ID   DDX27_MOUSE             Reviewed;         760 AA.
AC   Q921N6; Q3UUG2; Q8R0W3; Q8R1E2;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX27;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 27;
GN   Name=Ddx27;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Forelimb, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Eye, Mammary cancer, and Salivary gland;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-25, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-25, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Probable ATP-dependent RNA helicase. Component of the
CC       nucleolar ribosomal RNA (rRNA) processing machinery that regulates 3'
CC       end formation of ribosomal 47S rRNA. {ECO:0000250|UniProtKB:Q96GQ7}.
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   -!- SUBUNIT: Associates with PeBoW complex, composed of BOP1, PES1 and
CC       WDR12. Interacts directly with BOP1 and PES1.
CC       {ECO:0000250|UniProtKB:Q96GQ7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q96GQ7}. Chromosome
CC       {ECO:0000250|UniProtKB:Q96GQ7}. Note=Associates with 60S and 90S pre-
CC       ribosomal particles. {ECO:0000250|UniProtKB:Q96GQ7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q921N6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q921N6-2; Sequence=VSP_007073, VSP_007074;
CC   -!- DOMAIN: The C-terminal domain regulates nucleolar localization.
CC       {ECO:0000250|UniProtKB:Q96GQ7}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH11321.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK134274; BAE22077.1; -; mRNA.
DR   EMBL; AK138442; BAE23664.1; -; mRNA.
DR   EMBL; AL591711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466551; EDL06495.1; -; Genomic_DNA.
DR   EMBL; BC011321; AAH11321.1; ALT_INIT; mRNA.
DR   EMBL; BC024730; AAH24730.1; -; mRNA.
DR   EMBL; BC026381; AAH26381.1; -; mRNA.
DR   CCDS; CCDS38336.1; -. [Q921N6-1]
DR   RefSeq; NP_694705.2; NM_153065.3. [Q921N6-1]
DR   AlphaFoldDB; Q921N6; -.
DR   SMR; Q921N6; -.
DR   BioGRID; 230792; 40.
DR   CORUM; Q921N6; -.
DR   IntAct; Q921N6; 1.
DR   STRING; 10090.ENSMUSP00000018143; -.
DR   GlyGen; Q921N6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q921N6; -.
DR   PhosphoSitePlus; Q921N6; -.
DR   EPD; Q921N6; -.
DR   jPOST; Q921N6; -.
DR   MaxQB; Q921N6; -.
DR   PaxDb; 10090-ENSMUSP00000018143; -.
DR   PeptideAtlas; Q921N6; -.
DR   ProteomicsDB; 279849; -. [Q921N6-1]
DR   ProteomicsDB; 279850; -. [Q921N6-2]
DR   Pumba; Q921N6; -.
DR   Antibodypedia; 13624; 192 antibodies from 25 providers.
DR   DNASU; 228889; -.
DR   Ensembl; ENSMUST00000018143.16; ENSMUSP00000018143.10; ENSMUSG00000017999.17. [Q921N6-1]
DR   Ensembl; ENSMUST00000150571.2; ENSMUSP00000135265.2; ENSMUSG00000017999.17. [Q921N6-2]
DR   GeneID; 228889; -.
DR   KEGG; mmu:228889; -.
DR   UCSC; uc008nza.1; mouse. [Q921N6-2]
DR   UCSC; uc008nzb.1; mouse. [Q921N6-1]
DR   AGR; MGI:2385884; -.
DR   CTD; 55661; -.
DR   MGI; MGI:2385884; Ddx27.
DR   VEuPathDB; HostDB:ENSMUSG00000017999; -.
DR   eggNOG; KOG0338; Eukaryota.
DR   GeneTree; ENSGT00550000074997; -.
DR   HOGENOM; CLU_003041_3_3_1; -.
DR   InParanoid; Q921N6; -.
DR   OMA; CPTSRQT; -.
DR   OrthoDB; 149428at2759; -.
DR   PhylomeDB; Q921N6; -.
DR   TreeFam; TF314780; -.
DR   BioGRID-ORCS; 228889; 21 hits in 81 CRISPR screens.
DR   ChiTaRS; Ddx27; mouse.
DR   PRO; PR:Q921N6; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q921N6; Protein.
DR   Bgee; ENSMUSG00000017999; Expressed in ectoplacental cone and 263 other cell types or tissues.
DR   ExpressionAtlas; Q921N6; baseline and differential.
DR   GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR   CDD; cd17947; DEADc_DDX27; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   PANTHER; PTHR47959:SF14; DEAD-BOX ATP-DEPENDENT RNA HELICASE 28; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
DR   Genevisible; Q921N6; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Chromosome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..760
FT                   /note="Probable ATP-dependent RNA helicase DDX27"
FT                   /id="PRO_0000055032"
FT   DOMAIN          215..389
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          419..569
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           55..57
FT                   /note="Required for interaction with the PEBOW complex"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GQ7"
FT   MOTIF           157..166
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           184..212
FT                   /note="Q motif"
FT   MOTIF           337..340
FT                   /note="DEAD box"
FT   COMPBIAS        81..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..144
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..722
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..743
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         228..235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GQ7"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GQ7"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96GQ7"
FT   VAR_SEQ         292
FT                   /note="G -> E (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_007073"
FT   VAR_SEQ         293..760
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_007074"
FT   CONFLICT        341
FT                   /note="R -> K (in Ref. 4; AAH11321)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   760 AA;  85939 MW;  C351B13DAC1B1E0B CRC64;
     MLAELGFIRT IGENDEVPVE PESDSGDEEE EGPIVLGRKQ KALQKNRSAD FNPDFVFTEK
     EGMYDGSWAL ADVMSQLKKK RAATTLDEKI EKVRKRRKAE DKEAKSGKVE EKEGQADSDL
     KGQENPGEDE AGSKDEDSET DYSSEDEEIL TKADTLKVKE KKKKKKGQAA GGFFEDASEY
     DKSLSFQDMN LSRPLLKAIT AMGFKQPTPI QKACIPVGLL GKDICACAAT GTGKTAAFAL
     PVLERLIYKP RQAAVTRVLV LVPTRELGIQ VHSVTKQLAQ FCSITTCLAV GGLDVKSQEA
     ALRAAPDILI ATPGRLIDHL HNCPSFHLSS IEVLILDEAD RMLDEYFEEQ MKEIIRMCSH
     HRQTMLFSAT MTDEVKDLAS VSLKNPVRIF VNSNTDVAPF LRQEFIRIRP NREGDREAIV
     AALLMRTFTD HVMLFTQTKK QAHRMHILLG LLGLQVGELH GNLSQTQRLE ALRRFKDEQI
     DILVATDVAA RGLDIEGVKT VINFTMPNTV KHYVHRVGRT ARAGRAGRSV SLVGEEERKM
     LKEIVKAAKA PVKARILPQD VILKFRDKIE KLEKDVYAVL QLEAEEKEMQ QSEAQIDTAQ
     RLLAKGKETA DQEPERSWFQ TKEERKKEKI AKALQEFDLA LRGKKKRKKF MKDAKKKGEM
     TAEERSQFEI LKAQMFAERL AKRNRRTKRA RAMPEDEPTG PAKKQKQQQK SVFDEELTNT
     SKKALKQYRA GPSFEERKQS GLPRQRRGNF KSKSRYKRKK
//