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Conserved domains on  [gi|21389577|ref|NP_653280|]
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AP-4 complex accessory subunit tepsin isoform 2 [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 ...
 16-134 5.41e-56

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: 183.14  E-value: 5.41e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577  16 RLPILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNS 95
Cdd:cd03572   1 DRPLLDKATSDDDEPTPGYLLEEIAKLTRSSPGSCQELLDYLLKRLKKSSPHVKLKALRIIKHLCQKGSPEFRRELQRNS 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21389577  96 AFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSD 134
Cdd:cd03572  81 AAIRECTSYRGPPDPLHGDALYKAVREAAQELLEALFSD 119
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 357-518 1.63e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577   357 PARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVF--LQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPA---PGDP 431
Cdd:PHA03307  118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASppAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPaepPPST 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577   432 SEAEARLAESRRWRPERIPGGTDSPKRGPSscawSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKE 511
Cdd:PHA03307  198 PPAAASPRPPRRSSPISASASSPAPAPGRS----AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEAS 273


                  ....*..
gi 21389577   512 PPGSEPS 518
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 ...
 16-134 5.41e-56

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: 183.14  E-value: 5.41e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577  16 RLPILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNS 95
Cdd:cd03572   1 DRPLLDKATSDDDEPTPGYLLEEIAKLTRSSPGSCQELLDYLLKRLKKSSPHVKLKALRIIKHLCQKGSPEFRRELQRNS 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21389577  96 AFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSD 134
Cdd:cd03572  81 AAIRECTSYRGPPDPLHGDALYKAVREAAQELLEALFSD 119
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 357-518 1.63e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577   357 PARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVF--LQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPA---PGDP 431
Cdd:PHA03307  118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASppAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPaepPPST 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577   432 SEAEARLAESRRWRPERIPGGTDSPKRGPSscawSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKE 511
Cdd:PHA03307  198 PPAAASPRPPRRSSPISASASSPAPAPGRS----AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEAS 273


                  ....*..
gi 21389577   512 PPGSEPS 518
Cdd:PHA03307  274 GWNGPSS 280
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 24-99 3.36e-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: 37.54  E-value: 3.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21389577    24 TSDDDVPCPGYLFEEIAKISHeSPGSSQCLLEYLLSRL--HSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSAFIQ 99
Cdd:pfam01417  12 TNNDPWGPSGTLMDEIARLTY-NYVEFPEIMKMLWKRLndKGKNWRHIYKALTLLEYLLKNGSERVVDDLRENIYIIR 88
 
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 ...
 16-134 5.41e-56

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: 183.14  E-value: 5.41e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577  16 RLPILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNS 95
Cdd:cd03572   1 DRPLLDKATSDDDEPTPGYLLEEIAKLTRSSPGSCQELLDYLLKRLKKSSPHVKLKALRIIKHLCQKGSPEFRRELQRNS 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21389577  96 AFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSD 134
Cdd:cd03572  81 AAIRECTSYRGPPDPLHGDALYKAVREAAQELLEALFSD 119
VHS_ENTH_ANTH cd00197
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ...
 19-133 2.86e-06

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: 46.26  E-value: 2.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577  19 ILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSaFI 98
Cdd:cd00197   4 TVEKATSNENMGPDWPLIMEICDLINETNVGPKEAVDAIKKRINNKNPHVVLKALTLLEYCVKNCGERFHQEVASND-FA 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 21389577  99 QEAAAFagPPDPLHGNSLYQKVRAAAQDLGSTLFS 133
Cdd:cd00197  83 VELLKF--DKSGLLGDDVSTNVREKAIELVQLWAS 115
ENTH cd03571
Epsin N-Terminal Homology (ENTH) domain family; The Epsin N-Terminal Homology (ENTH) domain is ...
 24-104 2.37e-04

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: 40.96  E-value: 2.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577  24 TSDDDVPCPGYLFEEIAKISHESPGSSQcLLEYLLSRLhssSGHGK-----LKVLKILLYLCSHGSSFFLLILKRNSAFI 98
Cdd:cd03571   9 TSNEPWGPTGSQLAEIAQATFDYDDYQR-IMKVLWKRL---NDKGKnwrhvYKALTLLEYLLKNGSERVVDEFRDNLYLI 84


                ....*.
gi 21389577  99 QEAAAF 104
Cdd:cd03571  85 RTLQDF 90
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 357-518 1.63e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577   357 PARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVF--LQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPA---PGDP 431
Cdd:PHA03307  118 PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASppAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPaepPPST 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577   432 SEAEARLAESRRWRPERIPGGTDSPKRGPSscawSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKE 511
Cdd:PHA03307  198 PPAAASPRPPRRSSPISASASSPAPAPGRS----AADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEAS 273


                  ....*..
gi 21389577   512 PPGSEPS 518
Cdd:PHA03307  274 GWNGPSS 280
PHA03378 PHA03378
EBNA-3B; Provisional
 309-462 2.61e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.82  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577  309 SSDLLPQEHILLRTRPWLQELSMGSPGPVTNKATKILRHFEASCGQLSPARGTSAEP--GPTAALPGPSDLLTDAVPLPG 386
Cdd:PHA03378 650 TPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPpaAPPGRAQRPAAATGRARPPAA 729

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21389577  387 SQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPGDPS-EAEARLAESRRWRPERIPGGTDSPKRGPSS 462
Cdd:PHA03378 730 APGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTpQPPPQAPPAPQQRPRGAPTPQPPPQAGPTS 806
ENTH pfam01417
ENTH domain; The ENTH (Epsin N-terminal homology) domain is found in proteins involved in ...
 24-99 3.36e-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: 37.54  E-value: 3.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21389577    24 TSDDDVPCPGYLFEEIAKISHeSPGSSQCLLEYLLSRL--HSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSAFIQ 99
Cdd:pfam01417  12 TNNDPWGPSGTLMDEIARLTY-NYVEFPEIMKMLWKRLndKGKNWRHIYKALTLLEYLLKNGSERVVDDLRENIYIIR 88
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
358-524 4.36e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.83  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577  358 ARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQP-LSSTPVSSRSPAPSS--GMPSSPVPTPPPDASPIPAPGDPSEA 434
Cdd:PRK07003 385 ARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAAtRAEAPPAAPAPPATAdrGDDAADGDAPVPAKANARASADSRCD 464

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21389577  435 EARLAESRRWRPERIPGGTDSPKRGPSSCAWSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKEPPG 514
Cdd:PRK07003 465 ERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAA 544

                        170
                 ....*....|
gi 21389577  515 SEPSAFAFLN 524
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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