SMART: Pfam domain HIP1_clath

The domain within your query sequence starts at position 71 and ends at position 161; the E-value for the HIP1_clath_bdg domain shown below is 4.4e-24.

HADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQEL
QVLHSNLETSAQSEAKWLTQIAELEKEQGSL

HIP1_clath_bdg

PFAM accession number:	PF16515
Interpro abstract (IPR032422):	This entry represents the coiled-coil region of Huntingtin-interacting protein 1 (HIP1). It carries a highly conserved HADLLRKN sequence motif at its N terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. This binding then stimulates clathrin lattice assembly. HIP1 is an obligate binding partner for Huntingtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Huntington's disease [ (PUBMED:17257618) ]. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding [ (PUBMED:20179344) ].

PFAM accession number:

PF16515

Interpro abstract (IPR032422):

This entry represents the coiled-coil region of Huntingtin-interacting protein 1 (HIP1). It carries a highly conserved HADLLRKN sequence motif at its N terminus which effects the binding of HIP1R to clathrin light-chain EED regulatory site. This binding then stimulates clathrin lattice assembly. HIP1 is an obligate binding partner for Huntingtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Huntington's disease [ (PUBMED:17257618) ]. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding [ (PUBMED:20179344) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry HIP1_clath_bdg