ANTH domain

The ANTH domain is a membrane binding domain that shows weak specificity for PtdIns(4,5)P2. It was found in AP180 (homologous to CALM[1]) 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.[2][3]

ANTH domain
Clathrin assembly lymphoid myeloid leukemia (CALM) protein
Identifiers
SymbolANTH
PfamPF07651
InterProIPR011417
OPM superfamily38
OPM protein1hfa
CDDcd03564

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
  1. "Clathrin and its interactions with AP180". Archived from the original on 2007-03-11.
  2. 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): 28993–9. doi:10.1074/jbc.M302865200. PMID 12740367.
  3. Payne GS, Duncan MC (2003). "ENTH/ANTH domains expand to the Golgi". Trends Cell Biol. 13 (5): 211–5. doi:10.1016/S0962-8924(03)00076-X. PMID 12742163.

Further reading
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