DACT2_DANRE
ID DACT2_DANRE Reviewed; 837 AA.
AC Q673G8; A0JPE4; Q5YFS6; Q800W5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Dapper homolog 2;
DE AltName: Full=Frodo 2;
GN Name=dact2; Synonyms=dpr2, frd2; ORFNames=zgc:152832;
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], FUNCTION, INTERACTION WITH DVL2, SUBCELLULAR
RP 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15459392; DOI=10.1126/science.1100569;
RA Zhang L., Zhou H., Su Y., Sun Z., Zhang H., Zhang L., Zhang Y., Ning Y.,
RA Chen Y.-G., Meng A.;
RT "Zebrafish Dpr2 inhibits mesoderm induction by promoting degradation of
RT nodal receptors.";
RL Science 306:114-117(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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. Positive regulator of the Wnt
CC signaling pathway which acts downstream of wnt1 indicative for non-
CC canonical Wnt signaling. Also negatively regulates the Nodal signaling
CC pathway, possibly by promoting the lysosomal degradation of Nodal
CC receptors. Required for convergent extension movements in gastrulation.
CC {ECO:0000269|PubMed:15459392, ECO:0000269|PubMed:15539487}.
CC -!- SUBUNIT: Interacts with dvl2. {ECO:0000269|PubMed:15539487}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Late endosome. Nucleus. Cell membrane.
CC Note=Predominantly cytoplasmic. Also found in late endosomes, the
CC nucleus and at the cell membrane.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Restricted to the dorsal
CC blastoderm margin in early gastrula and the future dorsal side of the
CC embryo at the sphere stage. At the shield stage, expressed throughout
CC the shield and in lateral areas. Expressed in the anterior brain and
CC axial mesoderm at the tailbud stage, and subsequently maintained in the
CC lateral mesoderm. During somitogenesis, up-regulated in the anterior of
CC the older somites, and expressed in the posterior presomitic mesoderm
CC and tailbud. {ECO:0000269|PubMed:15188426, ECO:0000269|PubMed:15459392,
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO49711.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY549444; AAT42266.1; -; mRNA.
DR EMBL; AY208969; AAO49711.2; ALT_FRAME; mRNA.
DR EMBL; AY513131; AAS82844.1; -; mRNA.
DR EMBL; BC127383; AAI27384.1; -; mRNA.
DR AlphaFoldDB; Q673G8; -.
DR IntAct; Q673G8; 1.
DR STRING; 7955.ENSDARP00000078756; -.
DR PaxDb; Q673G8; -.
DR PRIDE; Q673G8; -.
DR ZFIN; ZDB-GENE-030131-9975; dact2.
DR eggNOG; ENOG502QVT3; Eukaryota.
DR InParanoid; Q673G8; -.
DR PhylomeDB; Q673G8; -.
DR PRO; PR:Q673G8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048332; P:mesoderm morphogenesis; IMP:ZFIN.
DR GO; GO:1900108; P:negative regulation of nodal signaling pathway; IDA:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:ZFIN.
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 Cell membrane; Coiled coil; Cytoplasm; Developmental protein; Endosome;
KW Membrane; Nucleus; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..837
FT /note="Dapper homolog 2"
FT /id="PRO_0000191359"
FT REGION 189..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..113
FT /evidence="ECO:0000255"
FT MOTIF 834..837
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 243..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..539
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..782
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 76
FT /note="A -> V (in Ref. 4; AAI27384)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="T -> S (in Ref. 3; AAS82844)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="S -> A (in Ref. 4; AAI27384)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="G -> E (in Ref. 2; AAO49711)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="E -> D (in Ref. 1; AAT42266)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="S -> L (in Ref. 1; AAT42266)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="S -> F (in Ref. 3; AAS82844)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="S -> C (in Ref. 1; AAT42266)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="R -> K (in Ref. 4; AAI27384)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="G -> R (in Ref. 1; AAT42266)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="S -> T (in Ref. 1; AAT42266 and 4; AAI27384)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="L -> V (in Ref. 1; AAT42266)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="D -> V (in Ref. 1; AAT42266)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="K -> N (in Ref. 1; AAT42266)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="S -> N (in Ref. 4; AAI27384)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="L -> S (in Ref. 1; AAT42266 and 4; AAI27384)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="T -> N (in Ref. 1; AAT42266)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="T -> N (in Ref. 4; AAI27384)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="P -> R (in Ref. 4; AAI27384)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="S -> F (in Ref. 3; AAS82844)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="S -> T (in Ref. 3; AAS82844)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="Y -> C (in Ref. 4; AAI27384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 837 AA; 91295 MW; C55BD8215010E4C8 CRC64;
MLGRKIPGSG VLGAGAGMDR GRTGERLHAA LAGLQELHFL RDKQSAMVHW ALTLNRDQPD
PSKQENVSKE ELRLEATLSL LKQQLTRLRR QDVGLKTHLQ QLDQQITELK LDVCKASTEH
LESDSRPSSG FYELSDGGSG SLSNSCTSVY SESLSSSSQT SLLPLLSTSY ASHGRSSCGQ
TGVSRRCSAD ESTAQSDAPR SGVKLGSSLI RTATARADRA RQRPVSTGDL DRMIGPGFGA
FKSTDVKSST PCSSPQNPSV DPKYQSNLVS SNGTEVYRYP SPLHAVALQS PIFSCTSDQG
SSVALDEMPE EETQNLNEES TISSSVGYIN KLLQRSSSRV NLLSSIKRIE TVSGTHEQIP
RSQEMIYGSL NGPQLLGSLQ QLSMPLENAL ETGKTSALNN NQKQMDPPCL GSNFKEVEVQ
MLHHGKHPES SLDLQKNNFP INNTAGKVGA ESDNGASEKR SGHFPKDLSV VQKPVERKSS
FTSGREGSRA SCHDKSSIPQ SEFVHAQFVP AGSQRVKVRQ ADKKTKSVKL RKKSSEKPSA
KKQHQKPLSR EFCTKNRTDL KQSGSCRGKV TYLEESQAQS CSDCSCNGLI NSHCIQNNHQ
QIPSSKSTKS RKAPEPVYHP LDHAKKKPSS RKWPSSSEIP LPPTLHTQRS KEMLNSRKVA
MVRSVSARPR SGHWGCPPPR ALPHSLSTSS YFSYLESRYP AAPVSSRHPP RCESEFSEYS
AECASLFHST IAASSDGEMS DYTTNRFGDS ESSQGSQTAS ESDSSLSLDE EDLLEEEEED
EGGLVWAQAA MGTTAAGFSL QQHHRSESAA CRIKASRALK KKIRRFQPAS LKVMTLV
