DDX27_MOUSE
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 03-AUG-2022, entry version 155.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 iPTMnet; Q921N6; -.
DR PhosphoSitePlus; Q921N6; -.
DR EPD; Q921N6; -.
DR jPOST; Q921N6; -.
DR MaxQB; Q921N6; -.
DR PaxDb; Q921N6; -.
DR PeptideAtlas; Q921N6; -.
DR PRIDE; Q921N6; -.
DR ProteomicsDB; 279849; -. [Q921N6-1]
DR ProteomicsDB; 279850; -. [Q921N6-2]
DR Antibodypedia; 13624; 180 antibodies from 26 providers.
DR DNASU; 228889; -.
DR Ensembl; ENSMUST00000018143; ENSMUSP00000018143; ENSMUSG00000017999. [Q921N6-1]
DR Ensembl; ENSMUST00000150571; ENSMUSP00000135265; ENSMUSG00000017999. [Q921N6-2]
DR GeneID; 228889; -.
DR KEGG; mmu:228889; -.
DR UCSC; uc008nza.1; mouse. [Q921N6-2]
DR UCSC; uc008nzb.1; mouse. [Q921N6-1]
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; AAHTDIR; -.
DR OrthoDB; 268859at2759; -.
DR PhylomeDB; Q921N6; -.
DR TreeFam; TF314780; -.
DR BioGRID-ORCS; 228889; 20 hits in 75 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 260 other tissues.
DR ExpressionAtlas; Q921N6; baseline and differential.
DR Genevisible; Q921N6; MM.
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 Gene3D; 3.40.50.300; -; 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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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.
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
