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Conserved domains on  [gi|18401075|ref|NP_566540|]
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ENTH/VHS family protein [Arabidopsis thaliana]

Protein Classification

ENTH domain-containing protein( domain architecture ID 10132404)

ENTH (Epsin N-Terminal Homology) domain-containing protein may be involved in clathrin-mediated endocytosis; similar to Homo sapiens AP-4 complex accessory subunit Tepsin that associates with the adapter-like complex 4 (AP-4) and may therefore play a role in vesicular trafficking of proteins at the trans-Golgi network

CATH:  1.25.40.90
Gene Ontology:  GO:0030276|GO:1901981|GO:0006897|GO:0072659|GO:0005543
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_like_Tepsin cd03572
Epsin N-Terminal Homology (ENTH)-like domain of AP-4 complex accessory subunit Tepsin and ...
 13-132 6.45e-47

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: 161.57  E-value: 6.45e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401075  13 RSRMIDAVTSDEDKVAPVYKLEEICDLLRSSHvSIVKEFSEFILKRLDNKSPIVKQKALRLIKYAVGKSGSEFRREMQRN 92
Cdd:cd03572   1 DRPLLDKATSDDDEPTPGYLLEEIAKLTRSSP-GSCQELLDYLLKRLKKSSPHVKLKALRIIKHLCQKGSPEFRRELQRN 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18401075  93 SVAVRNLFHYKGHPDPLKGDALNKAVRETAHETISAIFSE 132
Cdd:cd03572  80 SAAIRECTSYRGPPDPLHGDALYKAVREAAQELLEALFSD 119
 
Name Accession Description Interval E-value
ENTH_like_Tepsin cd03572
Epsin N-Terminal Homology (ENTH)-like domain of AP-4 complex accessory subunit Tepsin and ...
 13-132 6.45e-47

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: 161.57  E-value: 6.45e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401075  13 RSRMIDAVTSDEDKVAPVYKLEEICDLLRSSHvSIVKEFSEFILKRLDNKSPIVKQKALRLIKYAVGKSGSEFRREMQRN 92
Cdd:cd03572   1 DRPLLDKATSDDDEPTPGYLLEEIAKLTRSSP-GSCQELLDYLLKRLKKSSPHVKLKALRIIKHLCQKGSPEFRRELQRN 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18401075  93 SVAVRNLFHYKGHPDPLKGDALNKAVRETAHETISAIFSE 132
Cdd:cd03572  80 SAAIRECTSYRGPPDPLHGDALYKAVREAAQELLEALFSD 119
VHS smart00288
Domain present in VPS-27, Hrs and STAM; Unpublished observations. Domain of unknown function.
 13-148 9.67e-31

Domain present in VPS-27, Hrs and STAM; Unpublished observations. Domain of unknown function.


Pssm-ID: 197630 [Multi-domain]  Cd Length: 133  Bit Score: 117.01  E-value: 9.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401075     13 RSRMIDAVTSDEDKVAPVYKLEEICDLLRSSHVsIVKEFSEFILKRLDNKSPIVKQKALRLIKYAVGKSGSEFRREMQRN 92
Cdd:smart00288   1 VERLIDKATSPSLLEEDWELILEICDLINSTPD-GPKDAVRLLKKRLNNKNPHVALLALTLLDACVKNCGSKFHLEVASK 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18401075     93 SVAVrNLFHYKGHPDPLKGdaLNKAVRETAHETISAI-FSEENGTKPAAPESINRRI 148
Cdd:smart00288  80 EFLN-ELVKLIKPKYPLPL--VKKRILELIQEWADAFkNDPDLSQIVDVYDLLKKKG 133
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 21-104 6.07e-03

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: 37.15  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401075    21 TSDEDKVAPVYKLEEICDLLRSShvsivKEFSE---FILKRLDNKSP--IVKQKALRLIKYAVgKSGSE-FRREMQRNSV 94
Cdd:pfam01417  12 TNNDPWGPSGTLMDEIARLTYNY-----VEFPEimkMLWKRLNDKGKnwRHIYKALTLLEYLL-KNGSErVVDDLRENIY 85

                          90
                  ....*....|..
gi 18401075    95 AVRNL--FHYKG 104
Cdd:pfam01417  86 IIRTLtdFHYID 97
 
Name Accession Description Interval E-value
ENTH_like_Tepsin cd03572
Epsin N-Terminal Homology (ENTH)-like domain of AP-4 complex accessory subunit Tepsin and ...
 13-132 6.45e-47

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: 161.57  E-value: 6.45e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401075  13 RSRMIDAVTSDEDKVAPVYKLEEICDLLRSSHvSIVKEFSEFILKRLDNKSPIVKQKALRLIKYAVGKSGSEFRREMQRN 92
Cdd:cd03572   1 DRPLLDKATSDDDEPTPGYLLEEIAKLTRSSP-GSCQELLDYLLKRLKKSSPHVKLKALRIIKHLCQKGSPEFRRELQRN 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18401075  93 SVAVRNLFHYKGHPDPLKGDALNKAVRETAHETISAIFSE 132
Cdd:cd03572  80 SAAIRECTSYRGPPDPLHGDALYKAVREAAQELLEALFSD 119
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 13-131 1.09e-37

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: 136.01  E-value: 1.09e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401075  13 RSRMIDAVTSDEDKVAPVYKLEEICDLLRSShVSIVKEFSEFILKRLDNKSPIVKQKALRLIKYAVGKSGSEFRREMQRN 92
Cdd:cd00197   1 FEKTVEKATSNENMGPDWPLIMEICDLINET-NVGPKEAVDAIKKRINNKNPHVVLKALTLLEYCVKNCGERFHQEVASN 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18401075  93 SVAVRNLFHykgHPDPLKGDALNKAVRETAHETISAIFS 131
Cdd:cd00197  80 DFAVELLKF---DKSGLLGDDVSTNVREKAIELVQLWAS 115
VHS smart00288
Domain present in VPS-27, Hrs and STAM; Unpublished observations. Domain of unknown function.
 13-148 9.67e-31

Domain present in VPS-27, Hrs and STAM; Unpublished observations. Domain of unknown function.


Pssm-ID: 197630 [Multi-domain]  Cd Length: 133  Bit Score: 117.01  E-value: 9.67e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401075     13 RSRMIDAVTSDEDKVAPVYKLEEICDLLRSSHVsIVKEFSEFILKRLDNKSPIVKQKALRLIKYAVGKSGSEFRREMQRN 92
Cdd:smart00288   1 VERLIDKATSPSLLEEDWELILEICDLINSTPD-GPKDAVRLLKKRLNNKNPHVALLALTLLDACVKNCGSKFHLEVASK 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18401075     93 SVAVrNLFHYKGHPDPLKGdaLNKAVRETAHETISAI-FSEENGTKPAAPESINRRI 148
Cdd:smart00288  80 EFLN-ELVKLIKPKYPLPL--VKKRILELIQEWADAFkNDPDLSQIVDVYDLLKKKG 133
VHS cd03561
VHS (Vps27/Hrs/STAM) domain family; The VHS domain is present in Vps27 (Vacuolar Protein ...
 14-101 8.27e-04

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: 39.94  E-value: 8.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401075  14 SRMIDAVTSdEDKVAPVYKLE-EICDLLRSSHVSIvKEFSEFILKRLDNKSPIVKQKALRLIKYAVGKSGSEFRREmqrn 92
Cdd:cd03561   2 EELVEKATS-ESLTEPDWALNlEICDLVNSDPAQA-KDAVRALRKRLQSKNPKVQLLALTLLETLVKNCGAPFHSE---- 75


                ....*....
gi 18401075  93 sVAVRNLFH 101
Cdd:cd03561  76 -VASRDFLQ 83
VHS_Vps27 cd16979
VHS (Vps27/Hrs/STAM) domain of Vacuolar protein sorting-associated protein 27; Vacuolar ...
 35-120 3.99e-03

VHS (Vps27/Hrs/STAM) domain of Vacuolar protein sorting-associated protein 27; Vacuolar protein sorting-associated protein 27 (Vps27 or Vps27p) is also called Golgi retention defective protein 11, and is the yeast homolog of Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate). Together with class E vacuolar protein-sorting machinery protein HSE1, it comprises the ESCRT-0 complex, the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB). The complex directly binds to ubiquitinated transmembrane proteins and recruits both ubiquitin ligases and deubiquitinating enzymes. It is also required the efficient recycling of late Golgi proteins including the carboxypeptidase Y (CPY) sorting receptor, Vps10. Vps27 contain similar domains and motifs to Hrs; it contains an N-terminal VHS domain, which has a superhelical structure similar to the structure of ARM (Armadillo) repeats, a FYVE (Fab1p, YOTB, Vac1p, and EEA1) zinc finger domain, two Ubiquitin-Interacting Motifs (UIMs), a GAT (GGA and TOM) domain, two a P(S/T)XP motifs that recruit ESCRT-I, and a short peptide motif near the C-terminus that recruits clathrin.


Pssm-ID: 340776  Cd Length: 141  Bit Score: 38.33  E-value: 3.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401075  35 EICDLLRSSHVSiVKEFSEFILKRLDNKSPIVKQKALRLIKYAVGKSGSEFRREmqrnsVAVR----NLFHYkghpdpLK 110
Cdd:cd16979  27 EISDLIRSKSVP-PKDAMRSLKKRILHKNPNVQLLALKLTDVCVKNGGDHFLVE-----IASRefmdNLVSL------IR 94

                        90
                ....*....|
gi 18401075 111 GDALNKAVRE 120
Cdd:cd16979  95 STGVNPEVKE 104
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 21-104 6.07e-03

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: 37.15  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401075    21 TSDEDKVAPVYKLEEICDLLRSShvsivKEFSE---FILKRLDNKSP--IVKQKALRLIKYAVgKSGSE-FRREMQRNSV 94
Cdd:pfam01417  12 TNNDPWGPSGTLMDEIARLTYNY-----VEFPEimkMLWKRLNDKGKnwRHIYKALTLLEYLL-KNGSErVVDDLRENIY 85

                          90
                  ....*....|..
gi 18401075    95 AVRNL--FHYKG 104
Cdd:pfam01417  86 IIRTLtdFHYID 97
 
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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