TDRD3_XENLA
ID TDRD3_XENLA Reviewed; 650 AA.
AC Q6NRP6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Tudor domain-containing protein 3;
GN Name=tdrd3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC070694; AAH70694.1; -; mRNA.
DR RefSeq; NP_001084774.1; NM_001091305.1.
DR AlphaFoldDB; Q6NRP6; -.
DR SMR; Q6NRP6; -.
DR BioGRID; 101176; 1.
DR IntAct; Q6NRP6; 1.
DR DNASU; 431810; -.
DR GeneID; 431810; -.
DR KEGG; xla:431810; -.
DR CTD; 431810; -.
DR Xenbase; XB-GENE-949081; tdrd3.L.
DR OrthoDB; 914913at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 431810; Expressed in lung and 19 other tissues.
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; 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; 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..650
FT /note="Tudor domain-containing protein 3"
FT /id="PRO_0000367249"
FT DOMAIN 192..232
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 554..614
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 147..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 72626 MW; 440A0D14399545AC CRC64;
MLRVQLTDGH TSCTAVELNH LSKISLNTPP GTKIKLLGTI EVKNGYLLLD DTNTVVLGGE
VEHLIEKWEL QRSLSKHSRS NIGIEGGPPP FVPFGQRCAS VASVDSKELD SRKTLQASSV
TKAVGENDEF EKQRTAAIAE VAKSKETKTF GGGGNAGSNL NPGAGGSRNR EVFQKEKIIR
AEGKSEGVYR ELVDEKALRH ITEMGFCKDA ARQALMDHSN NVEAALNFLL TGSKPKVVQG
PPPRGKGKGR GRTRGEEDDE LTSARPSAPS TLFDFLESKM GSFSIEDNKS HSQAQSQTHP
KALNLEQNGI KDYNQPRQFT RNDTRAPRNE KPPRFQKEIQ ASRQYEGNGP PKSRGPEKQS
SSVAEHWMED RNKCERGYPR NDRLKDFSHP PSNHQNEGSY RKSCNNPMQS RGIKGGNHTE
VKVEFHHQNS TTEGSHQKRG KKDDQRYNSE FYTDRRARTG NNETVASTPN EKCFSANNEL
SNFQTILIKE GANDLSNGEV DQKARRFGPI KPIGTNLNST HDDKSKMFSY NNTKKKSGSI
KPDKPLEAVY SGFSWRSGDE CLALYWEDNK YYRAEVEALH SSGTTAVVKF SDYGNYEEVL
LENIRPIQAE AWEEEGEFGD SLDFRRGGDG QPRRSTRPTQ QFYQPPRARN
