DVL2_XENLA
ID DVL2_XENLA Reviewed; 736 AA.
AC P51142;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Segment polarity protein dishevelled homolog DVL-2;
DE Short=Dishevelled-2;
DE AltName: Full=DSH homolog 2;
DE AltName: Full=Xdsh;
GN Name=dvl2; Synonyms=dsh;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Oocyte;
RX PubMed=7600981; DOI=10.1242/dev.121.6.1637;
RA Sokol S.Y., Klingensmith J., Perrimon N., Itoh K.;
RT "Dorsalizing and neuralizing properties of Xdsh, a maternally expressed
RT Xenopus homolog of dishevelled.";
RL Development 121:1637-1647(1995).
RN [2]
RP ERRATUM OF PUBMED:7600981.
RX PubMed=7588081; DOI=10.1242/dev.121.10.3487;
RA Sokol S.Y., Klingensmith J., Perrimon N., Itoh K.;
RL Development 121:3487-3487(1995).
RN [3]
RP FUNCTION.
RX PubMed=8939601; DOI=10.1016/s0960-9822(96)00750-6;
RA Sokol S.Y.;
RT "Analysis of Dishevelled signalling pathways during Xenopus development.";
RL Curr. Biol. 6:1456-1467(1996).
RN [4]
RP FUNCTION.
RX PubMed=9076682; DOI=10.1016/s0925-4773(96)00627-2;
RA Itoh K., Sokol S.Y.;
RT "Graded amounts of Xenopus dishevelled specify discrete anteroposterior
RT cell fates in prospective ectoderm.";
RL Mech. Dev. 61:113-125(1997).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10427095; DOI=10.1083/jcb.146.2.427;
RA Miller J.R., Rowning B.A., Larabell C.A., Yang-Snyder J.A., Bates R.L.,
RA Moon R.T.;
RT "Establishment of the dorsal-ventral axis in Xenopus embryos coincides with
RT the dorsal enrichment of dishevelled that is dependent on cortical
RT rotation.";
RL J. Cell Biol. 146:427-437(1999).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10906785;
RX DOI=10.1002/1097-0177(2000)9999:9999<::aid-dvdy1017>3.0.co;2-9;
RA Medina A., Steinbeisser H.;
RT "Interaction of Frizzled 7 and Dishevelled in Xenopus.";
RL Dev. Dyn. 218:671-680(2000).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND DOMAIN.
RX PubMed=10698942; DOI=10.1093/emboj/19.5.1010;
RA Rothbaecher U., Laurent M.N., Deardorff M.A., Klein P.S., Cho K.W.Y.,
RA Fraser S.E.;
RT "Dishevelled phosphorylation, subcellular localization and multimerization
RT regulate its role in early embryogenesis.";
RL EMBO J. 19:1010-1022(2000).
RN [8]
RP FUNCTION, INTERACTION WITH ARP, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=10688669; DOI=10.1128/mcb.20.6.2228-2238.2000;
RA Itoh K., Antipova A., Ratcliffe M.J., Sokol S.Y.;
RT "Interaction of dishevelled and Xenopus axin-related protein is required
RT for wnt signal transduction.";
RL Mol. Cell. Biol. 20:2228-2238(2000).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10811222; DOI=10.1038/35011077;
RA Wallingford J.B., Rowning B.A., Vogeli K.M., Rothbaecher U., Fraser S.E.,
RA Harland R.M.;
RT "Dishevelled controls cell polarity during Xenopus gastrulation.";
RL Nature 405:81-85(2000).
RN [10]
RP FUNCTION.
RX PubMed=11493574; DOI=10.1242/dev.128.13.2581;
RA Wallingford J.B., Harland R.M.;
RT "Xenopus Dishevelled signaling regulates both neural and mesodermal
RT convergent extension: parallel forces elongating the body axis.";
RL Development 128:2581-2592(2001).
RN [11]
RP FUNCTION.
RX PubMed=12421719; DOI=10.1242/dev.00123;
RA Wallingford J.B., Harland R.M.;
RT "Neural tube closure requires Dishevelled-dependent convergent extension of
RT the midline.";
RL Development 129:5815-5825(2002).
RN [12]
RP FUNCTION, AND INTERACTION WITH DACT1-A.
RX PubMed=11941372; DOI=10.1038/ncb784;
RA Gloy J., Hikasa H., Sokol S.Y.;
RT "Frodo interacts with Dishevelled to transduce Wnt signals.";
RL Nat. Cell Biol. 4:351-357(2002).
RN [13]
RP INTERACTION WITH PRICKLE1.
RX PubMed=12699625; DOI=10.1016/s0960-9822(03)00245-8;
RA Takeuchi M., Nakabayashi J., Sakaguchi T., Yamamoto T.S., Takahashi H.,
RA Takeda H., Ueno N.;
RT "The prickle-related gene in vertebrates is essential for gastrulation cell
RT movements.";
RL Curr. Biol. 13:674-679(2003).
RN [14]
RP FUNCTION, INTERACTION WITH EFNB1; EPHB1 AND EPHB2, TISSUE SPECIFICITY, AND
RP TYROSINE PHOSPHORYLATION.
RX PubMed=12574121; DOI=10.1093/emboj/cdg088;
RA Tanaka M., Kamo T., Ota S., Sugimura H.;
RT "Association of Dishevelled with Eph tyrosine kinase receptor and ephrin
RT mediates cell repulsion.";
RL EMBO J. 22:847-858(2003).
RN [15]
RP FUNCTION.
RX PubMed=15548584; DOI=10.1242/dev.01542;
RA Ewald A.J., Peyrot S.M., Tyszka J.M., Fraser S.E., Wallingford J.B.;
RT "Regional requirements for Dishevelled signaling during Xenopus
RT gastrulation: separable effects on blastopore closure, mesendoderm
RT internalization and archenteron formation.";
RL Development 131:6195-6209(2004).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15936275; DOI=10.1016/j.cub.2005.04.062;
RA Park T.J., Gray R.S., Sato A., Habas R., Wallingford J.B.;
RT "Subcellular localization and signaling properties of dishevelled in
RT developing vertebrate embryos.";
RL Curr. Biol. 15:1039-1044(2005).
RN [17]
RP FUNCTION, AND INTERACTION WITH CCDC88C.
RX PubMed=16026968; DOI=10.1016/j.mod.2005.05.003;
RA Kobayashi H., Michiue T., Yukita A., Danno H., Sakurai K., Fukui A.,
RA Kikuchi A., Asashima M.;
RT "Novel Daple-like protein positively regulates both the Wnt/beta-catenin
RT pathway and the Wnt/JNK pathway in Xenopus.";
RL Mech. Dev. 122:1138-1153(2005).
RN [18]
RP FUNCTION.
RX PubMed=15677333; DOI=10.1073/pnas.0409472102;
RA Liu J., Bang A.G., Kintner C., Orth A.P., Chanda S.K., Ding S.,
RA Schultz P.G.;
RT "Identification of the Wnt signaling activator leucine-rich repeat in
RT Flightless interaction protein 2 by a genome-wide functional analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1927-1932(2005).
RN [19]
RP FUNCTION, INTERACTION WITH EFNB1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16362052; DOI=10.1038/ncb1344;
RA Lee H.-S., Bong Y.-S., Moore K.B., Soria K., Moody S.A., Daar I.O.;
RT "Dishevelled mediates ephrinB1 signalling in the eye field through the
RT planar cell polarity pathway.";
RL Nat. Cell Biol. 8:55-63(2006).
RN [20]
RP INTERACTION WITH SDC4, AND SUBCELLULAR LOCATION.
RX PubMed=16604063; DOI=10.1038/ncb1399;
RA Munoz R., Moreno M., Oliva C., Orbenes C., Larrain J.;
RT "Syndecan-4 regulates non-canonical Wnt signalling and is essential for
RT convergent and extension movements in Xenopus embryos.";
RL Nat. Cell Biol. 8:492-500(2006).
RN [21]
RP INTERACTION WITH LRRC6.
RX PubMed=18539122; DOI=10.1016/j.devcel.2008.03.010;
RA Kishimoto N., Cao Y., Park A., Sun Z.;
RT "Cystic kidney gene seahorse regulates cilia-mediated processes and Wnt
RT pathways.";
RL Dev. Cell 14:954-961(2008).
RN [22]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=18552847; DOI=10.1038/ng.104;
RA Park T.J., Mitchell B.J., Abitua P.B., Kintner C., Wallingford J.B.;
RT "Dishevelled controls apical docking and planar polarization of basal
RT bodies in ciliated epithelial cells.";
RL Nat. Genet. 40:871-879(2008).
RN [23]
RP INTERACTION WITH CUSTOS.
RX PubMed=25157132; DOI=10.1073/pnas.1414437111;
RA Komiya Y., Mandrekar N., Sato A., Dawid I.B., Habas R.;
RT "Custos controls beta-catenin to regulate head development during
RT vertebrate embryogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:13099-13104(2014).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 252-340 IN COMPLEX WITH DACT1-B,
RP FUNCTION, INTERACTION WITH DACT1-B, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF 272-GLN--GLU-275 AND ASN-317.
RX PubMed=11970895; DOI=10.1016/s1534-5807(02)00140-5;
RA Cheyette B.N.R., Waxman J.S., Miller J.R., Takemaru K., Sheldahl L.C.,
RA Khlebtsova N., Fox E.P., Earnest T.N., Moon R.T.;
RT "Dapper, a Dishevelled-associated antagonist of beta-catenin and JNK
RT signaling, is required for notochord formation.";
RL Dev. Cell 2:449-461(2002).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 252-340.
RA Friedland N., Hung L.-W., Cheyette B.N.R., Miller J.R., Moon R.T.,
RA Earnest T.N.;
RT "Conformational flexibility in the PDZ domain of Dishevelled induced by
RT target binding.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Involved in at least 2 independent signaling cascades,
CC controlling cell fate via canonical Wnt signaling and cell polarity via
CC a planar cell polarity (PCP) cascade. Acts synergistically with
CC dal/dapple-like to activate Wnt signaling, stabilizing ctnnb1/beta-
CC catenin and leading to dorsal axis formation. Also prevents degradation
CC of ctnnb1/beta-catenin by displacing gsk3 from a complex with ARP/Axin-
CC related protein. Has an additional role in anterior-posterior (A/P)
CC axis formation, specifying different neuroectodermal cell fates along
CC the A/P axis in a dose-dependent manner by activating several early
CC patterning genes. In the PCP pathway, required at the cell membrane for
CC PCP-mediated neural and mesodermal convergent extension during
CC gastrulation and subsequent neural tube closure, acting to activate
CC jnk. Also involved in blastopore closure and archenteron elongation
CC during early, but not late, gastrulation. Associates with ephrin
CC receptors and ligands and acts as part of a downstream PCP pathway to
CC mediate ephrin-mediated cell repulsion via activation of rhoa. Required
CC for efnb1/ephrin-B1-driven movement of non-retinal progenitor cells
CC into the retina during eye field formation. Patterns the hindbrain.
CC Required for ciliogenesis. Controls the docking of basal bodies to the
CC apical plasma membrane; mediates the activation, but not localization
CC of rhoa at the apical surface of ciliated cells during basal body
CC docking. Furthermore, required for the association of basal bodies with
CC membrane-bound vesicles and the vesicle-trafficking protein exoc4/sec8,
CC and this association is in turn required for basal body docking. Once
CC basal bodies are docked, required for the planar polarization of basal
CC bodies that underlies ciliary beating and the directional fluid flow
CC across ciliated epithelia. {ECO:0000269|PubMed:10427095,
CC ECO:0000269|PubMed:10688669, ECO:0000269|PubMed:10811222,
CC ECO:0000269|PubMed:11493574, ECO:0000269|PubMed:11941372,
CC ECO:0000269|PubMed:11970895, ECO:0000269|PubMed:12421719,
CC ECO:0000269|PubMed:12574121, ECO:0000269|PubMed:15548584,
CC ECO:0000269|PubMed:15677333, ECO:0000269|PubMed:15936275,
CC ECO:0000269|PubMed:16026968, ECO:0000269|PubMed:16362052,
CC ECO:0000269|PubMed:18552847, ECO:0000269|PubMed:7600981,
CC ECO:0000269|PubMed:8939601, ECO:0000269|PubMed:9076682}.
CC -!- SUBUNIT: Can form homomultimers. Interacts with prickle1. Interacts
CC (via PDZ domain) with ccdc88c/dal and dact1-B/dpr. Interacts (via DIX
CC domain) with ARP/Axin-related protein and dact1-A/frodo. Interacts with
CC sdc4, possibly via fz7. Interacts directly (via DEP domain) with
CC efnb1/ephrin-B1 and indirectly with the phosphorylated ephrin receptors
CC ephb1 and ephb2, via association with SH domain-containing adapters.
CC May interact with lrrc6. Interacts with custos (via NLS1 and NLS2); the
CC interaction is negatively regulated by Wnt stimulation
CC (PubMed:25157132). {ECO:0000269|PubMed:10688669,
CC ECO:0000269|PubMed:10698942, ECO:0000269|PubMed:11941372,
CC ECO:0000269|PubMed:11970895, ECO:0000269|PubMed:12574121,
CC ECO:0000269|PubMed:12699625, ECO:0000269|PubMed:16026968,
CC ECO:0000269|PubMed:16362052, ECO:0000269|PubMed:16604063,
CC ECO:0000269|PubMed:18539122, ECO:0000269|PubMed:25157132}.
CC -!- INTERACTION:
CC P51142; Q8AXM9: ctnnd1; NbExp=2; IntAct=EBI-6257503, EBI-6260685;
CC P51142; Q8QG92: dact1-b; NbExp=2; IntAct=EBI-6257503, EBI-6257549;
CC P51142; A5J090; NbExp=4; IntAct=EBI-6257503, EBI-7401819;
CC P51142; A0A0U2ULT4; Xeno; NbExp=2; IntAct=EBI-6257503, EBI-20720366;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle. Cell projection,
CC cilium. Nucleus. Cell membrane; Peripheral membrane protein.
CC Note=Phosphorylated and recruited from the cytoplasm to the cell
CC membrane by frizzled proteins. Also relocated to the cell membrane by
CC sdc4 and ephb1/ephrin-B1. Concentrated at cell membrane in both
CC ciliated and non-ciliated cells. Enriched at the apical surface of
CC ciliated cells. Localized to the cilium rootlet.
CC -!- TISSUE SPECIFICITY: Expressed equally in both animal-vegetal and
CC dorsal-ventral directions of the early blastula. Becomes enriched on
CC the dorsal side of the embryo after cortical rotation. Expressed along
CC the anterior margin of eye field of neurulae (stage 16 embryos) and in
CC the anterolateral crescent that borders the eye field. Continues to be
CC expressed in the optic cup at stage 26. Expressed in the central
CC nervous system throughout the early tailbud stage including the entire
CC hindbrain. {ECO:0000269|PubMed:10427095, ECO:0000269|PubMed:12574121,
CC ECO:0000269|PubMed:16362052, ECO:0000269|PubMed:7600981}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Most abundant in eggs and
CC expressed at a low level in blastulae, gastrulae, neurulae and tailbud
CC embryonic stages. {ECO:0000269|PubMed:7600981}.
CC -!- DOMAIN: The C-terminal region containing the DEP domain is required for
CC membrane accumulation and phosphorylation. Wnt signaling and axis
CC induction requires the DIX domain. The C-terminus contributes to the
CC localization at the cilia base. {ECO:0000269|PubMed:10688669,
CC ECO:0000269|PubMed:10698942, ECO:0000269|PubMed:18552847}.
CC -!- PTM: Phosphorylated. Phosphorylation is controlled by frizzled
CC proteins, correlates with the onset of embryo dorsalizing events and is
CC higher in the dorsal half of early cleavage embryos. Phosphorylated on
CC tyrosine residues in response to association with efnb1/ephrin-B1.
CC {ECO:0000269|PubMed:10698942}.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000305}.
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DR EMBL; U31552; AAB00688.1; -; mRNA.
DR PIR; I51691; I51691.
DR RefSeq; NP_001084096.1; NM_001090627.1.
DR PDB; 1L6O; X-ray; 2.20 A; A/B/C=252-340.
DR PDB; 2F0A; X-ray; 1.80 A; A/B/C/D=252-340.
DR PDB; 3FY5; X-ray; 2.40 A; A/B=254-343.
DR PDBsum; 1L6O; -.
DR PDBsum; 2F0A; -.
DR PDBsum; 3FY5; -.
DR AlphaFoldDB; P51142; -.
DR SMR; P51142; -.
DR BioGRID; 100626; 3.
DR ELM; P51142; -.
DR IntAct; P51142; 7.
DR MINT; P51142; -.
DR PRIDE; P51142; -.
DR DNASU; 399301; -.
DR GeneID; 399301; -.
DR KEGG; xla:399301; -.
DR CTD; 399301; -.
DR Xenbase; XB-GENE-1017467; dvl2.L.
DR OrthoDB; 474724at2759; -.
DR EvolutionaryTrace; P51142; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 399301; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0035253; C:ciliary rootlet; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046875; F:ephrin receptor binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0045545; F:syndecan binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:UniProtKB.
DR GO; GO:0032053; P:ciliary basal body organization; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0060026; P:convergent extension; IMP:UniProtKB.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:UniProtKB.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR024580; Dishevelled_C-dom.
DR InterPro; IPR008339; Dishevelled_fam.
DR InterPro; IPR003351; Dishevelled_protein_dom.
DR InterPro; IPR001158; DIX.
DR InterPro; IPR038207; DIX_dom_sf.
DR InterPro; IPR015506; Dsh/Dvl-rel.
DR InterPro; IPR008341; DVL2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10878; PTHR10878; 1.
DR PANTHER; PTHR10878:SF8; PTHR10878:SF8; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF02377; Dishevelled; 1.
DR Pfam; PF00778; DIX; 1.
DR Pfam; PF12316; Dsh_C; 1.
DR Pfam; PF00595; PDZ; 1.
DR PRINTS; PR01760; DISHEVELLED.
DR PRINTS; PR01762; DISHEVELLED2.
DR SMART; SM00021; DAX; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoplasmic vesicle;
KW Developmental protein; Gastrulation; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..736
FT /note="Segment polarity protein dishevelled homolog DVL-2"
FT /id="PRO_0000145748"
FT DOMAIN 1..82
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT DOMAIN 254..326
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 428..502
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 79..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..427
FT /note="Interaction with custos"
FT /evidence="ECO:0000269|PubMed:25157132"
FT REGION 574..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 272..275
FT /note="QSNE->AANA: No effect on interaction with dact1-
FT B/dpr."
FT /evidence="ECO:0000269|PubMed:11970895"
FT MUTAGEN 317
FT /note="N->T: Abolishes interaction with dact1-B/dpr."
FT /evidence="ECO:0000269|PubMed:11970895"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:2F0A"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:2F0A"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:2F0A"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:2F0A"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:2F0A"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:2F0A"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:2F0A"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:2F0A"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:2F0A"
SQ SEQUENCE 736 AA; 79787 MW; AF6C9A1662DD7CEB CRC64;
MAETKVIYHL DEEETPYLVK VPVPATDIRL RDFKAALGRG HAKYFFKAMD QDFGVVKEEI
SDDNAKLPCF NDRVVSWLAS SEGSQPDSAP PAPATEVRPE PPPPVPPPIP PPPAERTSGI
GDSRPPSFHP NVSGSTEQLD QDNESVISMR RDRVRRRESS EQAGVGRGVN GRTERHLSGY
ESSSTLLTSE IETSICDSEE DDTMSRFSSS TEQSSASRLL KRHRRRRKQR PPRLERTSSF
SSVTDSTMSL NIITVTLNME KYNFLGISIV GQSNERGDGG IYIGSIMKGG AVAADGRIEP
GDMLLQVNDI NFENMSNDDA VRVLRDIVHK PGPIVLTVAK CWDPSPQGYF TLPRNEPIHP
IDPAAWVSHS AALSGSFPVY PGSASMSSMT SSTSVTETEL SHALPPVSLF SLSVHTDLAS
VVKVMASPES GLEVRDRMWL KITIPNAFLG SDVVDWLYHH VEGFQDRREA RKFASNLLKA
GFIRHTVNKI TFSEQCYYIF GDLTGCENYM TNLSLNDNDG SSGASDQDTL APLPLPGASP
WPLLPTFSYQ YQAPHPYSTQ PPAYHELSSY SYGMGSAGSQ HSEGSRSSGS NRSDGGRGMQ
KDDRSGVAGV GGGDSKSGSG SESEYSTRSS IRRVGGGEAG PPSERSTSSR LPPHHPPSVH
SYAAPGVPLS YNPMMLMMMP PPPLPPPGVC PPNSSVPPGA PPLVRDLASV PPELTATRQS
FHMAMGNPSE FFVDVM
