TDRD3_XENTR
ID TDRD3_XENTR Reviewed; 710 AA.
AC Q6P1U3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Tudor domain-containing protein 3;
GN Name=tdrd3;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-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 -!- SEQUENCE CAUTION:
CC Sequence=AAH64868.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC064868; AAH64868.1; ALT_INIT; mRNA.
DR RefSeq; NP_989385.1; NM_204054.1.
DR AlphaFoldDB; Q6P1U3; -.
DR SMR; Q6P1U3; -.
DR STRING; 8364.ENSXETP00000063638; -.
DR PRIDE; Q6P1U3; -.
DR Ensembl; ENSXETT00000087476; ENSXETP00000098929; ENSXETG00000012815.
DR GeneID; 395019; -.
DR KEGG; xtr:395019; -.
DR CTD; 81550; -.
DR Xenbase; XB-GENE-949075; tdrd3.
DR eggNOG; KOG3683; Eukaryota.
DR InParanoid; Q6P1U3; -.
DR OrthoDB; 914913at2759; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000012815; Expressed in testis and 12 other tissues.
DR ExpressionAtlas; Q6P1U3; baseline.
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; Nucleus; Reference proteome.
FT CHAIN 1..710
FT /note="Tudor domain-containing protein 3"
FT /id="PRO_0000367250"
FT DOMAIN 250..290
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 617..677
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 206..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 79601 MW; DA9F235B1225F62E CRC64;
MLLIALNTDL RTTGKKFLPN DINGGKVEKV NGPCVLQIQK IRNISAPKDN EESQAAPRML
RLQLTDGHTS CTAIELNYLS KISLNTPPGT KIKLLGTIEV KNGYLLLDDT NTVVLGGEVE
HLIEKWELQR SLSKHSRSNI GIEGGPPPFV PFGQRCASVA SVDSKELDSR KTLQASSVTK
PVGENDEFEK QRTAAIAEVA KSKETKTFGG GGNAGSNLNP GAGGSRNKEV FQKEKIIRAE
GKSEGVYREL VDEKALRHIT EMGFSKDAAR QALMDHSNNV EAALNSLLTG NKSKPVQGPP
ARGKGKGRGR TRAEEDDELT SARPSAPSTL FDFLESKMGS FSIEDHKLQS QSQSQVHQKP
LNLEQNGIKD YNHKDYNQPR QFTRNDTRAP RNEKPPRFQK EIQASRQYEG NGPPKSRGSE
KQSSSVAEQW MEERNKCERG YPRNDRLKDF SHLPSSHQNE GSYKKSYTNP MQGRGMKGGN
HTEVKEEFHH QNSNTEGSHQ KRGKKDDQRY NSEFYTDRRA RTGNTETFTN IPNEKCFSAN
NELSNFQTIL IKDGANDLSN GEVDQKARRF GPIKPIGTNL NSSHEDKSKM FSYNNAKKRS
GPIKQERPLE AVYSGFSWRP GDECLALYWE DNKYYRAEVE ALHSSGTTAV VKFSDYGNYE
EVLLENIRPI QAEAWEEEGD FGDFRRGGDG QPRRSTRPTQ QFYQPPRARN
