Please note: this site relies heavily on the use of javascript. Without a javascript-enabled browser, this site will not function correctly. Please enable javascript and reload the page, or switch to a different browser.
0  structures 78  species 0  interactions 392  sequences 14  architectures

Family: Arm_2 (PF04826)

Summary: Armadillo-like

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 "Armadillo repeats". More...

Armadillo repeats Edit Wikipedia article

Armadillo repeat domain
PDB 3bct EBI.jpg
Structure of the armadillo domain of beta-catenin.[1]
Identifiers
Symbol Arm
Pfam PF00514
Pfam clan CL0020
InterPro IPR000225
SMART SM00185
PROSITE PS50176
SCOP 3bct
SUPERFAMILY 3bct

Armadillo repeat is the name of a characteristic, repetitive amino acid sequence found in β-catenin and many other proteins, like α-importin,[2] plakoglobin,[3] or adenomatous polyposis coli (APC).[4] Its name derives from the historical name of the β-catenin gene in the fruitfly Drosophila: where they were first discovered. Armadillo repeats are approximately 40 amino acids long and proteins that contain them usually have many tandemly repeated copies.[5][6] These tandem repeats usually fold together to form a single, rigid protein domain called the armadillo (ARM) domain. Because ARM domains can consist of a variable number of repeats, they are a good example of solenoid protein domains. The best characterized example of armadillo domains is found in β-catenin. β-catenin is a protein involved in linking cadherin cell adhesion proteins to the cytoskeleton,[1] but the Armadillo repeat is found in a wide range of proteins with other functions. This type of protein domain is important in transducing WNT signals during embryonic development.

References

  1. ^ a b Huber AH, Nelson WJ, Weis WI (September 1997). "Three-dimensional structure of the armadillo repeat region of beta-catenin". Cell 90 (5): 871–82. doi:10.1016/S0092-8674(00)80352-9. PMID 9298899. 
  2. ^ Herold A, Truant R, Wiegand H, Cullen BR (October 1998). "Determination of the functional domain organization of the importin alpha nuclear import factor". J. Cell Biol. 143 (2): 309–18. doi:10.1083/jcb.143.2.309. PMC 2132842. PMID 9786944. 
  3. ^ McCrea PD, Turck CW, Gumbiner B (November 1991). "A homolog of the armadillo protein in Drosophila (plakoglobin) associated with E-cadherin". Science 254 (5036): 1359–61. doi:10.1126/science.1962194. PMID 1962194. 
  4. ^ Hirschl D, Bayer P, Müller O (March 1996). "Secondary structure of an armadillo single repeat from the APC protein". FEBS Lett. 383 (1-2): 31–6. doi:10.1016/0014-5793(96)00215-3. PMID 8612785. 
  5. ^ Peifer, M; Berg, S; Reynolds, AB (1994). "A repeating amino acid motif shared by proteins with diverse cellular roles". Cell 76 (5): 789–91. doi:10.1016/0092-8674(94)90353-0. PMID 7907279.  edit
  6. ^ Groves, MR; Barford, D (1999). "Topological characteristics of helical repeat proteins". Current opinion in structural biology 9 (3): 383–9. doi:10.1016/S0959-440X(99)80052-9. PMID 10361086.  edit

External links


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.

Armadillo-like Provide feedback

This domain contains armadillo-like repeats [1]. Proteins containing this domain interact with numerous other proteins, through these interactions they are involved in a wide variety of processes including carcinogenesis [2] control of cellular ageing and survival [1] regulation of circadian rhythm [3] and lysosomal sorting of G protein-coupled receptors [4].

Literature references

  1. Heese K, Yamada T, Akatsu H, Yamamoto T, Kosaka K, Nagai Y, Sawada T;, J Cell Biochem. 2004;91:1030-1042.: Characterizing the new transcription regulator protein p60TRP. PUBMED:15034937 EPMC:15034937

  2. Zhou X, Yang G, Huang R, Chen X, Hu G;, FEBS Lett. 2007;581:4943-4948.: SVH-B interacts directly with p53 and suppresses the transcriptional activity of p53. PUBMED:17904127 EPMC:17904127

  3. Matsuki T, Kiyama A, Kawabuchi M, Okada M, Nagai K;, Brain Res. 2001;916:1-10.: A novel protein interacts with a clock-related protein, rPer1. PUBMED:11597585 EPMC:11597585

  4. Whistler JL, Enquist J, Marley A, Fong J, Gladher F, Tsuruda P, Murray SR, Von Zastrow M;, Science. 2002;297:615-620.: Modulation of postendocytic sorting of G protein-coupled receptors. PUBMED:12142540 EPMC:12142540


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR006911

This domain contains armadillo-like repeats [PUBMED:15034937]. Proteins containing this domain interact with numerous other proteins, through these interactions they are involved in a wide variety of processes including carcinogenesis [PUBMED:17904127], control of cellular ageing and survival [PUBMED:15034937], regulation of circadian rhythm [PUBMED:11597585] and lysosomal sorting of G protein-coupled receptors [PUBMED:12142540].

Domain organisation

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

Loading domain graphics...

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...

View options

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
(11)
Full
(392)
Representative proteomes NCBI
(672)
Meta
(4)
RP15
(33)
RP35
(46)
RP55
(80)
RP75
(216)
Jalview View  View  View  View  View  View  View  View 
HTML View  View  View  View  View  View     
PP/heatmap 1 View  View  View  View  View     
Pfam viewer View  View             

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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

Format an alignment

  Seed
(11)
Full
(392)
Representative proteomes NCBI
(672)
Meta
(4)
RP15
(33)
RP35
(46)
RP55
(80)
RP75
(216)
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
(11)
Full
(392)
Representative proteomes NCBI
(672)
Meta
(4)
RP15
(33)
RP35
(46)
RP55
(80)
RP75
(216)
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.

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: Pfam-B_2700 (release 7.6)
Previous IDs: DUF634;
Type: Family
Author: Kerrison ND, Eberhardt R
Number in seed: 11
Number in full: 392
Average length of the domain: 217.60 aa
Average identity of full alignment: 29 %
Average coverage of the sequence by the domain: 44.07 %

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 20.4 20.4
Trusted cut-off 20.4 20.4
Noise cut-off 20.3 20.3
Model length: 254
Family (HMM) version: 8
Download: download the raw HMM for this family

Species distribution

Sunburst controls

Show

This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

Loading sunburst data...

Tree controls

Hide

The tree shows the occurrence of this domain across different species. More...

Loading...

Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.