DVL2_XENTR
ID DVL2_XENTR Reviewed; 732 AA.
AC Q05AS8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Segment polarity protein dishevelled homolog DVL-2 {ECO:0000250|UniProtKB:P51142};
DE Short=Dishevelled-2 {ECO:0000250|UniProtKB:P51142};
DE AltName: Full=DSH homolog 2;
GN Name=dvl2 {ECO:0000312|EMBL:AAI23949.1};
GN Synonyms=dsh {ECO:0000250|UniProtKB:P51142};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAI23949.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAI23949.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P51142}.
CC -!- SUBUNIT: Can form homomultimers. Interacts with prickle1. Interacts
CC (via the PDZ domain) with ccdc88c/dal and dact1-B/dpr. Interacts (via
CC the DIX domain) with ARP/Axin-related protein and dact1-A/frodo.
CC Interacts with sdc4, possibly via fz7. Interacts directly (via the DEP
CC domain) with efnb1/ephrin-B1. May interact indirectly with the
CC phosphorylated ephrin receptors ephb1 and ephb2 via SH domain-
CC containing adapters (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51142}.
CC Cytoplasmic vesicle {ECO:0000250|UniProtKB:P51142}. Cell projection,
CC cilium {ECO:0000250|UniProtKB:P51142}. Nucleus
CC {ECO:0000250|UniProtKB:P51142}. Cell membrane
CC {ECO:0000250|UniProtKB:P51142}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P51142}. Note=Recruited from the cytoplasm to
CC the cell membrane by frizzled proteins. Also relocated to the cell
CC membrane by sdc4 and ephb1/ephrin-B1. Concentrated at the cell membrane
CC in both ciliated and non-ciliated cells. Enriched at the apical surface
CC of ciliated cells. Localized to the cilium rootlet (By similarity).
CC {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250|UniProtKB:P51142}.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000255}.
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DR EMBL; BC123948; AAI23949.1; -; mRNA.
DR RefSeq; NP_001072660.1; NM_001079192.1.
DR AlphaFoldDB; Q05AS8; -.
DR SMR; Q05AS8; -.
DR PaxDb; Q05AS8; -.
DR DNASU; 780117; -.
DR GeneID; 780117; -.
DR KEGG; xtr:780117; -.
DR CTD; 1856; -.
DR Xenbase; XB-GENE-1017461; dvl2.
DR eggNOG; KOG3571; Eukaryota.
DR InParanoid; Q05AS8; -.
DR OrthoDB; 474724at2759; -.
DR Reactome; R-XTR-201688; WNT mediated activation of DVL.
DR Reactome; R-XTR-4086400; PCP/CE pathway.
DR Reactome; R-XTR-4641258; Degradation of DVL.
DR Reactome; R-XTR-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-XTR-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR Reactome; R-XTR-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-XTR-8856828; Clathrin-mediated endocytosis.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0035253; C:ciliary rootlet; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0046875; F:ephrin receptor binding; ISS:UniProtKB.
DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0045545; F:syndecan binding; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0009948; P:anterior/posterior axis specification; ISS:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0032053; P:ciliary basal body organization; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0060026; P:convergent extension; ISS:UniProtKB.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; ISS:UniProtKB.
DR GO; GO:0009950; P:dorsal/ventral axis specification; ISS:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; ISS:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISS:UniProtKB.
DR GO; GO:0001702; P:gastrulation with mouth forming second; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; ISS: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 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoplasmic vesicle; Developmental protein; Gastrulation;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..732
FT /note="Segment polarity protein dishevelled homolog DVL-2"
FT /id="PRO_0000354665"
FT DOMAIN 1..82
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT DOMAIN 250..335
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 424..498
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 81..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 79277 MW; 2683B15F9FAA5841 CRC64;
MAETKVIYHL DEEETPYLVK VPVPANEIRL RDFKAALGRG HAKYFFKAMD QDFGVVKEEI
SDDNAKLPCF NGRVVSWLVS SETSQTDSAP PAAEVRPDPP PVPPPVPPPP AERTSGIGDS
RPPSFHPNVS GSTEQLDQDN ESVISMRRDR VRRRDSTEQG VARGVNGRAE RHLSGYESSS
TLLTSEIETS ICDSEEDDAM SRFSSSTEQS SASRLLKRHR RRRKQRPPRL ERTSSFSSVT
DSTMSLNIIT VTLNMEKYNF LGISIVGQSN ERGDGGIYIG SIMKGGAVAA DGRIEPGDML
LQVNDINFEN MSNDDAVRVL RDIVHKPGPI ILTVAKCWDP SPQGYFTLPR NEPIQPIDPA
AWVSHSAALS GSFPVYPGSA SMSSMTSSTS VTETELSHAL PPVSLFSLSV HTDLASVAKV
MASPESGLEV RDRMWLKITI PNAFLGSDMV DWLYHHVEGF QDRREARKFA SNLLKAGLIR
HTVNKITFSE QCYYIFGDLT GCENYMANLS LNDNDGSSGA SDQDTLAPLP LPGASPWPLL
PTFSYQYPAP HPYSTQPPAY HELSSYSYGM GSAGSQHSEG SRSSGSNRSD GGRGTQKDER
SGVVGVGGGE SKSGSGSESE YSTRSSIRRI GGGEAGPPSE RSTSSRPPLH HPPSVHSYAA
PGVPLSYNPM MLMMMPPPPL PPPGACPPSS SVPPGAPPLV RDLASVPPEL TASRQSFHMA
MGNPSEFFVD VM
