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Conserved domains on  [gi|2462553224|ref|XP_054171094|]
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AP-4 complex accessory subunit tepsin isoform X6 [Homo sapiens]

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 ...
 16-136 1.37e-53

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: 178.13  E-value: 1.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  16 RLPILLKGTSDDDVPCPGYLFEEIAtaEISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKR 95
Cdd:cd03572     1 DRPLLDKATSDDDEPTPGYLLEEIA--KLTRSSPGSCQELLDYLLKRLKKSSPHVKLKALRIIKHLCQKGSPEFRRELQR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462553224  96 NSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSD 136
Cdd:cd03572    79 NSAAIRECTSYRGPPDPLHGDALYKAVREAAQELLEALFSD 119
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 427-588 4.19e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  427 PARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPG-----DP 501
Cdd:PHA03307   118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPaepppST 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  502 SEAEARLAESRRWRPERIPGGTDSPKRGPSscawSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKE 581
Cdd:PHA03307   198 PPAAASPRPPRRSSPISASASSPAPAPGRS----AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEAS 273


                   ....*..
gi 2462553224  582 PPGSEPS 588
Cdd:PHA03307   274 GWNGPSS 280
 
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 ...
 16-136 1.37e-53

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: 178.13  E-value: 1.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  16 RLPILLKGTSDDDVPCPGYLFEEIAtaEISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKR 95
Cdd:cd03572     1 DRPLLDKATSDDDEPTPGYLLEEIA--KLTRSSPGSCQELLDYLLKRLKKSSPHVKLKALRIIKHLCQKGSPEFRRELQR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462553224  96 NSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSD 136
Cdd:cd03572    79 NSAAIRECTSYRGPPDPLHGDALYKAVREAAQELLEALFSD 119
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 427-588 4.19e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  427 PARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPG-----DP 501
Cdd:PHA03307   118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPaepppST 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  502 SEAEARLAESRRWRPERIPGGTDSPKRGPSscawSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKE 581
Cdd:PHA03307   198 PPAAASPRPPRRSSPISASASSPAPAPGRS----AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEAS 273


                   ....*..
gi 2462553224  582 PPGSEPS 588
Cdd:PHA03307   274 GWNGPSS 280
 
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 ...
 16-136 1.37e-53

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: 178.13  E-value: 1.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  16 RLPILLKGTSDDDVPCPGYLFEEIAtaEISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKR 95
Cdd:cd03572     1 DRPLLDKATSDDDEPTPGYLLEEIA--KLTRSSPGSCQELLDYLLKRLKKSSPHVKLKALRIIKHLCQKGSPEFRRELQR 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462553224  96 NSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSD 136
Cdd:cd03572    79 NSAAIRECTSYRGPPDPLHGDALYKAVREAAQELLEALFSD 119
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 19-135 3.27e-04

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: 40.49  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  19 ILLKGTSDDDVPCPGYLFEEIAtaEISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSa 98
Cdd:cd00197     4 TVEKATSNENMGPDWPLIMEIC--DLINETNVGPKEAVDAIKKRINNKNPHVVLKALTLLEYCVKNCGERFHQEVASND- 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462553224  99 FIQEAAAFagPPDPLHGNSLYQKVRAAAQDLGSTLFS 135
Cdd:cd00197    81 FAVELLKF--DKSGLLGDDVSTNVREKAIELVQLWAS 115
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 427-588 4.19e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 4.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  427 PARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPG-----DP 501
Cdd:PHA03307   118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPaepppST 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  502 SEAEARLAESRRWRPERIPGGTDSPKRGPSscawSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKE 581
Cdd:PHA03307   198 PPAAASPRPPRRSSPISASASSPAPAPGRS----AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEAS 273


                   ....*..
gi 2462553224  582 PPGSEPS 588
Cdd:PHA03307   274 GWNGPSS 280
PHA03378 PHA03378
EBNA-3B; Provisional
 379-532 5.99e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224 379 SSDLLPQEHILLRTRPWLQELSMGSPGPVTNKATKILRHFEASCGQLSPARGTSAEP--GPTAALPGPSDLLTDAVPLPG 456
Cdd:PHA03378  650 TPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPpaAPPGRAQRPAAATGRARPPAA 729

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462553224 457 SQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPGDPS-EAEARLAESRRWRPERIPGGTDSPKRGPSS 532
Cdd:PHA03378  730 APGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTpQPPPQAPPAPQQRPRGAPTPQPPPQAGPTS 806
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 24-106 6.74e-03

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: 36.73  E-value: 6.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224  24 TSDDDVPCPGYLFEEIATAeiSHESPGSSQcLLEYLLSRLhssSGHGK-----LKVLKILLYLCSHGSSFFLLILKRNSA 98
Cdd:cd03571     9 TSNEPWGPTGSQLAEIAQA--TFDYDDYQR-IMKVLWKRL---NDKGKnwrhvYKALTLLEYLLKNGSERVVDEFRDNLY 82


                  ....*...
gi 2462553224  99 FIQEAAAF 106
Cdd:cd03571    83 LIRTLQDF 90
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
428-594 8.78e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.06  E-value: 8.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224 428 ARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQP-LSSTPVSSRSPAPSS--GMPSSPVPTPPPDASPIPAPGDPSEA 504
Cdd:PRK07003  385 ARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAAtRAEAPPAAPAPPATAdrGDDAADGDAPVPAKANARASADSRCD 464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462553224 505 EARLAESRRWRPERIPGGTDSPKRGPSSCAWSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKEPPG 584
Cdd:PRK07003  465 ERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAA 544

                         170
                  ....*....|
gi 2462553224 585 SEPSAFAFLN 594
Cdd:PRK07003  545 RAGGAAAALD 554
 
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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