DVL1_RAT
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 03-AUG-2022, entry version 173.
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}.
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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; Q9WVB9; -.
DR Ensembl; ENSRNOT00000026439; ENSRNOP00000026439; ENSRNOG00000019423.
DR GeneID; 83721; -.
DR KEGG; rno:83721; -.
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; 474724at2759; -.
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 tissues.
DR Genevisible; Q9WVB9; RN.
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: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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
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: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:0001505; P:regulation of neurotransmitter levels; 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:0006355; P:regulation of transcription, DNA-templated; 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:0016055; P:Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; ISO:RGD.
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; IPR008340; DVL-1.
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:SF5; PTHR10878:SF5; 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 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 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
