DVL3_XENLA
ID DVL3_XENLA Reviewed; 717 AA.
AC Q6DKE2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Segment polarity protein dishevelled homolog DVL-3 {ECO:0000250|UniProtKB:Q92997};
DE Short=Dishevelled-3 {ECO:0000250|UniProtKB:Q92997};
DE AltName: Full=DSH homolog 3;
GN Name=dvl3 {ECO:0000250|UniProtKB:Q92997};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH74187.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH74187.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18552847; DOI=10.1038/ng.104;
RA Park T.J., Mitchell B.J., Abitua P.B., Kintner C., Wallingford J.B.;
RT "Dishevelled controls apical docking and planar polarization of basal
RT bodies in ciliated epithelial cells.";
RL Nat. Genet. 40:871-879(2008).
CC -!- FUNCTION: Involved in the signal transduction pathway mediated by
CC multiple Wnt genes (By similarity). Required during ciliogenesis for
CC the docking of basal bodies to the apical plasma membrane.
CC {ECO:0000250|UniProtKB:Q61062, ECO:0000269|PubMed:18552847}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14641}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the epidermis.
CC {ECO:0000269|PubMed:18552847}.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000255}.
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DR EMBL; BC074187; AAH74187.1; -; mRNA.
DR RefSeq; NP_001086098.1; NM_001092629.1.
DR AlphaFoldDB; Q6DKE2; -.
DR SMR; Q6DKE2; -.
DR GeneID; 444527; -.
DR KEGG; xla:444527; -.
DR CTD; 444527; -.
DR Xenbase; XB-GENE-977365; dvl3.L.
DR OrthoDB; 474724at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 444527; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0032053; P:ciliary basal body organization; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; IPR008342; DVL3.
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:SF6; PTHR10878:SF6; 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 Cilium biogenesis/degradation; Cytoplasm; Developmental protein;
KW Reference proteome; Wnt signaling pathway.
FT CHAIN 1..717
FT /note="Segment polarity protein dishevelled homolog DVL-3"
FT /id="PRO_0000354666"
FT DOMAIN 1..82
FT /note="DIX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00069"
FT DOMAIN 248..333
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 421..495
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REGION 89..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 78770 MW; 19A97688E4C1BC01 CRC64;
MGETKVIYHL DEQETPYLVK LPVPAEKVTL GDFKNILNKP NYKFFFKSMD DDFGVVKEEI
SDDNAKLPCF NGRVVCWLVS ADGSQSDAGS VCADIQSDLP PPIERTGGIG DSRPPSFHPN
TRGSQENLDN ETETDSVVSA RRERPGRKET SEHATRINGT SKMERRRDTG GYESSSTLMS
SELDSTSFFD SDEDDSTSRF SNSTEQSSAS RLMRRHKRRR RKPKAPQIER SSSFSSITDS
TMSLNIITVT LNMEKYNFLG ISIVGQSNER GDGGIYIGSI MKGGAVAADG RIEPGDMLLQ
VNDTNFENMS NDDAVRVLRD IVHKPGPITL TVAKCWDPSP RNCFTLPRSE PIRPIDPAAW
VSHTAAMTGT YPAYGMSPSM STITSTSSSI TSSIPETERF DDFQLSIHSD MVTIVKAMSS
SESGLEVRDR MWLKITIPNA FIGSDVVDWL YHHVEGFTDR REARKYASNL LKAGYIRHTV
NKITFSEQCY YIFGDLCGNM ANLSLNDHDG SSGTSDQDTL APLPHPGAAP WPIAFQYQYP
LPHPYSPHPG FPDPAYIYGG GSAGSQHSEG SRSSGSNRSS TEKRKDRETK GGDSKSGGSG
SESDHTTRSS LRRDRAASER SVPASEHSHR SHHSIAHSIR SHHTHQSFGP PGIPPLYGAP
MMMMPAPVSV MGPPGAPPSR DLASVPPELT ASRQSFRMAM GNPSEFFVDV IKEFWGV
