ID A0A287CZ49_ICTTR Unreviewed; 688 AA.
AC A0A287CZ49;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Dishevelled segment polarity protein 1 {ECO:0000313|Ensembl:ENSSTOP00000026587.1};
GN Name=DVL1 {ECO:0000313|Ensembl:ENSSTOP00000026587.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000026587.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000026587.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DSH family. {ECO:0000256|ARBA:ARBA00008735}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGTP01101335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A287CZ49; -.
DR Ensembl; ENSSTOT00000033887.1; ENSSTOP00000026587.1; ENSSTOG00000013023.3.
DR GeneTree; ENSGT00950000182903; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0022603; P:regulation of anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd04438; DEP_dishevelled; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.240.130; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; 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; SEGMENT POLARITY PROTEIN DISHEVELLED; 1.
DR PANTHER; PTHR10878:SF5; SEGMENT POLARITY PROTEIN DISHEVELLED HOMOLOG DVL-1-RELATED; 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 PRINTS; PR01761; DISHEVELLED1.
DR SMART; SM00021; DAX; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50841; DIX; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|PROSITE-
KW ProRule:PRU00069}.
FT DOMAIN 1..88
FT /note="DIX"
FT /evidence="ECO:0000259|PROSITE:PS50841"
FT DOMAIN 243..315
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 417..491
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT REGION 81..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 688 AA; 74150 MW; 1913C8AA6586F5CA CRC64;
MAETKIIYHM DEEETPYLVK LPVAPERVTL ADFKNVLSNR PVHAYKFFFK SMDQDFGSVG
RAAWAGAGGH LSLVLAEGAH SDAGSQGTDC HTDLPPPLER TGGIGDSRPP SFHPNVASSR
DGMDNETGTE SMVSHRRERA RRRNREEAAR ANGHPRGDRR RDLGLPPDSA STVLSSELES
SSFIDSDEED NTSRLSSSTE QSTSSRLIRK HKRRRRKQRL RQTDRASSFS SITDSTMSLN
IITVTLNMER HHFLGISIVG QSNDRGDGGI YIGSIMKGGA VAADGRIEPG DMLLQVNDVN
FENMSNDDAV RVLRELVSQT GPISLTVAKC WDPTPRSYFT IPRADPVRPI DPAAWLSHTA
ALTGALPRYG ASPCSSAVSR TSSSSLTSSV PGAPQLEEAP LTVKSDMSAV VRVMQLPDSG
LEIRDRMWLK ITIANAVIGA DVVDWLYTHV EGFKERREAR KYASGMLKHG FLRHTVNKVT
FSEQCYYVFG DLCSNLAALT LNSGSSGASD QDTLAPLPHP AAPWPLGQGY PYQYPGPPPC
FPPAYQDPGF GYGSGSAGSQ QSEGSKSSGS TRSSRRALGR EEERRAAGAR GSGSESDHTV
LSGSGGTGRR ERPVSQLSRG SSPHSQLSAV APGLPPLHPL TKAYAVVGGP PGGPPVRELA
AVPPELTGSR QSFQKAMGNP CEFFVDIM
//
