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18  structures 114  species 1  interaction 558  sequences 24  architectures

Family: DIX (PF00778)

Summary: DIX domain

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DIX domain Provide feedback

The DIX domain is present in Dishevelled and axin [2]. This domain is involved in homo- and hetero-oligomerisation. It is involved in the homo- oligomerisation of mouse axin O35625 [3]. The axin DIX domain also interacts with the dishevelled DIX domain [4]. The DIX domain has also been called the DAX domain.

Literature references

  1. Zeng L, Fagotto F, Zhang T, Hsu W, Vasicek TJ, Perry WL 3rd, Lee JJ, Tilghman SM, Gumbiner BM, Costantini F; , Cell 1997;90:181-192.: The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling pathway that regulates embryonic axis formation. PUBMED:9230313 EPMC:9230313

  2. Cadigan KM, Nusse R; , Genes Dev 1997;11:3286-3305.: Wnt signaling: a common theme in animal development. PUBMED:9407023 EPMC:9407023

  3. Sakanaka C, Williams LT; , J Biol Chem 1999;274:14090-14093.: Functional domains of axin. Importance of the C terminus as an oligomerization domain. PUBMED:10318824 EPMC:10318824

  4. Kishida S, Yamamoto H, Hino S, Ikeda S, Kishida M, Kikuchi A; , Mol Cell Biol 1999;19:4414-4422.: DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability. PUBMED:10330181 EPMC:10330181


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001158

Dishevelled (Dsh) protein is an important component of the Wnt signal-transduction pathway. It has three relatively conserved domains: DIX, PDZ and DEP. The DIX domain of Dvl-1 (a mammalian Dishevelled homologue) shares 37% identity with the C-terminal region of Axin. Dsh can interact with the Axin/APC/GSK3/beta-catenin complex, and may thus modulate its activity [PUBMED:10330181].

The Wnt signalling pathway is conserved in various species from Caenorhabditis elegans to mammals, and plays important roles in development, cellular proliferation, and differentiation. The molecular mechanisms by which the Wnt signal regulates cellular functions are becoming increasingly well understood. Wnt stabilises cytoplasmic beta-catenin, which stimulates the expression of genes including c-myc, c-jun, fra-1, and cyclin D1. Axin and its homologue Axil are components of the Wnt signalling pathway that negatively regulate this pathway. Other components of the Wnt signalling pathway, including Dvl, glycogen synthase kinase-3beta (GSK-3beta), beta-catenin, and adenomatous polyposis coli (APC), interact with Axin, and the phosphorylation and stability of beta-catenin are regulated in the Axin complex. Axil has similar functions to Axin. Thus, Axin and Axil act as scaffold proteins in the Wnt signalling pathway, thereby modulating the Wnt-dependent cellular functions [PUBMED:10647780].

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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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
(25)
Full
(558)
Representative proteomes NCBI
(508)
Meta
(1)
RP15
(70)
RP35
(98)
RP55
(185)
RP75
(287)
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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
(25)
Full
(558)
Representative proteomes NCBI
(508)
Meta
(1)
RP15
(70)
RP35
(98)
RP55
(185)
RP75
(287)
Alignment:
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Sequence:
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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
(25)
Full
(558)
Representative proteomes NCBI
(508)
Meta
(1)
RP15
(70)
RP35
(98)
RP55
(185)
RP75
(287)
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

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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

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: Alignment kindly provided by SMART
Previous IDs: DAX;
Type: Family
Author: Marcu O, SMART
Number in seed: 25
Number in full: 558
Average length of the domain: 77.40 aa
Average identity of full alignment: 42 %
Average coverage of the sequence by the domain: 11.79 %

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 21.4 21.4
Trusted cut-off 21.8 21.6
Noise cut-off 21.2 20.9
Model length: 84
Family (HMM) version: 12
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

DIX

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 DIX domain has been found. There are 18 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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