LOCUS       NP_001032278             782 aa            linear   ROD 27-APR-2025
DEFINITION  nucleolar RNA helicase 2 [Rattus norvegicus].
ACCESSION   NP_001032278 XP_228810
VERSION     NP_001032278.1
DBSOURCE    REFSEQ: accession NM_001037201.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 782)
  AUTHORS   Song,C., Hotz-Wagenblatt,A., Voit,R. and Grummt,I.
  TITLE     SIRT7 and the DEAD-box helicase DDX21 cooperate to resolve genomic
            R loops and safeguard genome stability
  JOURNAL   Genes Dev 31 (13), 1370-1381 (2017)
   PUBMED   28790157
REFERENCE   2  (residues 1 to 782)
  AUTHORS   Treiber,T., Treiber,N., Plessmann,U., Harlander,S., Daiss,J.L.,
            Eichner,N., Lehmann,G., Schall,K., Urlaub,H. and Meister,G.
  TITLE     A Compendium of RNA-Binding Proteins that Regulate MicroRNA
            Biogenesis
  JOURNAL   Mol Cell 66 (2), 270-284 (2017)
   PUBMED   28431233
REFERENCE   3  (residues 1 to 782)
  AUTHORS   Calo,E., Flynn,R.A., Martin,L., Spitale,R.C., Chang,H.Y. and
            Wysocka,J.
  TITLE     RNA helicase DDX21 coordinates transcription and ribosomal RNA
            processing
  JOURNAL   Nature 518 (7538), 249-253 (2015)
   PUBMED   25470060
REFERENCE   4  (residues 1 to 782)
  AUTHORS   Baltz,A.G., Munschauer,M., Schwanhausser,B., Vasile,A.,
            Murakawa,Y., Schueler,M., Youngs,N., Penfold-Brown,D., Drew,K.,
            Milek,M., Wyler,E., Bonneau,R., Selbach,M., Dieterich,C. and
            Landthaler,M.
  TITLE     The mRNA-bound proteome and its global occupancy profile on
            protein-coding transcripts
  JOURNAL   Mol Cell 46 (5), 674-690 (2012)
   PUBMED   22681889
REFERENCE   5  (residues 1 to 782)
  AUTHORS   Castello,A., Fischer,B., Eichelbaum,K., Horos,R., Beckmann,B.M.,
            Strein,C., Davey,N.E., Humphreys,D.T., Preiss,T., Steinmetz,L.M.,
            Krijgsveld,J. and Hentze,M.W.
  TITLE     Insights into RNA biology from an atlas of mammalian mRNA-binding
            proteins
  JOURNAL   Cell 149 (6), 1393-1406 (2012)
   PUBMED   22658674
REFERENCE   6  (residues 1 to 782)
  AUTHORS   Zhang,Z., Kim,T., Bao,M., Facchinetti,V., Jung,S.Y., Ghaffari,A.A.,
            Qin,J., Cheng,G. and Liu,Y.J.
  TITLE     DDX1, DDX21, and DHX36 helicases form a complex with the adaptor
            molecule TRIF to sense dsRNA in dendritic cells
  JOURNAL   Immunity 34 (6), 866-878 (2011)
   PUBMED   21703541
REFERENCE   7  (residues 1 to 782)
  AUTHORS   Ghosh,D., Lippert,D., Krokhin,O., Cortens,J.P. and Wilkins,J.A.
  TITLE     Defining the membrane proteome of NK cells
  JOURNAL   J Mass Spectrom 45 (1), 1-25 (2010)
   PUBMED   19946888
REFERENCE   8  (residues 1 to 782)
  AUTHORS   Foster,L.J., Zeemann,P.A., Li,C., Mann,M., Jensen,O.N. and
            Kassem,M.
  TITLE     Differential expression profiling of membrane proteins by
            quantitative proteomics in a human mesenchymal stem cell line
            undergoing osteoblast differentiation
  JOURNAL   Stem Cells 23 (9), 1367-1377 (2005)
   PUBMED   16210410
REFERENCE   9  (residues 1 to 782)
  AUTHORS   Valdez,B.C., Henning,D., Perumal,K. and Busch,H.
  TITLE     RNA-unwinding and RNA-folding activities of RNA helicase II/Gu--two
            activities in separate domains of the same protein
  JOURNAL   Eur J Biochem 250 (3), 800-807 (1997)
   PUBMED   9461305
REFERENCE   10 (residues 1 to 782)
  AUTHORS   Sykes,D.E. and Weiser,M.M.
  TITLE     The identification of genes specifically expressed in epithelial
            cells of the rat intestinal crypts
  JOURNAL   Differentiation 50 (1), 41-46 (1992)
   PUBMED   1639225
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC105878.1.
            
            On Nov 18, 2005 this sequence version replaced XP_228810.3.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC105878.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMD00132261,
                                           SAMD00132262 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..782
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="20"
                     /map="20q11"
     Protein         1..782
                     /product="nucleolar RNA helicase 2"
                     /EC_number="3.6.4.13"
                     /note="RH II/Gu; gu-alpha; DEAD box protein 21; nucleolar
                     RNA helicase Gu; nucleolar RNA helicase II; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 21; DEAD
                     (Asp-Glu-Ala-Asp) box polypeptide 21a; DEAD-box helicase
                     21; DEAD (Asp-Glu-Ala-Asp) box polypeptide 21b; DEAD
                     (Asp-Glu-Ala-Asp) box helicase 21"
                     /calculated_mol_wt=85835
     Region          1..184
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            7
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            39
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            135
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            145
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            169
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9JIK5; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Region          182..210
                     /region_name="Q motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00552"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Region          184..570
                     /region_name="SrmB"
                     /note="Superfamily II DNA and RNA helicase [Replication,
                     recombination and repair]; COG0513"
                     /db_xref="CDD:440279"
     Site            292
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Region          335..338
                     /region_name="DEAD box.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00541"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            563
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            596
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Region          613..705
                     /region_name="GUCT_RHII_Gualpha_beta"
                     /note="RNA-binding GUCT domain found in vertebrate RNA
                     helicase II/Gualpha (RH-II/Gualpha), RNA helicase
                     II/Gubeta (RH-II/Gubeta) and similar proteins; cd12936"
                     /db_xref="CDD:240593"
     Region          704..782
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Region          716..>765
                     /region_name="AdoMet_MTases"
                     /note="S-adenosylmethionine-dependent methyltransferases
                     (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes
                     that use S-adenosyl-L-methionine (SAM or AdoMet) as a
                     substrate for methyltransfer, creating the product
                     S-adenosyl-L-homocysteine (AdoHcy); cl17173"
                     /db_xref="CDD:473071"
     Region          720..747
                     /region_name="3 X 5 AA repeats"
                     /note="propagated from UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     Site            778
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q9NR30; propagated from
                     UniProtKB/Swiss-Prot (Q3B8Q1.1)"
     CDS             1..782
                     /gene="Ddx21"
                     /gene_synonym="Ddx21a; Ddx21b"
                     /coded_by="NM_001037201.1:45..2393"
                     /db_xref="GeneID:317399"
                     /db_xref="RGD:1307306"
ORIGIN      
        1 mpgklrsask sesegteesm etlqkpsekk trkekpkskt deategveea asskvkavkk
       61 kgpseddvgp pkskkakkqe eepqddpask sktskkkkep lekkapsakt kemkaeepse
      121 eeadapkpkk tkkgkeangd vgekspglkn glshpkpdss stqapgeese tekeipveqk
      181 egafsnfpis eetvkllkar gvnflfpiqa ktfhhvysgk dliaqartgt gktfsfaipl
      241 ieklqgglqe rkrgrapqvl vlaptrelan qvskdfsdit kklsvacfyg gtpyggqier
      301 mrsgidilvg tpgrikdhlq ngkldltklk hvvldevdqm ldmgfadqve eilcvaykkd
      361 sednpqtllf satcphwvfn vakkymksty eqvdligkkt qkaaitvehl aikchwtera
      421 avigdvirvy sghqgrtiif cetkkdaqel sqntcikqda qslhgdipqk qreitlkgfr
      481 ngnfgvlvat nvaargldip evdlvvqscp pkdvesyihr sgrtgragrt gvcicfyqhk
      541 eeyqlaqveq kagikfkrig vpsateiika sskdairlld svpptaighf kqsaekliee
      601 kgavealaaa lahisgatsv dqrslinsqa gfvtmilrcs vempnisyaw kelkeqlges
      661 idakvkgmvf lkgklgvcfd vrteavteik ekwhdsrrwq ltvateqpel egppegyrgg
      721 rgqrdgsrgs frgqrggsrn frgqgqrggs rnfrgqrpgg gnksnrspnk gqkrsfskaf
      781 gq
//
