|PROSITE documentation PDOC50942 [for PROSITE entry PS50942]|
The epsin NH2-terminal homology (ENTH) domain is a membrane interacting module of ~140 amino acids. Typically it is located within 20 residues of the NH2-terminus of proteins that often contain consensus sequences for binding to clathrin coat components and their accessory factors, and therefore function as endocytic adaptors. ENTH domain containing proteins have additional roles in signaling and actin regulation and may have yet other actions in the nucleus. The ENTH domain is found associated with other domains such as UIM (see <PDOC50330>), the EH domain binding motif NPF, the DPW/F motif or the I/LWEQ domain. The ENTH domain has been shown to bind to phosphoinositides, as well as to interact with proteins, such as the transcription factor PLZF and tubulin [1,2,3,4].
The ENTH domain forms a compact globular structure, composed of eight α-helices connected by loops of varying length (see <PDB:1EDU>). The general topology of the domain is determined by three helical hairpins that are stacked consecutively with a right handed twist. The most highly conserved amino acids fall roughly into two classes: (i) internal residues that are involved in packing and therefore are necessary for structural integrity, and (ii) solvent accessible residues that may be involved in protein-protein interactions. The ENTH domain is structurally similar to the VHS domain (see <PDOC50179>) [4,5].
Some proteins known to contain a ENTH domain are listed below:
The profile we developed spans the entire ENTH domain.Last update:
November 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Kay B.K. Yamabhai M. Wendland B. Emr S.D.|
|Title||Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery.|
|Source||Protein Sci. 8:435-438(1999).|
|2||Authors||Itoh T. Koshiba S. Kigawa T. Kikuchi A. Yokoyama S. Takenawa T.|
|Title||Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis.|
|3||Authors||Ford M.G.J. Pearse B.M.F. Higgins M.K. Vallis Y. Owen D.J. Gibson A. Hopkins C.R. Evans P.R. McMahon H.T.|
|Title||Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes.|
|4||Authors||Hyman J. Chen H. Di Fiore P.P. De Camilli P. Brunger A.T.|
|Title||Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF).|
|Source||J. Cell Biol. 149:537-546(2000).|
|5||Authors||De Camilli P. Chen H. Hyman J. Panepucci E. Bateman A. Brunger A.T.|
|Source||FEBS Lett. 513:11-18(2002).|