  Cd Length: 272  Bit Score: 40.36  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135  23 EIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRmLKDNKkNWRRVYKSLLLLAYLIRNGSERVVTSAR 102
Cdd:pfam07651   1 DLEVAVVKATSHDEAPPKEKHVREILVGTSSSAKLAALFWALSRR-LPLTR-SWVVAFKALILVHKLLREGHPSVLQELL 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1390249135 103 EHIYDLRSLEN-YHFvdEHGKDQGINIRQKVKELVE 137
Cdd:pfam07651  79 RARRRISSLLRiSSF--SLSWDYGAFIRAYAKYLDE 112
ENTH_like_Tepsin cd03572
Epsin N-Terminal Homology (ENTH)-like domain of AP-4 complex accessory subunit Tepsin and ...
 8-114 5.54e-03

Epsin N-Terminal Homology (ENTH)-like domain of AP-4 complex accessory subunit Tepsin and similar domains; This family is composed of proteins containing an ENTH-like domain including vertebrate AP-4 complex accessory subunit Tepsin and Arabidopsis thaliana VHS domain-containing protein At3g16270. Tepsin is also called ENTH Domain-containing protein 2 (ENTHD2), Epsin for AP-4, or Tetra-epsin. It associates with the adapter-like complex 4 (AP-4), a heterotetramer composed of two large adaptins (epsilon and beta), a medium adaptin (mu) and a small adaptin (sigma), which forms a non-clathrin coat on vesicles departing the Trans-Golgi Network. 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, 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: 340773  Cd Length: 119  Bit Score: 37.15  E-value: 5.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390249135   8 RELVDKATnvvmnyseieskvreATNDDPwgPSGQLMGEIAKATF-MYEQFPELMNMLWSRMlkdNKKNWRRVYKSLLLL 86
Cdd:cd03572     2 RPLLDKAT---------------SDDDEP--TPGYLLEEIAKLTRsSPGSCQELLDYLLKRL---KKSSPHVKLKALRII 61

                          90       100
                  ....*....|....*....|....*...
gi 1390249135  87 AYLIRNGSERVVTSAREHIYDLRSLENY 114
Cdd:cd03572    62 KHLCQKGSPEFRRELQRNSAAIRECTSY 89
 
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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