TDRD3_BOVIN
ID TDRD3_BOVIN Reviewed; 722 AA.
AC Q2HJG4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Tudor domain-containing protein 3;
GN Name=TDRD3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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. Interacts with FMR1, FXR1,
CC FXR2, EWSR1, FUS, SERBP1, EEF1A1 and DDX3X or DDX3Y, and with the small
CC nuclear ribonucleoprotein-associated proteins SNRPB and SNRPN.
CC Interacts with 'Lys-48'-linked tetra-ubiquitin, but not with
CC monoubiquitin or 'Lys-63'-linked ubiquitin chains. May interact with
CC the exon junction complex (EJC) composed at least of CASC3, EIF4A3,
CC MAGOH and RBM8A. Interacts with POLR2A (via the C-terminal domain
CC (CTD)). {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; BC105432; AAI05433.1; -; mRNA.
DR RefSeq; NP_001039891.1; NM_001046426.2.
DR AlphaFoldDB; Q2HJG4; -.
DR SMR; Q2HJG4; -.
DR STRING; 9913.ENSBTAP00000012261; -.
DR PaxDb; Q2HJG4; -.
DR PRIDE; Q2HJG4; -.
DR GeneID; 537918; -.
DR KEGG; bta:537918; -.
DR CTD; 81550; -.
DR eggNOG; KOG3683; Eukaryota.
DR InParanoid; Q2HJG4; -.
DR OrthoDB; 914913at2759; -.
DR Proteomes; UP000009136; 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:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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; 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; PF00567; TUDOR; 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; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..722
FT /note="Tudor domain-containing protein 3"
FT /id="PRO_0000367246"
FT DOMAIN 264..304
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 626..686
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 305..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..722
FT /note="EBM motif; may mediate interaction with the EJC"
FT /evidence="ECO:0000250"
FT COMPBIAS 321..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7E2"
FT CROSSLNK 541
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H7E2"
SQ SEQUENCE 722 AA; 80808 MW; 2900A05D7CD22827 CRC64;
MAEAPGAALS RAGWYLSDEG IEACTSSPDK VNVNDIILIA LNLEGPCVLQ IQKIRNVAAP
KDNEESQAAP RMLRLQMTDG HISCTAVEFS YLSKISLNTP PGTKVKLSGA VDIKNGFLLL
NDSNTTVLGG EVEHLIEKWE LQRSLSKHNR SNIGTEGGPP PFVPFGQKCV SHIQVDSREL
DRRKTLQVTM PVKPPNDNDE FEKQRTAAIA EVAKSKETKT FGGGGGGARS NLNMHAAGNR
NREILQKEKA NKSEGKHEGV YRELVDEKAL RHITEMGFSK EASRQALMDN GNNLEAALNV
LLNSNKQKPV TGPPLRGKGK GRGRIRSEDE EELGNARPSA PSTLFDFLES KMGTLSVEEP
KSQPQQLHQG QNRVSNTEQN GVKDNNQPRY LPRNDTRQPR NEKPPRFQRD TQNSKAVLEG
SGLPRNRGSE RPSTSSGSEG WAEERTKCDR SYSRYDRTKD TSYLLSSQHS DTVFKKRDNS
MQSRSGKGPS YTEAKENPFP QESVDYNNHK RGKRENQTAN SDHFYDRKPR TINNEAFSGV
KIEKHFNVNT DYQHPVRMNS FIGVPNGETE MPLKGRRVGP IKPAGPIMAS SCDDKIFYSS
GPKRRSGPIK PEKVLESSIP MEYAKLWKSG DECLALYWED NKFYRAEVEA LHSSGMTAVV
KFIDYGNYEE VLLSNIRPIQ SEAWEEEGTY DQTLEFRRGG DGQPRRSTRP TQQFYQPPRA
RN
