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InterPro: IPR000225 Armadillo

Protein matchesHelp
UniProtKB
Matches:
2481 proteins
AccessionHelp IPR000225 Armadillo
TypeHelp Repeat
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR011989 Armadillo-like helical
IPR013284 Beta-catenin
IPR016024 Armadillo-type fold
IPR016617 Uncharacterised conserved protein UCP013899, metal binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The armadillo (Arm) repeat is an approximately 40 amino acid long tandemly repeated sequence motif first identified in the Drosophila melanogaster segment polarity gene armadillo involved in signal transduction through wingless. Animal Arm-repeat proteins function in various processes, including intracellular signalling and cytoskeletal regulation, and include such proteins as beta-catenin, the junctional plaque protein plakoglobin, the adenomatous polyposis coli (APC) tumour suppressor protein, and the nuclear transport factor importin-alpha, amongst others [1]. A subset of these proteins is conserved across eukaryotic kingdoms. In higher plants, some Arm-repeat proteins function in intracellular signalling like their mammalian counterparts, while others have novel functions [2].

The 3-dimensional fold of an armadillo repeat is known from the crystal structure of beta-catenin, where the 12 repeats form a superhelix of alpha helices with three helices per unit [3]. The cylindrical structure features a positively charged grove, which presumably interacts with the acidic surfaces of the known interaction partners of beta-catenin.

Structural linksHelp
PDB - click here
CATH: 1.25.10.10
Database linksHelp
PROSITE doc: PDOC50176
PANDIT: PF00514
Blocks: IPB000225
Pfam Clan: CL0019.14
InteractionsHelp
This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000225 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O44326 Protein humpback-2

O60763 General vesicular transport factor p115

P12024 Chaoptin

P52293 Importin subunit alpha-2

Q02821 Importin subunit alpha

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000225 Armadillo
IPR013284 Beta-catenin
IPR003591 Leucine-rich repeat, typical subtype
IPR016024 Armadillo-type fold
IPR001611 Leucine-rich repeat
IPR011989 Armadillo-like helical
IPR006953 Uso1/p115 like vesicle tethering protein, head region
IPR006955 Uso1/p115 like vesicle tethering protein, C-terminal
IPR002652 Importin-alpha-like, importin-beta-binding domain
IPR020474 Toll-like receptor, leucine rich repeat-containing
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Hatzfeld M.
The armadillo family of structural proteins.
Int. Rev. Cytol. 186 179-224 1999 [PubMed: 9770300]
2. Coates JC.
Armadillo repeat proteins: beyond the animal kingdom.
Trends Cell Biol. 13 463-71 2003 [PubMed: 12946625]
http://dx.doi.org/10.1016/S0962-8924(03)00167-3
3. Huber AH, Nelson WJ, Weis WI.
Three-dimensional structure of the armadillo repeat region of beta-catenin.
Cell 90 871-82 1997 [PubMed: 9298899]
http://dx.doi.org/10.1016/S0092-8674(00)80352-9

Additional ReadingHelp
Choi HJ, Weis WI.
Structure of the armadillo repeat domain of plakophilin 1.
J. Mol. Biol. 346 2005 367-76 [PubMed: 15663951]
http://dx.doi.org/10.1016/j.jmb.2004.11.048
Yang CK, Kim JH, Li H, Stallcup MR.
Differential use of functional domains by coiled-coil coactivator in its synergistic coactivator function with beta-catenin or GRIP1.
J. Biol. Chem. 281 2006 3389-97 [PubMed: 16344550]
http://dx.doi.org/10.1074/jbc.M510403200
Su LK, Vogelstein B, Kinzler KW.
Association of the APC tumor suppressor protein with catenins.
Science 262 1993 1734-7 [PubMed: 8259519]
http://www.sciencemag.org/cgi/content/abstract/262/5140/1734
Rubinfeld B, Souza B, Albert I, Muller O, Chamberlain SH, Masiarz FR, Munemitsu S, Polakis P.
Association of the APC gene product with beta-catenin.
Science 262 1993 1731-4 [PubMed: 8259518]
http://www.sciencemag.org/cgi/content/abstract/262/5140/1731
Mitrousis G, Olia AS, Walker-Kopp N, Cingolani G.
Molecular basis for the recognition of snurportin 1 by importin beta.
J. Biol. Chem. 283 2008 7877-84 [PubMed: 18187419]
http://dx.doi.org/10.1074/jbc.M709093200
Peifer M, Wieschaus E.
The segment polarity gene armadillo encodes a functionally modular protein that is the Drosophila homolog of human plakoglobin.
Cell 63 1990 1167-76 [PubMed: 2261639]
http://dx.doi.org/10.1016/0092-8674(90)90413-9
Tarendeau F, Boudet J, Guilligay D, Mas PJ, Bougault CM, Boulo S, Baudin F, Ruigrok RW, Daigle N, Ellenberg J, Cusack S, Simorre JP, Hart DJ.
Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit.
Nat. Struct. Mol. Biol. 14 2007 229-33 [PubMed: 17310249]
http://dx.doi.org/10.1038/nsmb1212
Chen MH, Ben-Efraim I, Mitrousis G, Walker-Kopp N, Sims PJ, Cingolani G.
Phospholipid scramblase 1 contains a nonclassical nuclear localization signal with unique binding site in importin alpha.
J. Biol. Chem. 280 2005 10599-606 [PubMed: 15611084]
http://dx.doi.org/10.1074/jbc.M413194200
Raurell I, Castano J, Franci C, Garcia de Herreros A, Dunach M.
Presenilin-1 interacts with plakoglobin and enhances plakoglobin-Tcf-4 association. Implications for the regulation of beta-catenin/Tcf-4-dependent transcription.
J. Biol. Chem. 281 2006 1401-11 [PubMed: 16306047]
http://dx.doi.org/10.1074/jbc.M508153200
Choi HJ, Huber AH, Weis WI.
Thermodynamics of beta-catenin-ligand interactions: the roles of the N- and C-terminal tails in modulating binding affinity.
J. Biol. Chem. 281 2006 1027-38 [PubMed: 16293619]
http://dx.doi.org/10.1074/jbc.M511338200
Peifer M, Berg S, Reynolds AB.
A repeating amino acid motif shared by proteins with diverse cellular roles.
Cell 76 1994 789-91 [PubMed: 7907279]
http://dx.doi.org/10.1016/0092-8674(94)90353-0
Shaikh N, Terajima J, Watanabe H.
IpaC of Shigella binds to the C-terminal domain of beta-catenin.
Microb. Pathog. 35 2003 107-17 [PubMed: 12927518]
http://dx.doi.org/10.1016/S0882-4010(03)00093-7
Gumbiner BM.
Signal transduction of beta-catenin.
Curr. Opin. Cell Biol. 7 1995 634-40 [PubMed: 8573337]
http://dx.doi.org/10.1016/0955-0674(95)80104-9
Sampietro J, Dahlberg CL, Cho US, Hinds TR, Kimelman D, Xu W.
Crystal structure of a beta-catenin/BCL9/Tcf4 complex.
Mol. Cell 24 2006 293-300 [PubMed: 17052462]
http://dx.doi.org/10.1016/j.molcel.2006.09.001
Cavallo R, Rubenstein D, Peifer M.
Armadillo and dTCF: a marriage made in the nucleus.
Curr. Opin. Genet. Dev. 7 1997 459-66 [PubMed: 9309175]
http://dx.doi.org/10.1016/S0959-437X(97)80071-8
Olson LE, Tollkuhn J, Scafoglio C, Krones A, Zhang J, Ohgi KA, Wu W, Taketo MM, Kemler R, Grosschedl R, Rose D, Li X, Rosenfeld MG.
Homeodomain-mediated beta-catenin-dependent switching events dictate cell-lineage determination.
Cell 125 2006 593-605 [PubMed: 16678101]
http://dx.doi.org/10.1016/j.cell.2006.02.046
Groves MR, Barford D.
Topological characteristics of helical repeat proteins.
Curr. Opin. Struct. Biol. 9 1999 383-9 [PubMed: 10361086]
http://dx.doi.org/10.1016/S0959-440X(99)80052-9
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InterPro 23.1