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InterPro: IPR000225 Armadillo
Protein matches
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UniProtKB Matches: 2481 proteins |
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Accession
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IPR000225 Armadillo |
Type
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Repeat |
Signatures
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InterPro Relationships
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Found in
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IPR011989 Armadillo-like helical
IPR013284 Beta-catenin
IPR016024 Armadillo-type fold
IPR016617 Uncharacterised conserved protein UCP013899, metal binding
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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.
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Structural links
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Database links
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Pfam Clan: CL0019.14
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Interactions
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This domain has been experimentally proven to be involved in Protein:Protein interactions. Representative
data is shown with the following
example proteins:
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Additional Reading
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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