DACT1_DANRE
ID DACT1_DANRE Reviewed; 821 AA.
AC Q6QZN6; Q673G9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Dapper homolog 1;
DE AltName: Full=Frodo 1;
GN Name=dact1; Synonyms=dpr1, frd1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula;
RX PubMed=15188426; DOI=10.1002/dvdy.20060;
RA Gillhouse M., Wagner Nyholm M., Hikasa H., Sokol S.Y., Grinblat Y.;
RT "Two Frodo/Dapper homologs are expressed in the developing brain and
RT mesoderm of zebrafish.";
RL Dev. Dyn. 230:403-409(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-821, FUNCTION, INTERACTION WITH DVL2,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15539487; DOI=10.1242/dev.01520;
RA Waxman J.S., Hocking A.M., Stoick C.L., Moon R.T.;
RT "Zebrafish Dapper1 and Dapper2 play distinct roles in Wnt-mediated
RT developmental processes.";
RL Development 131:5909-5921(2004).
CC -!- FUNCTION: Involved in regulation of intracellular signaling pathways
CC during development. Specifically thought to play a role in canonical
CC and/or non-canonical Wnt signaling pathways through interaction with
CC DSH (Dishevelled) family proteins. Binds to dvl2 and may regulate the
CC degradation of ctnnb1/beta-catenin, thereby modulating the
CC transcriptional activation of target genes of the Wnt signaling
CC pathway. Seems to activate the canonical Wnt signaling pathway.
CC {ECO:0000269|PubMed:15539487}.
CC -!- SUBUNIT: Interacts with dvl2. {ECO:0000269|PubMed:15539487}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15539487}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the future mesendoderm during early
CC gastrulation. Expressed in the prechordal plate axial mesoderm and the
CC posterior neural plate in mid-gastrula, and in the anterior neural
CC plate at the end of gastrulation and during somitogenesis. Strongly
CC expressed in and the tail bud and several areas of the brain at the end
CC of somitogenesis. {ECO:0000269|PubMed:15188426,
CC ECO:0000269|PubMed:15539487}.
CC -!- DOMAIN: The C-terminal PDZ-binding motif may mediate interaction with
CC the PDZ domains of DSH (Dishevelled) family proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dapper family. {ECO:0000305}.
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DR EMBL; AY521628; AAS09955.1; -; mRNA.
DR EMBL; AY549443; AAT42265.1; -; mRNA.
DR AlphaFoldDB; Q6QZN6; -.
DR IntAct; Q6QZN6; 1.
DR STRING; 7955.ENSDARP00000058000; -.
DR PaxDb; Q6QZN6; -.
DR PRIDE; Q6QZN6; -.
DR ZFIN; ZDB-GENE-040623-3; dact1.
DR eggNOG; ENOG502QVXB; Eukaryota.
DR InParanoid; Q6QZN6; -.
DR PhylomeDB; Q6QZN6; -.
DR Reactome; R-DRE-4641258; Degradation of DVL.
DR PRO; PR:Q6QZN6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IBA:GO_Central.
DR GO; GO:2000095; P:regulation of Wnt signaling pathway, planar cell polarity pathway; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:ZFIN.
DR InterPro; IPR024848; Dact1.
DR InterPro; IPR024843; Dapper.
DR PANTHER; PTHR15919; PTHR15919; 1.
DR PANTHER; PTHR15919:SF12; PTHR15919:SF12; 1.
DR Pfam; PF15268; Dapper; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Developmental protein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..821
FT /note="Dapper homolog 1"
FT /id="PRO_0000191358"
FT REGION 288..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 88..136
FT /evidence="ECO:0000255"
FT MOTIF 818..821
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 576..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..655
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 15
FT /note="A -> T (in Ref. 2; AAT42265)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Q -> R (in Ref. 2; AAT42265)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="S -> I (in Ref. 2; AAT42265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 90721 MW; 265F2C7C0A570F4D CRC64;
MNEWSEMLVC RDYCALMMRD RKECDARCCR DGEGERVRAR ERLDATVAGL TELEYLRQRQ
ELLVRSVLSC PEAAGQDKPC LTVDDSYLNT EEKLLEENIL LLRKQLNCLR RRDAGLINQL
QELDRQISDL RLDTETSHEH VETDSRPSSG FYDLSDGASG SLSNSSNSVF SECLSSCRST
TCLCTPLDTS LCASEGRLKP ADDPGSCAEC DCHCEDSSSG TVRRSLSASY SPSPDSSCDG
ISKFHCDLIA KNGNDVYRYP SPLHAVAVQS PIFIQSMTSH LKDDCNFSKP GEALNDEQKP
EQVVGSQTSS WHASQMLPNK KLDSYIYGLL QRRAQPLRTN KPRTSINTDP SKSILRQASL
CSRAPASVQA QQWTSDLKPN WQTCLQDASA TSTEPSTASP QRQWSAESKG GTPQNGAYLS
SSQPQNSYST TNENTNCLLK KKVSGTSKGQ LLSATPKDCP DLGSPKAVSS PKLNKHCFYN
VEDNKTGQAM KASPLKRSPK TQTSLSCGKD SEQLAQELVS LGSSSQSQDE GGPLVSAQYI
PAQKQNVNLQ KGGTKNIKIV KVKNSASSKS RPQVFEHVSE TVRDKHRTGS RRTRQVDEVH
HLHKSSKKAS AKTKRIPASI PEGRILERHT SSSGARSSAQ RHHGHHRHHE AVLAKPKYKR
NDFHRRPRGL HEIPYEEAYR RAHRRQKREM LSHMYLPSNA HYTSPYAYVG SDSEYSAECA
SLFHSTILDT SEDERSNYTT NCFGDSESSA SEADYVAESS TSSDSEGSAG VNWRQISQAG
SGSHGMTSAQ AKAFVKIKAS HNLKKKILRF RSGSLKLMTT V