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Database: UniProt
Entry: Q3B8Q1
LinkDB: Q3B8Q1
Original site: Q3B8Q1 
ID   DDX21_RAT               Reviewed;         782 AA.
AC   Q3B8Q1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   13-NOV-2019, entry version 121.
DE   RecName: Full=Nucleolar RNA helicase 2 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9NR30};
DE   AltName: Full=DEAD box protein 21;
DE   AltName: Full=Gu-alpha;
DE   AltName: Full=Nucleolar RNA helicase Gu;
DE   AltName: Full=Nucleolar RNA helicase II;
DE   AltName: Full=RH II/Gu;
GN   Name=Ddx21; Synonyms=Ddx21a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: RNA helicase that acts as a sensor of the
CC       transcriptional status of both RNA polymerase (Pol) I and II:
CC       promotes ribosomal RNA (rRNA) processing and transcription from
CC       polymerase II (Pol II). Binds various RNAs, such as rRNAs,
CC       snoRNAs, 7SK and, at lower extent, mRNAs. In the nucleolus,
CC       localizes to rDNA locus, where it directly binds rRNAs and
CC       snoRNAs, and promotes rRNA transcription, processing and
CC       modification. Required for rRNA 2'-O-methylation, possibly by
CC       promoting the recruitment of late-acting snoRNAs SNORD56 and
CC       SNORD58 with pre-ribosomal complexes. In the nucleoplasm, binds
CC       7SK RNA and is recruited to the promoters of Pol II-transcribed
CC       genes: acts by facilitating the release of P-TEFb from inhibitory
CC       7SK snRNP in a manner that is dependent on its helicase activity,
CC       thereby promoting transcription of its target genes. Functions as
CC       cofactor for JUN-activated transcription: required for
CC       phosphorylation of JUN at 'Ser-77'. Can unwind double-stranded RNA
CC       (helicase) and can fold or introduce a secondary structure to a
CC       single-stranded RNA (foldase). Involved in rRNA processing. May
CC       bind to specific miRNA hairpins (By similarity). Component of a
CC       multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of
CC       viral double-stranded RNA (dsRNA) and plays a role in the
CC       activation of a cascade of antiviral responses including the
CC       induction of proinflammatory cytokines via the adapter molecule
CC       TICAM1 (By similarity). {ECO:0000250|UniProtKB:Q9JIK5,
CC       ECO:0000250|UniProtKB:Q9NR30}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000250|UniProtKB:Q9NR30};
CC   -!- SUBUNIT: Homodimer; homodimerizes via its N-terminus. Found in a
CC       multi-helicase-TICAM1 complex at least composed of DHX36, DDX1,
CC       DDX21 and TICAM1; this complex exists in resting cells with or
CC       without poly(I:C) RNA ligand stimulation. Interacts (via C-
CC       terminus) with TICAM1 (via TIR domain). Interacts with DHX36 (via
CC       C-terminus); this interaction serves as bridges to TICAM1.
CC       Interacts (via C-terminus) with DDX1 (via B30.2/SPRY domain); this
CC       interaction serves as bridges to TICAM1 (By similarity). Component
CC       of the B-WICH complex, at least composed of SMARCA5/SNF2H,
CC       BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts
CC       with C1QBP. Interacts with JUN. Interacts with WDR46. Interacts
CC       with MCM3AP (By similarity). Interacts with WDR43 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9JIK5, ECO:0000250|UniProtKB:Q9NR30}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9NR30}. Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q9NR30}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9JIK5}. Mitochondrion
CC       {ECO:0000250|UniProtKB:Q9JIK5}. Note=Present both in nucleolus and
CC       nucleoplasm. Interaction with JUN promotes translocation from the
CC       nucleolus to the nucleoplasm. Interaction with WDR46 is required
CC       for localization to the nucleolus. Colocalizes in the cytosol with
CC       DDX1, DHX36 and TICAM1. The multi-helicase-TICAM1 complex may
CC       translocate to the mitochondria upon poly(I:C) RNA ligand
CC       stimulation (By similarity). {ECO:0000250|UniProtKB:Q9JIK5,
CC       ECO:0000250|UniProtKB:Q9NR30}.
CC   -!- DOMAIN: The helicase and foldase activities reside in two separate
CC       domains, the helicase in the N-terminus and the foldase in the C-
CC       terminus. {ECO:0000250|UniProtKB:Q9NR30}.
CC   -!- DOMAIN: The 3 X 5 AA repeats seem to be critical for the RNA
CC       folding activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC       subfamily. {ECO:0000305}.
DR   EMBL; BC105878; AAI05879.1; -; mRNA.
DR   RefSeq; NP_001032278.1; NM_001037201.1.
DR   SMR; Q3B8Q1; -.
DR   IntAct; Q3B8Q1; 1.
DR   STRING; 10116.ENSRNOP00000063494; -.
DR   iPTMnet; Q3B8Q1; -.
DR   PhosphoSitePlus; Q3B8Q1; -.
DR   jPOST; Q3B8Q1; -.
DR   PaxDb; Q3B8Q1; -.
DR   PRIDE; Q3B8Q1; -.
DR   Ensembl; ENSRNOT00000068184; ENSRNOP00000063494; ENSRNOG00000043099.
DR   GeneID; 317399; -.
DR   KEGG; rno:317399; -.
DR   UCSC; RGD:1307306; rat.
DR   CTD; 9188; -.
DR   RGD; 1307306; Ddx21.
DR   eggNOG; KOG0331; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   GeneTree; ENSGT00940000155043; -.
DR   HOGENOM; HOG000268805; -.
DR   InParanoid; Q3B8Q1; -.
DR   KO; K16911; -.
DR   OMA; LPCNRAA; -.
DR   OrthoDB; 1139373at2759; -.
DR   PhylomeDB; Q3B8Q1; -.
DR   TreeFam; TF328622; -.
DR   Reactome; R-RNO-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q3B8Q1; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000043099; Expressed in 10 organ(s), highest expression level in spleen.
DR   Genevisible; Q3B8Q1; RN.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097322; F:7SK snRNA binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR   GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR012562; GUCT.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08152; GUCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Antiviral defense; ATP-binding; Complete proteome;
KW   Cytoplasm; Helicase; Hydrolase; Immunity; Innate immunity;
KW   Isopeptide bond; Mitochondrion; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW   rRNA processing; Transcription; Ubl conjugation.
FT   CHAIN         1    782       Nucleolar RNA helicase 2.
FT                                /FTId=PRO_0000282712.
FT   DOMAIN      213    392       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      425    569       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   REPEAT      720    724       1.
FT   REPEAT      731    735       2.
FT   REPEAT      741    747       3.
FT   NP_BIND     226    233       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION      720    747       3 X 5 AA repeats.
FT   MOTIF       182    210       Q motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00552}.
FT   MOTIF       335    338       DEAD box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOD_RES       7      7       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NR30}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NR30}.
FT   MOD_RES      39     39       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9JIK5}.
FT   MOD_RES     119    119       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NR30}.
FT   MOD_RES     145    145       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9JIK5}.
FT   MOD_RES     169    169       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9JIK5}.
FT   MOD_RES     292    292       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9NR30}.
FT   MOD_RES     563    563       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NR30}.
FT   MOD_RES     778    778       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9NR30}.
FT   CROSSLNK    114    114       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q9NR30}.
FT   CROSSLNK    114    114       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q9NR30}.
SQ   SEQUENCE   782 AA;  85966 MW;  FD8074E373921621 CRC64;
     MPGKLRSASK SESEGTEESM ETLQKPSEKK TRKEKPKSKT DEATEGVEEA ASSKVKAVKK
     KGPSEDDVGP PKSKKAKKQE EEPQDDPASK SKTSKKKKEP LEKKAPSAKT KEMKAEEPSE
     EEADAPKPKK TKKGKEANGD VGEKSPGLKN GLSHPKPDSS STQAPGEESE TEKEIPVEQK
     EGAFSNFPIS EETVKLLKAR GVNFLFPIQA KTFHHVYSGK DLIAQARTGT GKTFSFAIPL
     IEKLQGGLQE RKRGRAPQVL VLAPTRELAN QVSKDFSDIT KKLSVACFYG GTPYGGQIER
     MRSGIDILVG TPGRIKDHLQ NGKLDLTKLK HVVLDEVDQM LDMGFADQVE EILCVAYKKD
     SEDNPQTLLF SATCPHWVFN VAKKYMKSTY EQVDLIGKKT QKAAITVEHL AIKCHWTERA
     AVIGDVIRVY SGHQGRTIIF CETKKDAQEL SQNTCIKQDA QSLHGDIPQK QREITLKGFR
     NGNFGVLVAT NVAARGLDIP EVDLVVQSCP PKDVESYIHR SGRTGRAGRT GVCICFYQHK
     EEYQLAQVEQ KAGIKFKRIG VPSATEIIKA SSKDAIRLLD SVPPTAIGHF KQSAEKLIEE
     KGAVEALAAA LAHISGATSV DQRSLINSQA GFVTMILRCS VEMPNISYAW KELKEQLGES
     IDAKVKGMVF LKGKLGVCFD VRTEAVTEIK EKWHDSRRWQ LTVATEQPEL EGPPEGYRGG
     RGQRDGSRGS FRGQRGGSRN FRGQGQRGGS RNFRGQRPGG GNKSNRSPNK GQKRSFSKAF
     GQ
//
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