Summary: Clathrin-binding domain of Huntingtin-interacting protein 1
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Clathrin-binding domain of Huntingtin-interacting protein 1 Provide feedback
HIP1_clath_bdg is the coiled-coil region of Huntington-interacting proteins 1. 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. Huntingtin-interacting protein 1 (HIP1) is an obligate binding partner for Huntungtin, and loss of this interaction triggers the cascade of events that results in the apoptosis of neuronal cells and the onset of Hungtinton's disease [1]. Clathrin light-chain binds to a flexible coiled-coil domain in HIP1 and induces a compact state that is refractory to actin binding [2].
Literature references
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Ybe JA, Mishra S, Helms S, Nix J;, J Mol Biol. 2007;367:8-15.: Crystal structure at 2.8 A of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding. PUBMED:17257618 EPMC:17257618
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Wilbur JD, Hwang PK, Brodsky FM, Fletterick RJ;, Acta Crystallogr D Biol Crystallogr. 2010;66:314-318.: Accommodation of structural rearrangements in the huntingtin-interacting protein 1 coiled-coil domain. PUBMED:20179344 EPMC:20179344
Internal database links
SCOOP: | DUF1640 Filament SMC_N |
This tab holds annotation information from the InterPro database.
InterPro entry 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].
Domain organisation
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Alignments
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Seed (30) |
Full (566) |
Representative proteomes | UniProt (921) |
NCBI (1661) |
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RP15 (24) |
RP35 (112) |
RP55 (360) |
RP75 (603) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (30) |
Full (566) |
Representative proteomes | UniProt (921) |
NCBI (1661) |
Meta (0) |
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RP15 (24) |
RP35 (112) |
RP55 (360) |
RP75 (603) |
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Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
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Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
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Curation
Seed source: | pdb_2no2 |
Previous IDs: | none |
Type: | Coiled-coil |
Sequence Ontology: | SO:0001080 |
Author: |
Coggill P |
Number in seed: | 30 |
Number in full: | 566 |
Average length of the domain: | 96.30 aa |
Average identity of full alignment: | 43 % |
Average coverage of the sequence by the domain: | 9.83 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 99 | ||||||||||||
Family (HMM) version: | 6 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HIP1_clath_bdg domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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