ARM_DROME
ID ARM_DROME Reviewed; 843 AA.
AC P18824; A4V3V0; O02371; Q0KHX2; Q8IRW7; Q9W546;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Armadillo segment polarity protein;
GN Name=arm; ORFNames=CG11579;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=2707602; DOI=10.1101/gad.3.1.96;
RA Riggleman B., Wieschaus E., Schedl P.;
RT "Molecular analysis of the armadillo locus: uniformly distributed
RT transcripts and a protein with novel internal repeats are associated with a
RT Drosophila segment polarity gene.";
RL Genes Dev. 3:96-113(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CYTOPLASMIC AND NEURAL), FUNCTION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Head;
RX PubMed=9635189; DOI=10.1016/s0960-9822(98)70249-0;
RA Loureiro J., Peifer M.;
RT "Roles of Armadillo, a Drosophila catenin, during central nervous system
RT development.";
RL Curr. Biol. 8:622-632(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP PHOSPHORYLATION.
RX PubMed=7529201; DOI=10.1006/dbio.1994.1336;
RA Peifer M., Pai L.-M., Casey M.;
RT "Phosphorylation of the Drosophila adherens junction protein Armadillo:
RT roles for wingless signal and zeste-white 3 kinase.";
RL Dev. Biol. 166:543-556(1994).
RN [8]
RP INTERACTION WITH MER AND MOE, AND SUBCELLULAR LOCATION.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=8666669; DOI=10.1083/jcb.133.4.843;
RA McCartney B.M., Fehon R.G.;
RT "Distinct cellular and subcellular patterns of expression imply distinct
RT functions for the Drosophila homologues of moesin and the neurofibromatosis
RT 2 tumor suppressor, merlin.";
RL J. Cell Biol. 133:843-852(1996).
RN [9]
RP PHOSPHORYLATION.
RX PubMed=11927557; DOI=10.1093/emboj/21.7.1733;
RA Yanagawa S., Matsuda Y., Lee J.S., Matsubayashi H., Sese S., Kadowaki T.,
RA Ishimoto A.;
RT "Casein kinase I phosphorylates the Armadillo protein and induces its
RT degradation in Drosophila.";
RL EMBO J. 21:1733-1742(2002).
RN [10]
RP INTERACTION WITH INX2.
RX PubMed=15047872; DOI=10.1091/mbc.e04-01-0056;
RA Bauer R., Lehmann C., Martini J., Eckardt F., Hoch M.;
RT "Gap junction channel protein innexin 2 is essential for epithelial
RT morphogenesis in the Drosophila embryo.";
RL Mol. Biol. Cell 15:2992-3004(2004).
RN [11]
RP INTERACTION WITH MYO31DF, AND SUBCELLULAR LOCATION.
RX PubMed=16598259; DOI=10.1038/nature04623;
RA Speder P., Adam G., Noselli S.;
RT "Type ID unconventional myosin controls left-right asymmetry in
RT Drosophila.";
RL Nature 440:803-807(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-650; SER-688 AND SER-694, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [13]
RP INTERACTION WITH MYO31DF.
RX PubMed=22491943; DOI=10.1242/dev.047589;
RA Petzoldt A.G., Coutelis J.B., Geminard C., Speder P., Suzanne M.,
RA Cerezo D., Noselli S.;
RT "DE-Cadherin regulates unconventional Myosin ID and Myosin IC in Drosophila
RT left-right asymmetry establishment.";
RL Development 139:1874-1884(2012).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ALPHA-CAT.
RX PubMed=25653389; DOI=10.1242/jcs.163824;
RA Escobar D.J., Desai R., Ishiyama N., Folmsbee S.S., Novak M.N.,
RA Flozak A.S., Daugherty R.L., Mo R., Nanavati D., Sarpal R., Leckband D.,
RA Ikura M., Tepass U., Gottardi C.J.;
RT "alpha-Catenin phosphorylation promotes intercellular adhesion through a
RT dual-kinase mechanism.";
RL J. Cell Sci. 128:1150-1165(2015).
CC -!- FUNCTION: Isoform neural may associate with CadN and participate in the
CC transmission of developmental information. Can associate with alpha-
CC catenin. Isoform cytoplasmic accumulates through wg signaling; arm
CC function in wg signal transduction is required early in development for
CC determination of neuroblast fate. Arm and Abl proteins function
CC cooperatively at adherens junctions in both the CNS and epidermis.
CC {ECO:0000269|PubMed:9635189}.
CC -!- SUBUNIT: Interacts with Mer and Moe at the adherens junction
CC (PubMed:8666669). Interacts with Inx2 (PubMed:15047872). Interacts with
CC alpha-Cat (PubMed:25653389). Interacts with Myo31DF (PubMed:16598259,
CC PubMed:22491943). {ECO:0000269|PubMed:15047872,
CC ECO:0000269|PubMed:16598259, ECO:0000269|PubMed:22491943,
CC ECO:0000269|PubMed:25653389, ECO:0000269|PubMed:8666669}.
CC -!- INTERACTION:
CC P18824; P35220: alpha-Cat; NbExp=3; IntAct=EBI-216128, EBI-126806;
CC P18824; Q9W0N9: ebd1; NbExp=3; IntAct=EBI-216128, EBI-141287;
CC P18824; Q24368: Iswi; NbExp=2; IntAct=EBI-216128, EBI-367628;
CC P18824; Q961D9: lgs; NbExp=5; IntAct=EBI-216128, EBI-85519;
CC P18824; O01368: nej; NbExp=3; IntAct=EBI-216128, EBI-868028;
CC P18824; P91943: pan; NbExp=2; IntAct=EBI-216128, EBI-147301;
CC P18824; O00512: BCL9; Xeno; NbExp=3; IntAct=EBI-216128, EBI-533127;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8666669}. Cell
CC membrane {ECO:0000269|PubMed:8666669}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8666669}; Cytoplasmic side
CC {ECO:0000269|PubMed:8666669}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:16598259, ECO:0000269|PubMed:25653389}. Note=Inner
CC surface of cell membrane and adherens junction.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Cytoplasmic; Synonyms=A, B;
CC IsoId=P18824-1; Sequence=Displayed;
CC Name=Neural; Synonyms=C;
CC IsoId=P18824-2; Sequence=VSP_006738;
CC -!- TISSUE SPECIFICITY: Isoform cytoplasmic accumulates at low levels in
CC axons, at high levels in specific cells along the CNS midline and in
CC leg and eye imaginal disks. Isoform neural accumulates in the axon
CC tracts of the CNS. Both isoforms accumulate in the peripheral nervous
CC system. {ECO:0000269|PubMed:9635189}.
CC -!- DEVELOPMENTAL STAGE: Present at all stages, but reaches the highest
CC levels during early to mid-embryogenesis. Isoform cytoplasmic is the
CC predominant one from the cellular blastoderm stage until germ-band
CC retraction. Isoform neural is first seen after germ band retraction.
CC -!- PTM: Phosphorylated on Ser, Thr and Tyr residues (PubMed:7529201).
CC Level of phosphorylation varies both during embryonic development and
CC from embryonic tissue to tissue (PubMed:7529201). Sgg is required for
CC phosphorylation and wg signal negatively regulates arm phosphorylation
CC (PubMed:7529201). Hypophosphorylated form of arm increases in steady-
CC state levels (PubMed:7529201). Phosphorylated directly or indirectly by
CC CkIalpha which stimulates its degradation (PubMed:11927557).
CC {ECO:0000269|PubMed:11927557, ECO:0000269|PubMed:7529201}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X54468; CAA38350.1; -; Genomic_DNA.
DR EMBL; AF001213; AAB58731.1; -; mRNA.
DR EMBL; AE014298; AAF45686.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF45687.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09064.2; -; Genomic_DNA.
DR EMBL; AE014298; AAS65246.1; -; Genomic_DNA.
DR EMBL; AL021106; CAA15946.1; -; Genomic_DNA.
DR EMBL; AL021086; CAA15946.1; JOINED; Genomic_DNA.
DR EMBL; AL021086; CAA15935.1; -; Genomic_DNA.
DR EMBL; AL021106; CAA15935.1; JOINED; Genomic_DNA.
DR EMBL; AY118525; AAM49894.1; -; mRNA.
DR PIR; T12689; T12689.
DR RefSeq; NP_001259149.1; NM_001272220.1. [P18824-1]
DR RefSeq; NP_476665.2; NM_057317.4. [P18824-1]
DR RefSeq; NP_476666.1; NM_057318.4. [P18824-1]
DR RefSeq; NP_599100.1; NM_134273.2. [P18824-1]
DR RefSeq; NP_726775.2; NM_166912.2. [P18824-2]
DR RefSeq; NP_996328.1; NM_206605.2. [P18824-1]
DR AlphaFoldDB; P18824; -.
DR SMR; P18824; -.
DR BioGRID; 57697; 127.
DR DIP; DIP-19968N; -.
DR IntAct; P18824; 173.
DR MINT; P18824; -.
DR STRING; 7227.FBpp0089035; -.
DR iPTMnet; P18824; -.
DR PaxDb; P18824; -.
DR PRIDE; P18824; -.
DR EnsemblMetazoa; FBtr0089988; FBpp0089031; FBgn0000117. [P18824-1]
DR EnsemblMetazoa; FBtr0089989; FBpp0089032; FBgn0000117. [P18824-1]
DR EnsemblMetazoa; FBtr0089990; FBpp0089033; FBgn0000117. [P18824-2]
DR EnsemblMetazoa; FBtr0089991; FBpp0089034; FBgn0000117. [P18824-1]
DR EnsemblMetazoa; FBtr0089992; FBpp0089035; FBgn0000117. [P18824-1]
DR EnsemblMetazoa; FBtr0332583; FBpp0304835; FBgn0000117. [P18824-1]
DR GeneID; 31151; -.
DR KEGG; dme:Dmel_CG11579; -.
DR CTD; 31151; -.
DR FlyBase; FBgn0000117; arm.
DR VEuPathDB; VectorBase:FBgn0000117; -.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT00940000171121; -.
DR InParanoid; P18824; -.
DR OMA; KNEAHQR; -.
DR PhylomeDB; P18824; -.
DR Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-DME-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-DME-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-DME-209214; Phosphorylation of SMO.
DR Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR Reactome; R-DME-209396; Phosphorylation of ARM.
DR Reactome; R-DME-209407; Transport of ARM to the nucleus.
DR Reactome; R-DME-209413; Assembly of the 'destruction complex'.
DR Reactome; R-DME-209421; Transcription activation by ARM.
DR Reactome; R-DME-209440; Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM.
DR Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
DR Reactome; R-DME-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
DR Reactome; R-DME-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-DME-4086398; Ca2+ pathway.
DR Reactome; R-DME-418990; Adherens junctions interactions.
DR Reactome; R-DME-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DME-525793; Myogenesis.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-DME-8951430; RUNX3 regulates WNT signaling.
DR Reactome; R-DME-8980692; RHOA GTPase cycle.
DR Reactome; R-DME-9013026; RHOB GTPase cycle.
DR Reactome; R-DME-9013106; RHOC GTPase cycle.
DR Reactome; R-DME-9013407; RHOH GTPase cycle.
DR SignaLink; P18824; -.
DR BioGRID-ORCS; 31151; 0 hits in 3 CRISPR screens.
DR ChiTaRS; arm; fly.
DR GenomeRNAi; 31151; -.
DR PRO; PR:P18824; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000117; Expressed in wing disc and 24 other tissues.
DR ExpressionAtlas; P18824; baseline and differential.
DR Genevisible; P18824; DM.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:FlyBase.
DR GO; GO:0016342; C:catenin complex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030139; C:endocytic vesicle; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
DR GO; GO:0005915; C:zonula adherens; IDA:FlyBase.
DR GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IMP:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:FlyBase.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:WormBase.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:FlyBase.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IMP:FlyBase.
DR GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0001709; P:cell fate determination; IMP:FlyBase.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:FlyBase.
DR GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0046667; P:compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0035017; P:cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0060232; P:delamination; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0035153; P:epithelial cell type specification, open tracheal system; IMP:FlyBase.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0060914; P:heart formation; IMP:FlyBase.
DR GO; GO:0048526; P:imaginal disc-derived wing expansion; IMP:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0014019; P:neuroblast development; IMP:FlyBase.
DR GO; GO:0014017; P:neuroblast fate commitment; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0046530; P:photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0071896; P:protein localization to adherens junction; IMP:FlyBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:FlyBase.
DR GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR GO; GO:0045186; P:zonula adherens assembly; IMP:FlyBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR013284; Beta-catenin.
DR PANTHER; PTHR45976; PTHR45976; 1.
DR Pfam; PF00514; Arm; 4.
DR PRINTS; PR01869; BCATNINFAMLY.
DR SMART; SM00185; ARM; 12.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Cytoplasm; Developmental protein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Segmentation polarity protein;
KW Wnt signaling pathway.
FT CHAIN 1..843
FT /note="Armadillo segment polarity protein"
FT /id="PRO_0000064292"
FT REPEAT 159..200
FT /note="ARM 1"
FT REPEAT 201..242
FT /note="ARM 2"
FT REPEAT 243..284
FT /note="ARM 3"
FT REPEAT 285..326
FT /note="ARM 4"
FT REPEAT 327..368
FT /note="ARM 5"
FT REPEAT 369..410
FT /note="ARM 6"
FT REPEAT 411..449
FT /note="ARM 7"
FT REPEAT 450..496
FT /note="ARM 8"
FT REPEAT 497..538
FT /note="ARM 9"
FT REPEAT 539..584
FT /note="ARM 10"
FT REPEAT 585..608
FT /note="ARM 11"
FT REPEAT 609..647
FT /note="ARM 12"
FT REPEAT 648..689
FT /note="ARM 13; truncated"
FT MOD_RES 650
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 718..843
FT /note="LGPEEAYEGLYGQGPPSVHSSHGGRAFHQQGYDTLPIDSMQGLEISSPVGGG
FT GAGGAPGNGGAVGGASGGGGNIGAIPPSGAPTSPYSMDMDVGEIDAGALNFDLDAMPTP
FT PNDNNNLAAWYDTDC -> ILYQ (in isoform Neural)"
FT /evidence="ECO:0000303|PubMed:9635189"
FT /id="VSP_006738"
SQ SEQUENCE 843 AA; 91153 MW; 40DAD6FB83163049 CRC64;
MSYMPAQNRT MSHNNQYNPP DLPPMVSAKE QTLMWQQNSY LGDSGIHSGA VTQVPSLSGK
EDEEMEGDPL MFDLDTGFPQ NFTQDQVDDM NQQLSQTRSQ RVRAAMFPET LEEGIEIPST
QFDPQQPTAV QRLSEPSQML KHAVVNLINY QDDAELATRA IPELIKLLND EDQVVVSQAA
MMVHQLSKKE ASRHAIMNSP QMVAALVRAI SNSNDLESTK AAVGTLHNLS HHRQGLLAIF
KSGGIPALVK LLSSPVESVL FYAITTLHNL LLHQDGSKMA VRLAGGLQKM VTLLQRNNVK
FLAIVTDCLQ ILAYGNQESK LIILASGGPN ELVRIMRSYD YEKLLWTTSR VLKVLSVCSS
NKPAIVDAGG MQALAMHLGN MSPRLVQNCL WTLRNLSDAA TKVEGLEALL QSLVQVLGST
DVNVVTCAAG ILSNLTCNNQ RNKATVCQVG GVDALVRTII NAGDREEITE PAVCALRHLT
SRHVDSELAQ NAVRLNYGLS VIVKLLHPPS RWPLIKAVIG LIRNLALCPA NHAPLREHGA
IHHLVRLLMR AFQDTERQRS SIATTGSQQP SAYADGVRME EIVEGTVGAL HILARESHNR
ALIRQQSVIP IFVRLLFNEI ENIQRVAAGV LCELAADKEG AEIIEQEGAT GPLTDLLHSR
NEGVATYAAA VLFRMSEDKP QDYKKRLSIE LTNSLLREDN NIWANADLGM GPDLQDMLGP
EEAYEGLYGQ GPPSVHSSHG GRAFHQQGYD TLPIDSMQGL EISSPVGGGG AGGAPGNGGA
VGGASGGGGN IGAIPPSGAP TSPYSMDMDV GEIDAGALNF DLDAMPTPPN DNNNLAAWYD
TDC
