TDRD3_DANRE
ID TDRD3_DANRE Reviewed; 733 AA.
AC Q6NYG6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Tudor domain-containing protein 3;
GN Name=tdrd3; ORFNames=zgc:77174;
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 [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Scaffolding protein that specifically recognizes and binds
CC dimethylarginine-containing proteins. In nucleus, acts as a
CC coactivator: recognizes and binds asymmetric dimethylation on the core
CC histone tails associated with transcriptional activation (H3R17me2a and
CC H4R3me2a) and recruits proteins at these arginine-methylated loci. In
CC cytoplasm, may play a role in the assembly and/or disassembly of mRNA
CC stress granules and in the regulation of translation of target mRNAs by
CC binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing
CC proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of mRNA stress granules.
CC {ECO:0000250|UniProtKB:Q9H7E2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly cytoplasmic. Associated with actively translating
CC polyribosomes and with mRNA stress granules (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The Tudor domain specifically recognizes and binds asymmetric
CC dimethylation of histone H3 'Arg-17' (H3R17me2a) and histones H4 'Arg-
CC 3', 2 tags for epigenetic transcriptional activation. {ECO:0000250}.
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DR EMBL; BC066604; AAH66604.1; -; mRNA.
DR AlphaFoldDB; Q6NYG6; -.
DR SMR; Q6NYG6; -.
DR STRING; 7955.ENSDARP00000030883; -.
DR PaxDb; Q6NYG6; -.
DR PeptideAtlas; Q6NYG6; -.
DR ZFIN; ZDB-GENE-040426-19; tdrd3.
DR eggNOG; KOG3683; Eukaryota.
DR InParanoid; Q6NYG6; -.
DR PhylomeDB; Q6NYG6; -.
DR PRO; PR:Q6NYG6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR CDD; cd04508; TUDOR; 1.
DR CDD; cd14282; UBA_TDRD3; 1.
DR Gene3D; 2.40.50.770; -; 1.
DR InterPro; IPR033472; DUF1767.
DR InterPro; IPR013894; RMI1_N.
DR InterPro; IPR042470; RMI1_N_C_sf.
DR InterPro; IPR010304; SMN_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041915; UBA_TDRD3.
DR Pfam; PF08585; RMI1_N; 1.
DR Pfam; PF06003; SMN; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM01161; DUF1767; 1.
DR SMART; SM00333; TUDOR; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50304; TUDOR; 1.
DR PROSITE; PS50030; UBA; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..733
FT /note="Tudor domain-containing protein 3"
FT /id="PRO_0000367248"
FT DOMAIN 290..330
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 639..699
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 241..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 81779 MW; BDA59B742E107B8B CRC64;
MCDLSSALIK EGWYLTDEGI EECKSSSEKE KTSPTDIIQV ALNNDLRPIG KSFLPADINS
GRIEKLEGPC VLQVQKIRNV AASKDHEESQ AAPRMLRVQM TDGHTACTGL EFKQLSKISL
NTPPGTKVKL LGVVQVKNGI LLLDDSKIAV LGGEVDHMIE KWEFQRSLAK HSRRNIGAEG
GPPPFVPFGQ KCVHKEQVDS RALDQRKTLQ STNAVKSADD NDEFEKQRTA AIAEVAKSKE
TRTFGGGGNA GGNLANPGSS YKSRDTYQRK REEREKPWTE NKSDGVYRDL VDERALRDIM
EMGFNREAAR QALLDNNNNL EVALNLLLTR ANQPRAAPVE QSRPPPRGKG RGKGRSRQDE
DEEAGGRPSG PSTLFDFLES KMGTFSIDDS KPSQQDHQTK MNFSNSDQMS RDAGQFKPPP
RNDGRSQRND RPPRFQKDGD FPKPTPASSS FSQPQKWRDG ERTGRGGGPE RWKNESQDAR
NAPVSYSSSF SKSREQQGAS GKELNKEQDG TGPASFRKIQ SNGPAPPKFS TPADPKMRNE
PNNRRKGRPE RPNSGYFEHS QDALGKKDFQ DEGQFVKVGP VSNTPLPNGD LEHRRTGPIK
PHFSAPPPRQ TNMHNPASKR RSGPIKGPRD SVDINNFVNW KAGDQCLALY WEDNKFYRAR
IDAVHPSGST AVVVFSDYGN CEEVLLDSIK PLHMDDDEDV YYENSLEFRR GGDGQPRRSR
PTQQYYQPPR ARD
