Jump to content

ANTH domain

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by 2603:9000:a900:4577:c1e8:16fd:6c98:3c71 (talk) at 18:34, 27 June 2020 (Referenced previous edit supporting CALM is homologous to AP180). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

ANTH domain
Clathrin assembly lymphoid myeloid leukemia (CALM) protein
Identifiers
SymbolANTH
PfamPF07651
InterProIPR011417
OPM superfamily38
OPM protein1hfa
CDDcd03564
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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]

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. ^ https://web.archive.org/web/20070311024540/http://www.endocytosis.org/AP180/Clathrin.html
  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