ID DVL1_RAT Reviewed; 695 AA. AC Q9WVB9; Q9QUG5; Q9WVB8; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 3. DT 27-MAR-2024, entry version 181. DE RecName: Full=Segment polarity protein dishevelled homolog DVL-1; DE Short=Dishevelled-1; DE AltName: Full=DSH homolog 1; GN Name=Dvl1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=Wistar Kyoto; RX PubMed=11354832; DOI=10.1007/s100480000099; RA de Lange R.P.J., Burr K., Clark J.S., Negrin C.D., Brosnan M.J., RA St Clair D.M., Dominiczak A.F., Shaw D.J.; RT "Mapping and sequencing rat dishevelled-1: a candidate gene for cerebral RT ischaemic insult in a rat model of stroke."; RL Neurogenetics 3:99-106(2001). RN [2] RP INTERACTION WITH CXXC4. RX PubMed=11113207; DOI=10.1128/mcb.21.1.330-342.2001; RA Hino S., Kishida S., Michiue T., Fukui A., Sakamoto I., Takada S., RA Asashima M., Kikuchi A.; RT "Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding RT protein."; RL Mol. Cell. Biol. 21:330-342(2001). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Participates in Wnt signaling by binding to the cytoplasmic CC C-terminus of frizzled family members and transducing the Wnt signal to CC down-stream effectors. Plays a role both in canonical and non-canonical CC Wnt signaling. Plays a role in the signal transduction pathways CC mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 CC and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK CC which is important for MUSK-dependent regulation of AChR clustering CC during the formation of the neuromuscular junction (NMJ) (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with BRD7 and INVS. Interacts (via PDZ domain) with CC the VANGL1 and VANGL2 (via C-terminus). Interacts (via PDZ domain) with CC NXN. Interacts with CXXC4. Interacts with ARRB1; the interaction is CC enhanced by phosphorylation of DVL1. Interacts with CYLD. Interacts CC (via PDZ domain) with RYK. Self-associates (via DIX domain) and forms CC higher homooligomers. Interacts (via PDZ domain) with DACT1 and FZD7, CC where DACT1 and FZD7 compete for the same binding site. Interacts (via CC DEP domain) with MUSK; the interaction is direct and mediates the CC formation a DVL1, MUSK and PAK1 ternary complex involved in AChR CC clustering. Interacts (via PDZ domain) with TMEM88 (By similarity). CC Interacts with DCDC2. Interacts with FOXK2 (By similarity). Interacts CC with PKD1 (via extracellular domain) (By similarity). Interacts (via CC PDZ domain) with CCDC88C/DAPLE; competes with CCDC88C for binding to CC frizzled receptor FZD7 and dissociates from CCDC88C following CC initiation of non-canonical Wnt signaling when CCDC88C displaces DVL1 CC from ligand-activated FZD7 (By similarity). CC {ECO:0000250|UniProtKB:O14640, ECO:0000250|UniProtKB:P51141}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, CC cytosol {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. CC Note=Localizes at the cell membrane upon interaction with frizzled CC family members. {ECO:0000250}. CC -!- DOMAIN: The DIX domain promotes homooligomerization. {ECO:0000250}. CC -!- DOMAIN: The DEP domain mediates interaction with the cell membrane. CC {ECO:0000250}. CC -!- PTM: Ubiquitinated; undergoes both 'Lys-48'-linked ubiquitination, CC leading to its subsequent degradation by the ubiquitin-proteasome CC pathway, and 'Lys-63'-linked ubiquitination. The interaction with INVS CC is required for ubiquitination. Deubiquitinated by CYLD, which acts on CC 'Lys-63'-linked ubiquitin chains (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DSH 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; AF143545; AAD33896.2; -; mRNA. DR EMBL; AF143546; AAD33897.2; -; mRNA. DR EMBL; AF143548; AAD41492.2; -; Genomic_DNA. DR EMBL; AF143547; AAD41492.2; JOINED; Genomic_DNA. DR EMBL; AF143550; AAD41493.1; -; Genomic_DNA. DR EMBL; AF143549; AAD41493.1; JOINED; Genomic_DNA. DR RefSeq; NP_114008.1; NM_031820.1. DR AlphaFoldDB; Q9WVB9; -. DR SMR; Q9WVB9; -. DR BioGRID; 249815; 5. DR IntAct; Q9WVB9; 1. DR STRING; 10116.ENSRNOP00000026439; -. DR iPTMnet; Q9WVB9; -. DR PhosphoSitePlus; Q9WVB9; -. DR PaxDb; 10116-ENSRNOP00000026439; -. DR Ensembl; ENSRNOT00000026439.6; ENSRNOP00000026439.5; ENSRNOG00000019423.6. DR Ensembl; ENSRNOT00055023623; ENSRNOP00055019229; ENSRNOG00055013741. DR Ensembl; ENSRNOT00060007603; ENSRNOP00060005705; ENSRNOG00060004547. DR Ensembl; ENSRNOT00065016476; ENSRNOP00065012521; ENSRNOG00065010223. DR GeneID; 83721; -. DR KEGG; rno:83721; -. DR AGR; RGD:620632; -. DR CTD; 1855; -. DR RGD; 620632; Dvl1. DR eggNOG; KOG3571; Eukaryota. DR GeneTree; ENSGT00950000182903; -. DR HOGENOM; CLU_012601_1_0_1; -. DR InParanoid; Q9WVB9; -. DR OMA; SRTNGHP; -. DR OrthoDB; 2910598at2759; -. DR PhylomeDB; Q9WVB9; -. DR TreeFam; TF318198; -. DR Reactome; R-RNO-201688; WNT mediated activation of DVL. DR Reactome; R-RNO-4086400; PCP/CE pathway. DR Reactome; R-RNO-4641258; Degradation of DVL. DR Reactome; R-RNO-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane. DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins. DR PRO; PR:Q9WVB9; -. DR Proteomes; UP000002494; Chromosome 5. DR Bgee; ENSRNOG00000019423; Expressed in skeletal muscle tissue and 20 other cell types or tissues. DR GO; GO:0030424; C:axon; IDA:RGD. DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0030425; C:dendrite; IDA:RGD. DR GO; GO:0043197; C:dendritic spine; IDA:ParkinsonsUK-UCL. DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD. DR GO; GO:0030426; C:growth cone; IDA:RGD. DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI. DR GO; GO:0043005; C:neuron projection; ISO:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0098992; C:neuronal dense core vesicle; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IDA:ParkinsonsUK-UCL. DR GO; GO:0098793; C:presynapse; ISO:RGD. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD. DR GO; GO:0045202; C:synapse; ISO:RGD. DR GO; GO:1990909; C:Wnt signalosome; ISO:RGD. DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD. DR GO; GO:0019899; F:enzyme binding; ISO:RGD. DR GO; GO:0005109; F:frizzled binding; ISO:RGD. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0019901; F:protein kinase binding; IPI:RGD. DR GO; GO:0031267; F:small GTPase binding; IPI:RGD. DR GO; GO:0048675; P:axon extension; ISO:RGD. DR GO; GO:0007411; P:axon guidance; ISO:RGD. DR GO; GO:0007409; P:axonogenesis; ISO:RGD. DR GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD. DR GO; GO:0090103; P:cochlea morphogenesis; ISO:RGD. DR GO; GO:0048668; P:collateral sprouting; ISO:RGD. DR GO; GO:0022007; P:convergent extension involved in neural plate elongation; ISO:RGD. DR GO; GO:0060029; P:convergent extension involved in organogenesis; ISO:RGD. DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:RGD. DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD. DR GO; GO:0060997; P:dendritic spine morphogenesis; IGI:ParkinsonsUK-UCL. DR GO; GO:0001947; P:heart looping; ISO:RGD. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD. DR GO; GO:0021915; P:neural tube development; ISO:RGD. DR GO; GO:0007528; P:neuromuscular junction development; ISO:RGD. DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD. DR GO; GO:0003151; P:outflow tract morphogenesis; ISO:RGD. DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; ISO:RGD. DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IGI:ParkinsonsUK-UCL. DR GO; GO:0150012; P:positive regulation of neuron projection arborization; IGI:ARUK-UCL. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0099173; P:postsynapse organization; ISO:RGD. DR GO; GO:0060134; P:prepulse inhibition; ISO:RGD. DR GO; GO:0099054; P:presynapse assembly; ISO:RGD. DR GO; GO:0035372; P:protein localization to microtubule; ISO:RGD. DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD. DR GO; GO:0050821; P:protein stabilization; ISO:RGD. DR GO; GO:0043113; P:receptor clustering; ISO:RGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:RGD. DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD. DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD. DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD. DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISO:RGD. DR GO; GO:0035176; P:social behavior; ISO:RGD. DR GO; GO:0050808; P:synapse organization; ISO:RGD. DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:RGD. DR GO; GO:0016055; P:Wnt signaling pathway; IGI:ParkinsonsUK-UCL. DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; ISO:RGD. DR CDD; cd04438; DEP_dishevelled; 1. DR CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 2.40.240.130; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; 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; SEGMENT POLARITY PROTEIN DISHEVELLED; 1. DR PANTHER; PTHR10878:SF5; SEGMENT POLARITY PROTEIN DISHEVELLED HOMOLOG DVL-1-RELATED; 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; PR01761; DISHEVELLED1. DR SMART; SM00021; DAX; 1. DR SMART; SM00049; DEP; 1. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50186; DEP; 1. DR PROSITE; PS50841; DIX; 1. DR PROSITE; PS50106; PDZ; 1. DR Genevisible; Q9WVB9; RN. PE 1: Evidence at protein level; KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Developmental protein; KW Membrane; Phosphoprotein; Reference proteome; Ubl conjugation; KW Wnt signaling pathway. FT CHAIN 1..695 FT /note="Segment polarity protein dishevelled homolog DVL-1" FT /id="PRO_0000145745" FT DOMAIN 1..85 FT /note="DIX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069" FT DOMAIN 251..323 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 425..499 FT /note="DEP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066" FT REGION 89..236 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 551..641 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 120..137 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 138..173 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 560..582 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 599..635 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 194 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" SQ SEQUENCE 695 AA; 75447 MW; EEC4AA99A117D22A CRC64; MAETKIIYHM DEEETPYLVK LPVAPERVTL ADFKNVLSNR PVHAYKFFFK SMDQDFGVVK EEIFDDNAKL PCFNGRVVSW LVLAEGAHSD AGSQGTDSHT DLPPPLERTG GIGDSRPPSF HPNVASSRDG MDNETGTESM VSHRRERARR RNRDEAARTN GHPRGDRRRE LGLPPDSAST VLSSELESSS FIDSDEEDNT SRLSSSTEQS TSSRLIRKHK CRRRKQRLRQ TDRASSFSSI TDSTMSLNII TVTLNMERHH FLGISIVGQS NDRGDGGIYI GSIMKGGAVA ADGRIEPGDM LLQVNDVNFE NMSNDDAVRV LREIVSQTGP ISLTVAKCWD PTPRSYFTIP RADPVRPIDP AAWLSHTAAL TGALPRYGTS PCSSAITRTS SSSLTSSVPG APQLEEAPLT VKSDMSAIVR VMQLPDSGLE IRDRMWLKIT IANAVIGADV VDWLYTHVEG FKERREARKY ASSMLKHGFL RHTVNKITFS EQCYYVFGDL CSNLASLNLN SGSSGASDQD TLAPLPHPSV PWPLGQGYPY QYPGPPPCFP PAYQDPGFSY GSGSAGSQQS EGSKSSGSTR SSHRTPGREE RRATGAGGSG SESDHTVPSG SGSTGWWERP VSQLSRGSSP RSQASAVAPG LPPLHPLTKA YAVVGGPPGG PPVRELAAVP PELTGSRQSF QKAMGNPCEF FVDIM //