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ANTH domain

Clathrin assembly lymphoid myeloid leukemia (CALM) protein
Symbol ANTH
Pfam PF07651
InterPro IPR011417
OPM family 39
OPM protein 1hfa
Available PDB structures:

1hx8A:21-299 1hg5A:19-285 1hg2A:19-285 1hf8A:19-285 1hfaA:19-285

The ANTH domain is a membrane binding domain that shows weak specificity for PtdIns(4,5)P2. It was found in AP180 (a.k.a. CALM) endocytotic accessory protein 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[1][2].

Its structure is a solenoid of 9 helices. The PtdIns(4,5)P2 binding residues are spread over several helices at the tip of the structure. The PtdIns(4,5)P2 binding sequence is Kx9Kx(K/R)(H/Y).

An ANTH domain is also found in HIP1 and HIP1R, and the PtdIns(4,5)P2 binding sequence is conserved. More information is found on


Human proteins containing this domain



  1. ^ de Camilli P, McMahon HT, Peter BJ, Stahelin RV, Cho W, Long F, Murray D (2003). "Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains". J. Biol. Chem. 278 (31): 28993-28999. PMID 12740367.
  2. ^ Payne GS, Duncan MC (2003). "ENTH/ANTH domains expand to the Golgi". Trends Cell Biol. 13 (5): 211-215. PMID 12742163.

Ford, M.G.J., Pearse, B., Higgins, M., Vallis, Y., Owen, D., Gibson, A., Hopkins, C.R., Evans, P.R. and McMahon, H.T. (2001) Simultaneous binding of PI (4,5)P2 and clathrin by AP180 causes nucleation of clathrin lattices on membranes. Science 291, 1051-1055. pubmed

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "ANTH_domain". A list of authors is available in Wikipedia.
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