DVL1_HUMAN
ID DVL1_HUMAN Reviewed; 695 AA.
AC O14640; Q5TA33; Q5TA35;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Segment polarity protein dishevelled homolog DVL-1;
DE Short=Dishevelled-1;
DE AltName: Full=DSH homolog 1;
GN Name=DVL1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9192851; DOI=10.1006/geno.1997.4713;
RA Semenov M.V., Snyder M.;
RT "Human dishevelled genes constitute a DHR-containing multigene family.";
RL Genomics 42:302-310(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP INTERACTION WITH ARRB1.
RX PubMed=11742073; DOI=10.1073/pnas.211572798;
RA Chen W., Hu L.A., Semenov M.V., Yanagawa S., Kikuchi A., Lefkowitz R.J.,
RA Miller W.E.;
RT "beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity
RT through interaction with phosphorylated dishevelled proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14889-14894(2001).
RN [4]
RP INTERACTION WITH CCDC88C.
RX PubMed=14750955; DOI=10.1111/j.1365-2443.2003.00692.x;
RA Oshita A., Kishida S., Kobayashi H., Michiue T., Asahara T., Asashima M.,
RA Kikuchi A.;
RT "Identification and characterization of a novel Dvl-binding protein that
RT suppresses Wnt signalling pathway.";
RL Genes Cells 8:1005-1017(2003).
RN [5]
RP INTERACTION WITH RYK.
RX PubMed=15454084; DOI=10.1016/j.cell.2004.09.019;
RA Lu W., Yamamoto V., Ortega B., Baltimore D.;
RT "Mammalian Ryk is a Wnt coreceptor required for stimulation of neurite
RT outgrowth.";
RL Cell 119:97-108(2004).
RN [6]
RP INTERACTION WITH INVS.
RX PubMed=15852005; DOI=10.1038/ng1552;
RA Simons M., Gloy J., Ganner A., Bullerkotte A., Bashkurov M., Kroenig C.,
RA Schermer B., Benzing T., Cabello O.A., Jenny A., Mlodzik M., Polok B.,
RA Driever W., Obara T., Walz G.;
RT "Inversin, the gene product mutated in nephronophthisis type II, functions
RT as a molecular switch between Wnt signaling pathways.";
RL Nat. Genet. 37:537-543(2005).
RN [7]
RP INTERACTION WITH TMEM88.
RX PubMed=21044957; DOI=10.1074/jbc.m110.193383;
RA Lee H.J., Finkelstein D., Li X., Wu D., Shi D.L., Zheng J.J.;
RT "Identification of transmembrane protein 88 (TMEM88) as a dishevelled-
RT binding protein.";
RL J. Biol. Chem. 285:41549-41556(2010).
RN [8]
RP INTERACTION WITH DCDC2.
RX PubMed=25557784; DOI=10.1016/j.ajhg.2014.12.002;
RA Schueler M., Braun D.A., Chandrasekar G., Gee H.Y., Klasson T.D.,
RA Halbritter J., Bieder A., Porath J.D., Airik R., Zhou W., LoTurco J.J.,
RA Che A., Otto E.A., Boeckenhauer D., Sebire N.J., Honzik T., Harris P.C.,
RA Koon S.J., Gunay-Aygun M., Saunier S., Zerres K., Bruechle N.O.,
RA Drenth J.P., Pelletier L., Tapia-Paez I., Lifton R.P., Giles R.H., Kere J.,
RA Hildebrandt F.;
RT "DCDC2 mutations cause a renal-hepatic ciliopathy by disrupting Wnt
RT signaling.";
RL Am. J. Hum. Genet. 96:81-92(2015).
RN [9]
RP INVOLVEMENT IN DRS2.
RX PubMed=25817016; DOI=10.1016/j.ajhg.2015.02.015;
RG Baylor-Hopkins Center for Mendelian Genomics;
RA White J., Mazzeu J.F., Hoischen A., Jhangiani S.N., Gambin T., Alcino M.C.,
RA Penney S., Saraiva J.M., Hove H., Skovby F., Kayserili H., Estrella E.,
RA Vulto-van Silfhout A.T., Steehouwer M., Muzny D.M., Sutton V.R.,
RA Gibbs R.A., Lupski J.R., Brunner H.G., van Bon B.W., Carvalho C.M.;
RT "DVL1 frameshift mutations clustering in the penultimate exon cause
RT autosomal-dominant Robinow syndrome.";
RL Am. J. Hum. Genet. 96:612-622(2015).
RN [10]
RP INVOLVEMENT IN DRS2.
RX PubMed=25817014; DOI=10.1016/j.ajhg.2015.02.010;
RA Bunn K.J., Daniel P., Roesken H.S., O'Neill A.C., Cameron-Christie S.R.,
RA Morgan T., Brunner H.G., Lai A., Kunst H.P., Markie D.M., Robertson S.P.;
RT "Mutations in DVL1 cause an osteosclerotic form of Robinow syndrome.";
RL Am. J. Hum. Genet. 96:623-630(2015).
RN [11]
RP INTERACTION WITH FOXK2.
RX PubMed=25805136; DOI=10.1016/j.devcel.2015.01.031;
RA Wang W., Li X., Lee M., Jun S., Aziz K.E., Feng L., Tran M.K., Li N.,
RA McCrea P.D., Park J.I., Chen J.;
RT "FOXKs promote Wnt/beta-catenin signaling by translocating DVL into the
RT nucleus.";
RL Dev. Cell 32:707-718(2015).
RN [12]
RP INTERACTION WITH CCDC88C.
RX PubMed=26126266; DOI=10.7554/elife.07091;
RA Aznar N., Midde K.K., Dunkel Y., Lopez-Sanchez I., Pavlova Y., Marivin A.,
RA Barbazan J., Murray F., Nitsche U., Janssen K.P., Willert K., Goel A.,
RA Abal M., Garcia-Marcos M., Ghosh P.;
RT "Daple is a novel non-receptor GEF required for trimeric G protein
RT activation in Wnt signaling.";
RL Elife 4:E07091-E07091(2015).
RN [13]
RP INTERACTION WITH PKD1.
RX PubMed=27214281; DOI=10.1038/ncb3363;
RA Kim S., Nie H., Nesin V., Tran U., Outeda P., Bai C.X., Keeling J.,
RA Maskey D., Watnick T., Wessely O., Tsiokas L.;
RT "The polycystin complex mediates Wnt/Ca(2+) signalling.";
RL Nat. Cell Biol. 18:752-764(2016).
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).
CC -!- SUBUNIT: Interacts with CXXC4. Interacts (via PDZ domain) with NXN (By
CC similarity). Interacts with BRD7 and INVS. Interacts (via PDZ domain)
CC with VANGL1 and VANGL2 (via C-terminus). Interacts with ARRB1; the
CC interaction is enhanced by phosphorylation of DVL1. Interacts with CYLD
CC (By similarity). Interacts (via PDZ domain) with RYK. Self-associates
CC (via DIX domain) and forms higher homooligomers. Interacts (via PDZ
CC domain) with DACT1 and FZD7, where DACT1 and FZD7 compete for the same
CC binding site (By similarity). Interacts (via DEP domain) with MUSK; the
CC interaction is direct and mediates the formation a DVL1, MUSK and PAK1
CC ternary complex involved in AChR clustering (By similarity). Interacts
CC (via PDZ domain) with TMEM88. Interacts with DCDC2. Interacts with
CC FOXK2 (PubMed:25805136). Interacts with PKD1 (via extracellular domain)
CC (PubMed:27214281). Interacts (via PDZ domain) with CCDC88C/DAPLE;
CC competes with CCDC88C for binding to frizzled receptor FZD7 and
CC dissociates from CCDC88C following initiation of non-canonical Wnt
CC signaling when CCDC88C displaces DVL1 from ligand-activated FZD7
CC (PubMed:26126266, PubMed:14750955). {ECO:0000250|UniProtKB:P51141,
CC ECO:0000250|UniProtKB:Q9WVB9, ECO:0000269|PubMed:11742073,
CC ECO:0000269|PubMed:14750955, ECO:0000269|PubMed:15454084,
CC ECO:0000269|PubMed:15852005, ECO:0000269|PubMed:21044957,
CC ECO:0000269|PubMed:25557784, ECO:0000269|PubMed:25805136,
CC ECO:0000269|PubMed:26126266, ECO:0000269|PubMed:27214281}.
CC -!- INTERACTION:
CC O14640; P25054: APC; NbExp=6; IntAct=EBI-723489, EBI-727707;
CC O14640; P49674: CSNK1E; NbExp=6; IntAct=EBI-723489, EBI-749343;
CC O14640; O14640: DVL1; NbExp=2; IntAct=EBI-723489, EBI-723489;
CC O14640; Q92997: DVL3; NbExp=5; IntAct=EBI-723489, EBI-739789;
CC O14640; Q6P3W7: SCYL2; NbExp=4; IntAct=EBI-723489, EBI-1046810;
CC O14640; Q96EB6: SIRT1; NbExp=2; IntAct=EBI-723489, EBI-1802965;
CC O14640; Q14186: TFDP1; NbExp=3; IntAct=EBI-723489, EBI-749713;
CC O14640; Q9GZV5: WWTR1; NbExp=2; IntAct=EBI-723489, EBI-747743;
CC O14640; O70239: Axin1; Xeno; NbExp=12; IntAct=EBI-723489, EBI-6857773;
CC O14640; Q9EQC9: Cxxc4; Xeno; NbExp=5; IntAct=EBI-723489, EBI-9344960;
CC O14640-2; Q5S007: LRRK2; NbExp=7; IntAct=EBI-6504027, EBI-5323863;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14640-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14640-2; Sequence=VSP_024460;
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 -!- DISEASE: Robinow syndrome, autosomal dominant 2 (DRS2) [MIM:616331]: A
CC rare skeletal dysplasia syndrome characterized by dysmorphic features
CC resembling a fetal face, mesomelic limb shortening, hypoplastic
CC external genitalia in males, costovertebral segmentation defects, and
CC renal anomalies. {ECO:0000269|PubMed:25817014,
CC ECO:0000269|PubMed:25817016}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DVL1ID463ch1p36.html";
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DR EMBL; AF006011; AAB65242.1; -; mRNA.
DR EMBL; AL139287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS22.1; -. [O14640-2]
DR CCDS; CCDS81252.1; -. [O14640-1]
DR RefSeq; NP_001317240.1; NM_001330311.1. [O14640-1]
DR RefSeq; NP_004412.2; NM_004421.2. [O14640-2]
DR PDB; 6LCA; X-ray; 2.40 A; A/B/C/D/E/F/G/H=246-340.
DR PDB; 6LCB; X-ray; 1.40 A; A=246-340.
DR PDB; 6TTK; X-ray; 2.38 A; E/F/G/H=650-664.
DR PDBsum; 6LCA; -.
DR PDBsum; 6LCB; -.
DR PDBsum; 6TTK; -.
DR AlphaFoldDB; O14640; -.
DR SMR; O14640; -.
DR BioGRID; 108188; 101.
DR CORUM; O14640; -.
DR DIP; DIP-40773N; -.
DR IntAct; O14640; 48.
DR MINT; O14640; -.
DR STRING; 9606.ENSP00000368169; -.
DR BindingDB; O14640; -.
DR ChEMBL; CHEMBL6027; -.
DR iPTMnet; O14640; -.
DR PhosphoSitePlus; O14640; -.
DR BioMuta; DVL1; -.
DR EPD; O14640; -.
DR jPOST; O14640; -.
DR MassIVE; O14640; -.
DR MaxQB; O14640; -.
DR PaxDb; O14640; -.
DR PeptideAtlas; O14640; -.
DR PRIDE; O14640; -.
DR ProteomicsDB; 48138; -. [O14640-1]
DR ProteomicsDB; 48139; -. [O14640-2]
DR Antibodypedia; 26291; 258 antibodies from 32 providers.
DR DNASU; 1855; -.
DR Ensembl; ENST00000378888.10; ENSP00000368166.5; ENSG00000107404.21. [O14640-1]
DR Ensembl; ENST00000378891.9; ENSP00000368169.5; ENSG00000107404.21. [O14640-2]
DR GeneID; 1855; -.
DR KEGG; hsa:1855; -.
DR MANE-Select; ENST00000378888.10; ENSP00000368166.5; NM_001330311.2; NP_001317240.1.
DR UCSC; uc001aer.5; human. [O14640-1]
DR CTD; 1855; -.
DR DisGeNET; 1855; -.
DR GeneCards; DVL1; -.
DR GeneReviews; DVL1; -.
DR HGNC; HGNC:3084; DVL1.
DR HPA; ENSG00000107404; Tissue enhanced (skeletal).
DR MalaCards; DVL1; -.
DR MIM; 601365; gene.
DR MIM; 616331; phenotype.
DR neXtProt; NX_O14640; -.
DR OpenTargets; ENSG00000107404; -.
DR Orphanet; 3107; Autosomal dominant Robinow syndrome.
DR PharmGKB; PA27540; -.
DR VEuPathDB; HostDB:ENSG00000107404; -.
DR eggNOG; KOG3571; Eukaryota.
DR GeneTree; ENSGT00950000182903; -.
DR HOGENOM; CLU_012601_1_0_1; -.
DR InParanoid; O14640; -.
DR OMA; SRTNGHP; -.
DR OrthoDB; 474724at2759; -.
DR PhylomeDB; O14640; -.
DR TreeFam; TF318198; -.
DR PathwayCommons; O14640; -.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-201688; WNT mediated activation of DVL.
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5368598; Negative regulation of TCF-dependent signaling by DVL-interacting proteins.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-9673324; WNT5:FZD7-mediated leishmania damping.
DR SignaLink; O14640; -.
DR SIGNOR; O14640; -.
DR BioGRID-ORCS; 1855; 14 hits in 1076 CRISPR screens.
DR ChiTaRS; DVL1; human.
DR GeneWiki; DVL1; -.
DR GenomeRNAi; 1855; -.
DR Pharos; O14640; Tchem.
DR PRO; PR:O14640; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O14640; protein.
DR Bgee; ENSG00000107404; Expressed in hindlimb stylopod muscle and 207 other tissues.
DR ExpressionAtlas; O14640; baseline and differential.
DR Genevisible; O14640; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; ISS:BHF-UCL.
DR GO; GO:1990909; C:Wnt signalosome; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0005109; F:frizzled binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
DR GO; GO:0022007; P:convergent extension involved in neural plate elongation; IEA:Ensembl.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:Ensembl.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0021915; P:neural tube development; IEP:BHF-UCL.
DR GO; GO:0007528; P:neuromuscular junction development; ISS:BHF-UCL.
DR GO; GO:0007269; P:neurotransmitter secretion; ISS:BHF-UCL.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; TAS:ARUK-UCL.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IBA:GO_Central.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0150012; P:positive regulation of neuron projection arborization; ISS:ARUK-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:BHF-UCL.
DR GO; GO:1905386; P:positive regulation of protein localization to presynapse; TAS:ParkinsonsUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
DR GO; GO:0099054; P:presynapse assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:0035372; P:protein localization to microtubule; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043113; P:receptor clustering; ISS:BHF-UCL.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; ISS:BHF-UCL.
DR GO; GO:0032880; P:regulation of protein localization; IDA:ParkinsonsUK-UCL.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; IEA:Ensembl.
DR GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR GO; GO:0050808; P:synapse organization; ISS:BHF-UCL.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IDA:BHF-UCL.
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 3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Developmental protein; Dwarfism; Membrane;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..695
FT /note="Segment polarity protein dishevelled homolog DVL-1"
FT /id="PRO_0000145742"
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..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..667
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 177..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..229
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVB9"
FT VAR_SEQ 378..403
FT /note="GTSPCSSAVTRTSSSSLTSSVPGAPQ -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9192851"
FT /id="VSP_024460"
FT CONFLICT 2
FT /note="A -> G (in Ref. 1; AAB65242)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="A -> P (in Ref. 1; AAB65242)"
FT /evidence="ECO:0000305"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:6LCB"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:6LCB"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:6LCB"
FT HELIX 288..292
FT /evidence="ECO:0007829|PDB:6LCB"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:6LCB"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:6LCB"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:6LCB"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:6LCB"
SQ SEQUENCE 695 AA; 75187 MW; B009BDBCC57BD562 CRC64;
MAETKIIYHM DEEETPYLVK LPVAPERVTL ADFKNVLSNR PVHAYKFFFK SMDQDFGVVK
EEIFDDNAKL PCFNGRVVSW LVLAEGAHSD AGSQGTDSHT DLPPPLERTG GIGDSRPPSF
HPNVASSRDG MDNETGTESM VSHRRERARR RNREEAARTN GHPRGDRRRD VGLPPDSAST
ALSSELESSS FVDSDEDGST SRLSSSTEQS TSSRLIRKHK RRRRKQRLRQ ADRASSFSSI
TDSTMSLNIV TVTLNMERHH FLGISIVGQS NDRGDGGIYI GSIMKGGAVA ADGRIEPGDM
LLQVNDVNFE NMSNDDAVRV LREIVSQTGP ISLTVAKCWD PTPRSYFTVP RADPVRPIDP
AAWLSHTAAL TGALPRYGTS PCSSAVTRTS SSSLTSSVPG APQLEEAPLT VKSDMSAVVR
VMQLPDSGLE IRDRMWLKIT IANAVIGADV VDWLYTHVEG FKERREARKY ASSLLKHGFL
RHTVNKITFS EQCYYVFGDL CSNLATLNLN SGSSGTSDQD TLAPLPHPAA PWPLGQGYPY
QYPGPPPCFP PAYQDPGFSY GSGSTGSQQS EGSKSSGSTR SSRRAPGREK ERRAAGAGGS
GSESDHTAPS GVGSSWRERP AGQLSRGSSP RSQASATAPG LPPPHPTTKA YTVVGGPPGG
PPVRELAAVP PELTGSRQSF QKAMGNPCEF FVDIM
