TDRD3_RAT
ID TDRD3_RAT Reviewed; 651 AA.
AC Q66HC1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Tudor domain-containing protein 3;
GN Name=Tdrd3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC081929; AAH81929.1; -; mRNA.
DR RefSeq; NP_001012043.1; NM_001012043.1.
DR AlphaFoldDB; Q66HC1; -.
DR SMR; Q66HC1; -.
DR BioGRID; 258345; 1.
DR STRING; 10116.ENSRNOP00000012440; -.
DR iPTMnet; Q66HC1; -.
DR PhosphoSitePlus; Q66HC1; -.
DR PaxDb; Q66HC1; -.
DR PRIDE; Q66HC1; -.
DR Ensembl; ENSRNOT00000117994; ENSRNOP00000077267; ENSRNOG00000009034.
DR GeneID; 306066; -.
DR KEGG; rno:306066; -.
DR UCSC; RGD:1310126; rat.
DR CTD; 81550; -.
DR RGD; 1310126; Tdrd3.
DR eggNOG; KOG3683; Eukaryota.
DR GeneTree; ENSGT00940000155487; -.
DR InParanoid; Q66HC1; -.
DR OrthoDB; 914913at2759; -.
DR PhylomeDB; Q66HC1; -.
DR PRO; PR:Q66HC1; -.
DR Proteomes; UP000002494; Chromosome 15.
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; 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; SM00333; TUDOR; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50304; TUDOR; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..651
FT /note="Tudor domain-containing protein 3"
FT /id="PRO_0000342365"
FT DOMAIN 193..233
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 555..615
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 147..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..651
FT /note="EBM motif; may mediate interaction with the EJC"
FT /evidence="ECO:0000250"
FT COMPBIAS 170..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7E2"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H7E2"
SQ SEQUENCE 651 AA; 73028 MW; 226109C2519D3D59 CRC64;
MLRVQMTDGH TSCTAVEFSY ISKISLNTPP GTKVKLSGTV DIKNGFLLLS DSNTTVLGGE
VEHLIDKWAL QRSLLKHNRS NIGAEGGPPP FLPFGQKCAS TVQVDSRELD RRKTLQVSLP
AKPTNDNDEF EKQRTAAIAE VAKSKETKTF GGGGGGVRSH LNIGAGGHRN REVSQKEKAS
KSESKNEGVY RELVDEKALK HITEMGFSKE ASRQALMDNA NNLEAALNVL LNSSKQKPVV
GPPPRGRGKG RGRVRSEDEE DLGNARPSAP STLFDFLESK MGTLNMEEPR SQPQHLYQGQ
HRVSNTEQNG IKDGNQSRHL PRNDPRQPRN EKPPRFQRDT PNLKSALENS VLSRNRGSER
PSSSSGSDVW AEERIKCDRP YSRYDRTKDA SYPLGFQHND GAFKRRDNSM QNRSGRGPLY
AEAKENPHPS EFVDYNNQKR GKRENQTSNP DHFYDRKSRT MNSEAFSGLK IEKHFSANTD
YQNPVQSNSF VGVPNGETDM PMKGRRVGPI KPAGPVTAVP YDDKIFYNSG PKRRSGPIKP
EKVIESSIPV EYAKMWKPGD ECFALYWEDN KFYRAEVEAL HSSGMTAVVK FTDYGNYEEV
LLSNIKPVQT EAWEEEGTYD HTIEFRRGGD GQPRRSTRPT QQFYQPPRAR N
