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ANTH domain


Clathrin assembly lymphoid myeloid leukemia (CALM) protein

Identifiers
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].

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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 endocytosis.org.

Human proteins containing this domain

HIP1; HIP1R; PICALM; SNAP91;

References

^ 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.
^ 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

Categories: Protein domains | Peripheral membrane proteins