DACT2_MOUSE
ID DACT2_MOUSE Reviewed; 757 AA.
AC Q7TN08; Q6PDF4; Q8BHZ7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Dapper homolog 2;
DE Short=mDpr2;
DE AltName: Full=Dapper antagonist of catenin 2;
GN Name=Dact2; Synonyms=Dpr2, Frd2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=CD-1; TISSUE=Brain cortex;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [4]
RP FUNCTION, INTERACTION WITH TGFBR1, AND DEVELOPMENTAL STAGE.
RX PubMed=17197390; DOI=10.1096/fj.06-6246com;
RA Su Y., Zhang L., Gao X., Meng F., Wen J., Zhou H., Meng A., Chen Y.-G.;
RT "The evolutionally conserved activity of Dapper2 in antagonizing TGF-beta
RT signaling.";
RL FASEB J. 21:682-690(2007).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18716284; DOI=10.1242/jcs.032417;
RA Meng F., Cheng X., Yang L., Hou N., Yang X., Meng A.;
RT "Accelerated re-epithelialization in Dpr2-deficient mice is associated with
RT enhanced response to TGFbeta signaling.";
RL J. Cell Sci. 121:2904-2912(2008).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=20685821; DOI=10.1152/ajprenal.00148.2010;
RA Lee W.C., Hough M.T., Liu W., Ekiert R., Lindstrom N.O., Hohenstein P.,
RA Davies J.A.;
RT "Dact2 is expressed in the developing ureteric bud/collecting duct system
RT of the kidney and controls morphogenetic behavior of collecting duct
RT cells.";
RL Am. J. Physiol. 299:F740-F751(2010).
RN [7]
RP PHOSPHORYLATION, SELF-ASSOCIATION, AND INTERACTION WITH DACT1; DACT3;
RP CSNK1D; PKA; PKC; CSNK2B; DVL1; DVL2; DVL3; VANGL1; VANGL2; TGFBR1; CTNNB1;
RP CTNND2; CTNND1; LEF1; TCF7; TCF7L1 AND HDAC1.
RX PubMed=21718540; DOI=10.1186/1471-2091-12-33;
RA Kivimae S., Yang X.Y., Cheyette B.N.;
RT "All Dact (Dapper/Frodo) scaffold proteins dimerize and exhibit conserved
RT interactions with Vangl, Dvl, and serine/threonine kinases.";
RL BMC Biochem. 12:33-33(2011).
CC -!- FUNCTION: Involved in regulation of intracellular signaling pathways
CC during development. Negatively regulates the Nodal signaling pathway,
CC possibly by promoting the lysosomal degradation of Nodal receptors,
CC such as TGFBR1. May be involved in control of the morphogenetic
CC behavior of kidney ureteric bud cells by keeping cells epithelial and
CC restraining their mesenchymal character. May play an inhibitory role in
CC the re-epithelialization of skin wounds by attenuating TGF-beta
CC signaling. {ECO:0000269|PubMed:17197390, ECO:0000269|PubMed:18716284,
CC ECO:0000269|PubMed:20685821}.
CC -!- SUBUNIT: Can form homodimers and heterodimers with DACT1 or DACT3.
CC Interacts with CSNK1D, PKA catalytic subunit, PKC-type kinase, CSNK2B,
CC DVL1, DVL2, DVL3, VANGL1, VANGL2, TGFBR1, CTNNB1, CTNND2, CTNND1, LEF1,
CC TCF7, TCF7L1 and HDAC1. {ECO:0000269|PubMed:17197390,
CC ECO:0000269|PubMed:21718540}.
CC -!- INTERACTION:
CC Q7TN08; Q0PHV7: Dact3; NbExp=2; IntAct=EBI-6392494, EBI-6392520;
CC -!- TISSUE SPECIFICITY: Expressed in kidney (inner medullary collecting
CC duct). Expressed in epidermal keratinocytes and hair follicles.
CC {ECO:0000269|PubMed:18716284, ECO:0000269|PubMed:20685821}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the epiblast at the onset of
CC gastrulation and in somites, the neural tube and gut at later stages of
CC development. In the developing kidney is expressed in the ureteric
CC bud/collecting duct epithelium. {ECO:0000269|PubMed:16881060,
CC ECO:0000269|PubMed:17197390, ECO:0000269|PubMed:20685821}.
CC -!- DOMAIN: The C-terminal PDZ-binding motif may mediate interaction with
CC the PDZ domains of DSH (Dishevelled) family proteins. {ECO:0000250}.
CC -!- MISCELLANEOUS: Involved in non-canonical Wnt signaling only when
CC massively overexpressed.
CC -!- SIMILARITY: Belongs to the dapper family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31003.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY297430; AAP57185.1; -; mRNA.
DR EMBL; AK041604; BAC31003.1; ALT_FRAME; mRNA.
DR EMBL; BC058740; AAH58740.1; -; mRNA.
DR CCDS; CCDS28406.1; -.
DR RefSeq; NP_766414.3; NM_172826.3.
DR AlphaFoldDB; Q7TN08; -.
DR IntAct; Q7TN08; 24.
DR STRING; 10090.ENSMUSP00000051638; -.
DR iPTMnet; Q7TN08; -.
DR PhosphoSitePlus; Q7TN08; -.
DR PaxDb; Q7TN08; -.
DR PRIDE; Q7TN08; -.
DR ProteomicsDB; 279274; -.
DR Antibodypedia; 33560; 65 antibodies from 21 providers.
DR DNASU; 240025; -.
DR Ensembl; ENSMUST00000053218; ENSMUSP00000051638; ENSMUSG00000048826.
DR GeneID; 240025; -.
DR KEGG; mmu:240025; -.
DR UCSC; uc008amv.2; mouse.
DR CTD; 168002; -.
DR MGI; MGI:1920347; Dact2.
DR VEuPathDB; HostDB:ENSMUSG00000048826; -.
DR eggNOG; ENOG502QVT3; Eukaryota.
DR GeneTree; ENSGT00950000183181; -.
DR HOGENOM; CLU_021211_0_0_1; -.
DR InParanoid; Q7TN08; -.
DR OMA; NSCYPAK; -.
DR OrthoDB; 242694at2759; -.
DR PhylomeDB; Q7TN08; -.
DR TreeFam; TF331300; -.
DR BioGRID-ORCS; 240025; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Dact2; mouse.
DR PRO; PR:Q7TN08; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q7TN08; protein.
DR Bgee; ENSMUSG00000048826; Expressed in renal pelvis and 199 other tissues.
DR ExpressionAtlas; Q7TN08; baseline and differential.
DR Genevisible; Q7TN08; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR GO; GO:0070097; F:delta-catenin binding; IDA:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IDA:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0072061; P:inner medullary collecting duct development; IMP:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:1900108; P:negative regulation of nodal signaling pathway; IDA:UniProtKB.
DR GO; GO:0043588; P:skin development; IMP:UniProtKB.
DR InterPro; IPR024853; Dact2.
DR InterPro; IPR024843; Dapper.
DR PANTHER; PTHR15919; PTHR15919; 1.
DR PANTHER; PTHR15919:SF13; PTHR15919:SF13; 1.
DR Pfam; PF15268; Dapper; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..757
FT /note="Dapper homolog 2"
FT /id="PRO_0000326200"
FT REGION 1..281
FT /note="Inhibition of Nodal signaling"
FT REGION 486..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 55..107
FT /evidence="ECO:0000255"
FT MOTIF 754..757
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 505..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..728
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 640
FT /note="S -> P (in Ref. 1; AAP57185)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="T -> A (in Ref. 1; AAP57185)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="S -> G (in Ref. 1; AAP57185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 81668 MW; DB1A32713B36DFD5 CRC64;
MWAPSGQGPA GWDRRRVGAR LRAALAGLQE LQGLRATQQA RVRGALGLHP APGPRGQELR
LEAALTALRE QLSRLRRQDA GLKTHLDQLD QQISELQLDV SRSSCEALDS DSRPSSGFYE
LSDAGSCSLS TSCASVCSDR LSPSLGSWLP VFQPSKSRSG IGDWRPRSAD ETTVPAWSPQ
LTEDSRLLHG AEGTGRLTGM FRPRPVSTGD LERVLPADVG LQRAGTDAAH LLGQGIEIPA
HALDPTYQRD LVARGGQEVY PYPSPLHAVA LQSPLFALPK EAPCFDICSP PQEPPLVPVD
ENRTQPEPIR ELGSAEAYIH RLLHLRGQEL PLRDVGQEQG GDTAAFPPKP CGQRSESTCQ
LEKQACGADR GGLKLGRGAA KDSLKQHGPV SLVGAEPLSS PLKEETIPWN PCVHGDNTVG
SSPCSQAQQP LNDCGQGPVL SPSRVLGTES PPLAPEPFAY TSCTTGETSP VKLRMGFSQN
KAVKVRRRVS EKVPRLGKQL PPQPERQRVT ERDPSRPHQG GLSRRPTLAR EPPGRSCSES
TLYPVPFLVP VVVAQRESYP TSPQAFFPME AALLSSAARR KQRRWQSTME ISAKAGSVSQ
PGPSMGLPRS PAKRGSGPRA QSRPTLARQD ACARCESDPS EHSADCTSLY HSTIAETSED
EEASDHTANR FGDESSSNDS EGCFRGSRRR LAIGSAEAGQ GGWAWPRVPP QQPSRAPGNT
RPPLPPVPKL CRIKASKALK KKIRRFQPAA LKVMTMV
