DVL1_PANTR
ID DVL1_PANTR Reviewed; 670 AA.
AC Q5IS48;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Segment polarity protein dishevelled homolog DVL-1;
DE Short=Dishevelled-1;
DE AltName: Full=DSH homolog 1;
GN Name=DVL1;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
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 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 (By similarity). Interacts with PKD1 (via extracellular domain)
CC (By similarity). 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 (By
CC similarity). {ECO:0000250|UniProtKB:O14640,
CC ECO:0000250|UniProtKB:P51141, ECO:0000250|UniProtKB:Q9WVB9}.
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; AY665280; AAV74318.1; -; mRNA.
DR RefSeq; NP_001012432.1; NM_001012430.1.
DR AlphaFoldDB; Q5IS48; -.
DR SMR; Q5IS48; -.
DR STRING; 9598.ENSPTRP00000055553; -.
DR PaxDb; Q5IS48; -.
DR PRIDE; Q5IS48; -.
DR GeneID; 457191; -.
DR KEGG; ptr:457191; -.
DR CTD; 1855; -.
DR eggNOG; KOG3571; Eukaryota.
DR InParanoid; Q5IS48; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Developmental protein;
KW Membrane; Phosphoprotein; Reference proteome; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..670
FT /note="Segment polarity protein dishevelled homolog DVL-1"
FT /id="PRO_0000145744"
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 400..474
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 518..642
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 533..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVB9"
SQ SEQUENCE 670 AA; 72851 MW; DA314641C8453F07 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 TGALPRYELE EAPLTVKSDM SAVVRVMQLP DSGLEIRDRM WLKITIANAV
IGADVVDWLY THVEGFKERR EARKYASSLL KHGFLRHTVN KITFSEQCYY VFGDLCSNLA
TLNLNSGSSG ASDQDTLAPL PHPAAPWPLG QGYPYQYPGP PPCFPPAYQD PGFSYGSGST
GSQQSEGSKS SGSTRSSRRA PGREKERRAA GAGGSGSESD HTAPSGVGSS WRERPAGQLS
RGSSPRSQAS ATAPGLPPPH PTTKAYTVVG GPPGGPPVRE LAAVPPELTG SRQSFQKAMG
NPCEFFVDIM
