DACT3_HUMAN
ID DACT3_HUMAN Reviewed; 629 AA.
AC Q96B18;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Dapper homolog 3;
DE AltName: Full=Antagonist of beta-catenin Dapper homolog 3;
DE AltName: Full=Arginine-rich region 1 protein;
DE AltName: Full=Dapper antagonist of catenin 3;
GN Name=DACT3; Synonyms=RRR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION.
RX PubMed=16881060; DOI=10.1002/dvdy.20917;
RA Fisher D.A., Kivimaee S., Hoshino J., Suriben R., Martin P.-M., Baxter N.,
RA Cheyette B.N.R.;
RT "Three Dact gene family members are expressed during embryonic development
RT and in the adult brains of mice.";
RL Dev. Dyn. 235:2620-2630(2006).
RN [3]
RP FUNCTION, AND INTERACTION WITH DVL2.
RX PubMed=18538736; DOI=10.1016/j.ccr.2008.04.019;
RA Jiang X., Tan J., Li J., Kivimae S., Yang X., Zhuang L., Lee P.L.,
RA Chan M.T., Stanton L.W., Liu E.T., Cheyette B.N., Yu Q.;
RT "DACT3 is an epigenetic regulator of Wnt/beta-catenin signaling in
RT colorectal cancer and is a therapeutic target of histone modifications.";
RL Cancer Cell 13:529-541(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-165 AND SER-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May be involved in regulation of intracellular signaling
CC pathways during development. Specifically thought to play a role in
CC canonical and/or non-canonical Wnt signaling pathways through
CC interaction with DSH (Dishevelled) family proteins.
CC {ECO:0000269|PubMed:18538736}.
CC -!- SUBUNIT: Can form homodimers and heterodimers with DACT1 or DACT3.
CC Interacts with CSNK1D, PKA catalytic subunit, PKC-type kinase, DVL1,
CC DVL3, VANGL1, VANGL2 and CTNND1 (By similarity). Interacts with DVL2.
CC {ECO:0000250, ECO:0000269|PubMed:18538736}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16161.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC016161; AAH16161.1; ALT_SEQ; mRNA.
DR EMBL; BI603646; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS12688.2; -.
DR RefSeq; NP_001287975.1; NM_001301046.1.
DR RefSeq; NP_659493.2; NM_145056.2.
DR RefSeq; XP_011524801.1; XM_011526499.2.
DR RefSeq; XP_011524802.1; XM_011526500.2.
DR AlphaFoldDB; Q96B18; -.
DR BioGRID; 127095; 21.
DR STRING; 9606.ENSP00000375783; -.
DR iPTMnet; Q96B18; -.
DR PhosphoSitePlus; Q96B18; -.
DR BioMuta; DACT3; -.
DR DMDM; 119368655; -.
DR jPOST; Q96B18; -.
DR MassIVE; Q96B18; -.
DR PaxDb; Q96B18; -.
DR PeptideAtlas; Q96B18; -.
DR PRIDE; Q96B18; -.
DR ProteomicsDB; 76034; -.
DR Antibodypedia; 31468; 213 antibodies from 26 providers.
DR DNASU; 147906; -.
DR Ensembl; ENST00000391916.7; ENSP00000375783.2; ENSG00000197380.11.
DR GeneID; 147906; -.
DR KEGG; hsa:147906; -.
DR MANE-Select; ENST00000391916.7; ENSP00000375783.2; NM_145056.3; NP_659493.2.
DR UCSC; uc010ekq.3; human.
DR CTD; 147906; -.
DR DisGeNET; 147906; -.
DR GeneCards; DACT3; -.
DR HGNC; HGNC:30745; DACT3.
DR HPA; ENSG00000197380; Tissue enhanced (brain).
DR MIM; 611112; gene.
DR neXtProt; NX_Q96B18; -.
DR OpenTargets; ENSG00000197380; -.
DR PharmGKB; PA162383145; -.
DR VEuPathDB; HostDB:ENSG00000197380; -.
DR eggNOG; KOG4119; Eukaryota.
DR GeneTree; ENSGT00950000183181; -.
DR HOGENOM; CLU_031461_0_0_1; -.
DR InParanoid; Q96B18; -.
DR OMA; WASPWES; -.
DR OrthoDB; 1378126at2759; -.
DR PhylomeDB; Q96B18; -.
DR TreeFam; TF331300; -.
DR PathwayCommons; Q96B18; -.
DR SignaLink; Q96B18; -.
DR SIGNOR; Q96B18; -.
DR BioGRID-ORCS; 147906; 24 hits in 1080 CRISPR screens.
DR ChiTaRS; DACT3; human.
DR GenomeRNAi; 147906; -.
DR Pharos; Q96B18; Tbio.
DR PRO; PR:Q96B18; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96B18; protein.
DR Bgee; ENSG00000197380; Expressed in popliteal artery and 153 other tissues.
DR ExpressionAtlas; Q96B18; baseline and differential.
DR Genevisible; Q96B18; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070097; F:delta-catenin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0051018; F:protein kinase A binding; ISS:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR InterPro; IPR024844; Dact3.
DR InterPro; IPR024843; Dapper.
DR PANTHER; PTHR15919; PTHR15919; 1.
DR PANTHER; PTHR15919:SF1; PTHR15919:SF1; 1.
DR Pfam; PF15268; Dapper; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Methylation; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..629
FT /note="Dapper homolog 3"
FT /id="PRO_0000264616"
FT REGION 50..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 63..87
FT /evidence="ECO:0000255"
FT MOTIF 626..629
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 107..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0PHV7"
FT MOD_RES 258
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q0PHV7"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0PHV7"
SQ SEQUENCE 629 AA; 64949 MW; 916CAA2AA9370497 CRC64;
MIRAFSFPVS PERGRLRGWL EGSLAGLCEL HWLRERQEYR VQQALRLAQP GMGGAEAEDE
EDADEDEDAA AARRAAAALE EQLEALPGLV WDLGQQLGDL SLESGGLEQE SGRSSGFYED
PSSTGGPDSP PSTFCGDSGF SGSSSYGRLG PSEPRGIYAS ERPKSLGDAS PSAPEVVGAR
AAVPRSFSAP YPTAGGSAGP EACSSAERRA RAGPFLTPSP LHAVAMRSPR PCGRPPTDSP
DAGGAGRPLD GYISALLRRR RRRGAGQPRT SPGGADGGPR RQNSVRQRPP DASPSPGSAR
PAREPSLERV GGHPTSPAAL SRAWASSWES EAAPEPAAPP AAPSPPDSPA EGRLVKAQYI
PGAQAATRGL PGRAARRKPP PLTRGRSVEQ SPPRERPRAA GRRGRMAEAS GRRGSPRARK
ASRSQSETSL LGRASAVPSG PPKYPTAERE EPRPPRPRRG PAPTLAAQAA GSCRRWRSTA
EIDAADGRRV RPRAPAARVP GPGPSPSAPQ RRLLYGCAGS DSECSAGRLG PLGRRGPAGG
VGGGYGESES SASEGESPAF SSASSDSDGS GGLVWPQQLV AATAASGGGA GAGAPAGPAK
VFVKIKASHA LKKKILRFRS GSLKVMTTV
