TDRD3_MOUSE
ID TDRD3_MOUSE Reviewed; 743 AA.
AC Q91W18; E9Q2Q4; Q6NZG7; Q8BZW6; Q8C1A4;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Tudor domain-containing protein 3;
GN Name=Tdrd3;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 545-743 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Skin;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP STRUCTURE BY NMR OF 646-699.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the Tudor domain of Tudor domain containing protein
RT 3 from mouse.";
RL Submitted (JUN-2006) to the PDB data bank.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q91W18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91W18-2; Sequence=VSP_034485;
CC Name=3;
CC IsoId=Q91W18-3; Sequence=VSP_037054;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05670.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH66144.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC26033.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC28263.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK028617; BAC26033.1; ALT_INIT; mRNA.
DR EMBL; AK033390; BAC28263.1; ALT_INIT; mRNA.
DR EMBL; AC154562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005670; AAH05670.3; ALT_INIT; mRNA.
DR EMBL; BC066144; AAH66144.1; ALT_INIT; mRNA.
DR CCDS; CCDS27305.2; -. [Q91W18-1]
DR CCDS; CCDS56972.1; -. [Q91W18-2]
DR RefSeq; NP_001240684.1; NM_001253755.1. [Q91W18-2]
DR RefSeq; NP_766193.3; NM_172605.3. [Q91W18-1]
DR PDB; 2D9T; NMR; -; A=646-705.
DR PDBsum; 2D9T; -.
DR AlphaFoldDB; Q91W18; -.
DR BMRB; Q91W18; -.
DR SMR; Q91W18; -.
DR BioGRID; 230129; 13.
DR ComplexPortal; CPX-3302; TDRD3-TOP3B type IA topoisomerase complex. [Q91W18-1]
DR IntAct; Q91W18; 5.
DR MINT; Q91W18; -.
DR STRING; 10090.ENSMUSP00000129019; -.
DR iPTMnet; Q91W18; -.
DR PhosphoSitePlus; Q91W18; -.
DR EPD; Q91W18; -.
DR jPOST; Q91W18; -.
DR MaxQB; Q91W18; -.
DR PaxDb; Q91W18; -.
DR PeptideAtlas; Q91W18; -.
DR PRIDE; Q91W18; -.
DR ProteomicsDB; 262744; -. [Q91W18-1]
DR ProteomicsDB; 262745; -. [Q91W18-2]
DR ProteomicsDB; 262746; -. [Q91W18-3]
DR Antibodypedia; 24335; 148 antibodies from 23 providers.
DR DNASU; 219249; -.
DR Ensembl; ENSMUST00000168275; ENSMUSP00000129019; ENSMUSG00000022019. [Q91W18-1]
DR Ensembl; ENSMUST00000169504; ENSMUSP00000131542; ENSMUSG00000022019. [Q91W18-2]
DR Ensembl; ENSMUST00000170865; ENSMUSP00000126189; ENSMUSG00000022019. [Q91W18-3]
DR GeneID; 219249; -.
DR KEGG; mmu:219249; -.
DR UCSC; uc007uuf.3; mouse. [Q91W18-2]
DR UCSC; uc007uug.2; mouse. [Q91W18-1]
DR UCSC; uc011zpb.1; mouse. [Q91W18-3]
DR CTD; 81550; -.
DR MGI; MGI:2444023; Tdrd3.
DR VEuPathDB; HostDB:ENSMUSG00000022019; -.
DR eggNOG; KOG3683; Eukaryota.
DR GeneTree; ENSGT00940000155487; -.
DR HOGENOM; CLU_022646_0_0_1; -.
DR InParanoid; Q91W18; -.
DR OMA; IHNSENF; -.
DR OrthoDB; 914913at2759; -.
DR PhylomeDB; Q91W18; -.
DR TreeFam; TF316491; -.
DR BioGRID-ORCS; 219249; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Tdrd3; mouse.
DR EvolutionaryTrace; Q91W18; -.
DR PRO; PR:Q91W18; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q91W18; protein.
DR Bgee; ENSMUSG00000022019; Expressed in humerus cartilage element and 244 other tissues.
DR ExpressionAtlas; Q91W18; baseline and differential.
DR Genevisible; Q91W18; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0140225; C:DNA topoisomerase III-beta-TDRD3 complex; ISO:MGI.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0006265; P:DNA topological change; IC:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Cytoplasm;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..743
FT /note="Tudor domain-containing protein 3"
FT /id="PRO_0000183164"
FT DOMAIN 286..326
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 647..707
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 241..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..743
FT /note="EBM motif; may mediate interaction with the EJC"
FT /evidence="ECO:0000250"
FT COMPBIAS 343..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7E2"
FT CROSSLNK 563
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H7E2"
FT VAR_SEQ 1..14
FT /note="MAEVSGAALSQAGW -> MLFILFNR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037054"
FT VAR_SEQ 706..743
FT /note="EEEGTYDHTIEFRRGGDGQPRRSTRPTQQFYQPPRARN -> VRDPNSVQRL
FT L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034485"
FT CONFLICT 8
FT /note="A -> G (in Ref. 1; BAC28263)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="I -> V (in Ref. 3; AAH66144)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="E -> V (in Ref. 1; BAC28263)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="T -> M (in Ref. 3; AAH66144)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="G -> R (in Ref. 3; AAH66144)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="T -> S (in Ref. 3; AAH05670)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="K -> R (in Ref. 3; AAH05670)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="L -> F (in Ref. 3; AAH05670)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="V -> F (in Ref. 3; AAH05670)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="R -> S (in Ref. 3; AAH05670)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="A -> E (in Ref. 1; BAC28263)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="F -> L (in Ref. 3; AAH66144)"
FT /evidence="ECO:0000305"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:2D9T"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:2D9T"
FT STRAND 664..672
FT /evidence="ECO:0007829|PDB:2D9T"
FT STRAND 674..683
FT /evidence="ECO:0007829|PDB:2D9T"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:2D9T"
FT STRAND 689..693
FT /evidence="ECO:0007829|PDB:2D9T"
FT HELIX 694..696
FT /evidence="ECO:0007829|PDB:2D9T"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:2D9T"
SQ SEQUENCE 743 AA; 82253 MW; 23792E13FFE3A4B6 CRC64;
MAEVSGAALS QAGWYLSDEG VEACTSSPGK GSINDIILIA LNTDLRTIGK KFLPSDINGG
KVEKLEGPCV LQIQKVRNVA APKDNEESQA APRMLRVQMT DGHTSCTAVE FSYISKISLN
TPPGTKVKLS GTVDIKNGFL LLSDSNTTVL GGEVEHLIDK WALQRSLLKH NRSNIGAEGG
PPPFLPFGQK CASNVQVDSR ELDRRKTLQV SLPAKPANDN DEFEKQRTAA IAEVAKSKET
KTFGGGGGGA RSNLNIGAAG HRNREVLQKE KASKSESKNE GVYRELVDEK ALKHITEMGF
SKEASRQALM DNANNLEAAL NVLLNSSKQK PAVGPPARGR GKGRGRGRSE DEEDLGTARP
SAPSTLFDFL ESKMGTLNVE EPKSQPQHLH QGQHRGWNAE QNGMKDGTQS RHLPRNDTRQ
PRNERPPRFQ KDTPTSKSTV ENSVLSRNRG SERPSSSSGS DVWAEERIKC DRPYSRYDRT
KDASHPLGLQ HNDGAFKKRE NSMQNRPGRG PLYAEAKENP LPPEFVDYNN QRRGRRENQT
GHPDHCYERK PRTMNSEAVS GLKIEKHFSV NTDYPRPVQS NSLGVPNGET APPLKGRRVG
PIKSAGPVTA VPYDDKIFYN SGPKRRSGPI KPEKVIESSI PVEYAKVWKP GDECFALYWE
DNKFYRAEVE ALHSSGMTAV VKFTDYGNYE EVLLSNIKPV QTEAWEEEGT YDHTIEFRRG
GDGQPRRSTR PTQQFYQPPR ARN
