Summary: Armadillo-like
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This is the Wikipedia entry entitled "Armadillo repeats". More...
Armadillo repeats Edit Wikipedia article
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This article provides insufficient context for those unfamiliar with the subject. (December 2012) |
| Armadillo repeat domain | |||||||||
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| 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 | ||||||||
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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.
[edit] References
- ^ a b Huber AH, Nelson WJ, Weis WI (September 1997). "Three-dimensional structure of the armadillo repeat region of beta-catenin". Cell 90 (5): 871â82. doi:10.1016/S0092-8674(00)80352-9. PMID 9298899.
- ^ 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): 309â18. PMC 2132842. PMID 9786944. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2132842/.
- ^ McCrea PD, Turck CW, Gumbiner B (November 1991). "A homolog of the armadillo protein in Drosophila (plakoglobin) associated with E-cadherin". Science 254 (5036): 1359â61. PMID 1962194.
- ^ Hirschl D, Bayer P, Müller O (March 1996). "Secondary structure of an armadillo single repeat from the APC protein". FEBS Lett. 383 (1-2): 31â6. PMID 8612785.
- ^ Peifer, M; Berg, S; Reynolds, AB (1994). "A repeating amino acid motif shared by proteins with diverse cellular roles". Cell 76 (5): 789â91. doi:10.1016/0092-8674(94)90353-0. PMID 7907279.
- ^ Groves, MR; Barford, D (1999). "Topological characteristics of helical repeat proteins". Current opinion in structural biology 9 (3): 383â9. doi:10.1016/S0959-440X(99)80052-9. PMID 10361086.
[edit] External links
- Eukaryotic Linear Motif resource motif class TRG_NLS_Bipartite_1
- Eukaryotic Linear Motif resource motif class TRG_NLS_MonoCore_2
- Eukaryotic Linear Motif resource motif class TRG_NLS_MonoExtC_3
- Eukaryotic Linear Motif resource motif class TRG_NLS_MonoExtN_4
- Armadillo Domain Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)
- Armadillo/plakoglobin ARM repeat in PROSITE
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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
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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
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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
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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
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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
| PANDIT: | PF04826 |
| Pseudofam: | PF04826 |
| SYSTERS: | Arm_2 |
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...
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Pfam Clan
This family is a member of clan TPR (CL0020), which contains the following 117 members:
Adaptin_N Alkyl_sulf_dimr Apc3 Apc5 API5 Arm Arm_2 Avirulence BTAD CAS_CSE1 ChAPs CLASP_N Clathrin Clathrin-link Clathrin_propel Cnd1 Cnd3 Coatomer_E Cohesin_HEAT Cohesin_load CRM1_C Cse1 DNA_alkylation Drf_FH3 Drf_GBD DUF1822 DUF2225 DUF3385 DUF3458 DUF3808 DUF3856 EST1_DNA_bind FAT Fis1_TPR_C Fis1_TPR_N Foie-gras_1 GUN4 HAT HEAT HEAT_2 HEAT_EZ HEAT_PBS HemY_N IBB IBN_N IFRD KAP Leuk-A4-hydro_C LRV LRV_FeS MA3 MIF4G MIF4G_like MIF4G_like_2 MMS19_C Mo25 MRP-S27 NARP1 Neurochondrin Nro1 NSF Paf67 ParcG PC_rep PHAT PI3Ka PPP5 PPR PPR_1 PPR_2 PPR_3 Proteasom_PSMB PUF Rab5-bind Rapsyn_N RPN7 Sel1 SHNi-TPR SNAP SPO22 ST7 Suf SusD SusD-like SusD-like_2 SusD-like_3 Tcf25 TOM20_plant TPR_1 TPR_10 TPR_11 TPR_12 TPR_14 TPR_15 TPR_16 TPR_17 TPR_18 TPR_19 TPR_2 TPR_20 TPR_21 TPR_3 TPR_4 TPR_5 TPR_6 TPR_7 TPR_8 TPR_9 Upf2 V-ATPase_H_C V-ATPase_H_N Vac14_Fab1_bd Vitellogenin_N Vps39_1 W2 Xpo1 YfiOAlignments
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) |
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| RP15 (33) |
RP35 (46) |
RP55 (80) |
RP75 (216) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
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) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (33) |
RP35 (46) |
RP55 (80) |
RP75 (216) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
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
| 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
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 254 | ||||||||||||
| Family (HMM) version: | 8 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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