TDRD3_CHICK
ID TDRD3_CHICK Reviewed; 741 AA.
AC Q5ZMS6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Tudor domain-containing protein 3;
GN Name=TDRD3; ORFNames=RCJMB04_1e24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
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DR EMBL; AJ719308; CAG30967.1; -; mRNA.
DR RefSeq; NP_001025993.1; NM_001030822.1.
DR AlphaFoldDB; Q5ZMS6; -.
DR SMR; Q5ZMS6; -.
DR STRING; 9031.ENSGALP00000035723; -.
DR PaxDb; Q5ZMS6; -.
DR GeneID; 418823; -.
DR KEGG; gga:418823; -.
DR CTD; 81550; -.
DR VEuPathDB; HostDB:geneid_418823; -.
DR eggNOG; KOG3683; Eukaryota.
DR InParanoid; Q5ZMS6; -.
DR OrthoDB; 914913at2759; -.
DR PhylomeDB; Q5ZMS6; -.
DR PRO; PR:Q5ZMS6; -.
DR Proteomes; UP000000539; 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: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; 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 2: Evidence at transcript level;
KW Chromatin regulator; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..741
FT /note="Tudor domain-containing protein 3"
FT /id="PRO_0000367247"
FT DOMAIN 286..326
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 644..704
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 326..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 83806 MW; 56AAEAD54B956698 CRC64;
MADRARAALS ESGWYLSDEG IETCINSSEK VNTNDIILVA LNTDLRTIGK KFLPSDINGG
KVEKLEGPCV LQIQKIRNVS APKDNEESQA APRMLRLQMT DGHTSCTAIE YNSMSKISLN
TPPGTKIKLS GIIEVRNGFL LLDDSNTAVL GGEVEHLIEK WELQRSLAKH SRSNIGTEGG
PPPFLPFGQK CASHMQVDSR ELDRRKTLQM TNTAKPVTDN DEFEKQRTAA IAEVAKSKET
KTFGGGGGSS RSNLTVSAGG NRNRELFQKE KITKPEGKNE GVYRELVDEK ALKHITEMGF
SKEAARQALM DNSNNLEAAL NFLLSSNKQK PLQGPPPRGK GKGRGRIRPE DEEELGNARP
SAPSTLFDFL ESKMGTLTVE EPKLQFQPPH QVQPKVMNTE QNGIKENHSR HISRNDMRQP
RNEKPPRFQR DIQNSRQALE SGGLPRNRGP ERHNSLEHWT DEKIKSDRHY PRNDRPKDLG
YPIAAHQSDI SFKKRDNNMQ NRIGKGVSFT EFKENSAAQD ATDNNNQKRG KRENQIHNSE
NFCDRKARTI SNETFMVKSE QHFGVNNDYQ NPCRTDNFNS IPNGDTEHHQ KGRRVGPIKL
SGPTVIPSYD DKILYYNTGP KRRSGPIKPE KIMEPSIHAE YGKTWRPGDE CFALYWEDNK
FYRAEVEALH SSGMTAVVKF SDYGNYEEVL LSNIRPIHAD TWEDEEETYE QTLEFRRGGD
GQPRRSTRPT QQFYQPPRAR N
