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DVL3_XENTR
ID   DVL3_XENTR              Reviewed;         713 AA.
AC   B1WAP7;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAI61453.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula {ECO:0000312|EMBL:AAI61453.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250|UniProtKB:Q61062,
CC       ECO:0000250|UniProtKB:Q6DKE2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14641}.
CC   -!- SIMILARITY: Belongs to the DSH family. {ECO:0000255}.
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DR   EMBL; BC161453; AAI61453.1; -; mRNA.
DR   RefSeq; NP_001116929.1; NM_001123457.1.
DR   AlphaFoldDB; B1WAP7; -.
DR   SMR; B1WAP7; -.
DR   STRING; 8364.ENSXETP00000037606; -.
DR   PaxDb; B1WAP7; -.
DR   Ensembl; ENSXETT00000037606; ENSXETP00000037606; ENSXETG00000017275.
DR   GeneID; 100144702; -.
DR   KEGG; xtr:100144702; -.
DR   CTD; 1857; -.
DR   Xenbase; XB-GENE-977362; dvl3.
DR   eggNOG; KOG3571; Eukaryota.
DR   HOGENOM; CLU_012601_1_0_1; -.
DR   InParanoid; B1WAP7; -.
DR   OrthoDB; 474724at2759; -.
DR   Reactome; R-XTR-201688; WNT mediated activation of DVL.
DR   Reactome; R-XTR-4086400; PCP/CE pathway.
DR   Reactome; R-XTR-4641258; Degradation of DVL.
DR   Reactome; R-XTR-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR   Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000017275; Expressed in blastula and 12 other tissues.
DR   ExpressionAtlas; B1WAP7; baseline.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008013; F:beta-catenin binding; 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:0032053; P:ciliary basal body organization; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
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; 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..713
FT                   /note="Segment polarity protein dishevelled homolog DVL-3"
FT                   /id="PRO_0000354667"
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          87..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..652
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        212..226
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..577
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   713 AA;  78314 MW;  E43625C6BC9E79A4 CRC64;
     MGETKVIYHL DEQETPYLVK LPVPAEKVTL GDFKNVLNKP NYKFFFKSMD DDFGVVKEEI
     SDDNAKLPCF NGRVVCWLVS ADGSQSDAGS VCADNQSDLP PPIERTGGIG DSRPPSFHPN
     TRGSQENLDN ETETDSVVSA HRERPRRKET PEHATRLNGT SKMERRRDTG GYESSSTLMS
     SELDSTSFFD SDEDDSTSRF SNSTEQSSAS RLMRRHKRRR RKPKAPRIER SSSFSSITDS
     TMSLNIITVT LNMEKYNFLG ISIVGQSNER GDGGIYIGSI MKGGAVAADG RIEPGDMLLQ
     VNDTNFENMS NDDAVRVLRE IVHKPGPITL TVAKCWDPSP RNCFTLPRSE PIRPIDPAAW
     VSHTAAMTGS YPAYGMSPSM STITSTSSSI TSSIPETERF DDFQLSIHSD MVTIVKAMRS
     PESGLEVRDR MWLKITIPNA FIGSDVVDWL YHHVEGFTDR REARKYASNL LKAGYIRHTV
     NKITFSEQCY YIFGDLCGNM ANLSLNDHDG SSGTSDQDTL APLPHPGAAP WPIAFQYQYP
     LPHPYSPHPG FPDPAYSYGG GSAGSQHSEG SRSSGSNRSS TEKRKEREAK GGDTKSGGSG
     SESDHTTRSS VRRERAASER SVPASEHSHR SHHSIAHSIR SHHTHHSFGP PGIPPLYGAP
     MMMMPAPASV IGPPGAPPSR DLASVPPELT ASRQSFRMAM GNPTKNSGVF DFL
 
 
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