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13  structures 303  species 2  interactions 1195  sequences 20  architectures

Family: ANTH (PF07651)

Summary: ANTH domain

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "ANTH domain". More...

ANTH domain Edit Wikipedia article

ANTH domain
1hfa opm.gif
Clathrin assembly lymphoid myeloid leukemia (CALM) protein
Identifiers
Symbol ANTH
Pfam PF07651
InterPro IPR011417
OPM superfamily 39
OPM protein 1hfa

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]

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[edit]

HIP1; HIP1R; PICALM; SNAP91;

References[edit]

  1. ^ 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. 
  2. ^ 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[edit]

External links[edit]

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

ANTH domain Provide feedback

AP180 is an endocytotic accessory proteins 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].

Literature references

  1. Stahelin RV, Long F, Peter BJ, Murray D, De Camilli P, McMahon HT, Cho W; , J Biol Chem 2003;278:28993-28999.: Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. PUBMED:12740367 EPMC:12740367

  2. Duncan MC, Payne GS; , Trends Cell Biol 2003;13:211-215.: ENTH/ANTH domains expand to the Golgi. PUBMED:12742163 EPMC:12742163


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR011417

AP180 is an 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 [PUBMED:12740367, PUBMED:12742163].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan ENTH_VHS (CL0009), which has the following description:

This clan includes the related ENTH and ANTH domains as well as the VHS domain. The ENTH domain is approximately 150 residues in length and is a solenoid of alpha-helices. The various ENTH domains have various lipid specificities but the key feature that distinguishes it functionally from ANTH domains is its ability to bend membranes. It does this by folding an additional N-terminal helix on lipid binding. The ANTH domain is approximately 300 residues in length and is a PtdIns(4,5)P2 binding domain. It has no membrane bending properties. The VHS (Vps-27, Hrs and STAM) domain is a 140 residue long domain present in the very NH2-terminus of at least 60 proteins. Based on their functional characteristics and on recent data on the involvement of VHS in cargo recognition in trans-Golgi, VHS domains are considered to have a general membrane targeting/cargo recognition role in vesicular trafficking [5].

The clan contains the following 3 members:

ANTH ENTH VHS

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(29)
Full
(1195)
Representative proteomes NCBI
(1532)
Meta
(5)
RP15
(180)
RP35
(352)
RP55
(538)
RP75
(707)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(29)
Full
(1195)
Representative proteomes NCBI
(1532)
Meta
(5)
RP15
(180)
RP35
(352)
RP55
(538)
RP75
(707)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(29)
Full
(1195)
Representative proteomes NCBI
(1532)
Meta
(5)
RP15
(180)
RP35
(352)
RP55
(538)
RP75
(707)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

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.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: [1]
Previous IDs: none
Type: Domain
Author: Finn RD, Bateman A, McMahon H
Number in seed: 29
Number in full: 1195
Average length of the domain: 243.60 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 36.38 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.1 21.1
Trusted cut-off 21.1 21.1
Noise cut-off 21.0 21.0
Model length: 280
Family (HMM) version: 11
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

ANTH ENTH

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 ANTH domain has been found. There are 13 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 seqence.

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