DDX31_MOUSE
ID DDX31_MOUSE Reviewed; 687 AA.
AC Q6NZQ2; A2AIT3; A3KMM3; Q3TLT4;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX31;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 31;
GN Name=Ddx31;
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 TISSUE=Mammary gland;
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase (By similarity). Plays a
CC role in ribosome biogenesis and TP53/p53 regulation through its
CC interaction with NPM1 (By similarity). {ECO:0000250|UniProtKB:Q9H8H2}.
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: Interacts with NPM1; the interaction prevents interaction
CC between NPM1 and HDM2. {ECO:0000250|UniProtKB:Q9H8H2}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9H8H2}. Note=Colocalized with NPM1 in the
CC nucleoli. {ECO:0000250|UniProtKB:Q9H8H2}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {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; AK166327; BAE38708.1; -; mRNA.
DR EMBL; AL732526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08399.1; -; Genomic_DNA.
DR EMBL; BC066017; AAH66017.2; -; mRNA.
DR EMBL; BC132351; AAI32352.2; -; mRNA.
DR CCDS; CCDS15848.1; -.
DR RefSeq; NP_001028466.2; NM_001033294.3.
DR AlphaFoldDB; Q6NZQ2; -.
DR SMR; Q6NZQ2; -.
DR STRING; 10090.ENSMUSP00000109484; -.
DR iPTMnet; Q6NZQ2; -.
DR PhosphoSitePlus; Q6NZQ2; -.
DR EPD; Q6NZQ2; -.
DR MaxQB; Q6NZQ2; -.
DR PaxDb; Q6NZQ2; -.
DR PeptideAtlas; Q6NZQ2; -.
DR PRIDE; Q6NZQ2; -.
DR ProteomicsDB; 279901; -.
DR Antibodypedia; 18198; 68 antibodies from 16 providers.
DR DNASU; 227674; -.
DR Ensembl; ENSMUST00000113853; ENSMUSP00000109484; ENSMUSG00000026806.
DR GeneID; 227674; -.
DR KEGG; mmu:227674; -.
DR UCSC; uc008izg.2; mouse.
DR CTD; 64794; -.
DR MGI; MGI:2682639; Ddx31.
DR VEuPathDB; HostDB:ENSMUSG00000026806; -.
DR eggNOG; KOG0348; Eukaryota.
DR GeneTree; ENSGT00550000075041; -.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; Q6NZQ2; -.
DR OMA; AVHIKAD; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q6NZQ2; -.
DR TreeFam; TF323273; -.
DR BioGRID-ORCS; 227674; 18 hits in 75 CRISPR screens.
DR PRO; PR:Q6NZQ2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6NZQ2; protein.
DR Bgee; ENSMUSG00000026806; Expressed in lumbar dorsal root ganglion and 165 other tissues.
DR Genevisible; Q6NZQ2; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042254; P:ribosome biogenesis; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..687
FT /note="Probable ATP-dependent RNA helicase DDX31"
FT /id="PRO_0000434575"
FT DOMAIN 135..316
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 344..523
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 103..132
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 261..264
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 38
FT /note="K -> R (in Ref. 1; BAE38708)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="V -> A (in Ref. 1; BAE38708)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="V -> I (in Ref. 1; BAE38708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 76913 MW; 32967D263CD398BB CRC64;
MKRQAEATKR KHQVSSDAPP AKRRSEISSV LAKKASDKET QRTFKGSTHK TFPPKKYLDS
IGNGRQEEKP CIKTSSLFKN NPEIPELHST VVKQAREQVF SPEAFQELDL HPHLISTINT
VLKMSSMTSV QKQSIPVLLE GRDALVRSQT GSGKTLAYCV PVVQSLQALT SKIQRSDGPY
ALVLVPTREL ALQSFDTVQK LLKPFTWIVP GVLMGGEKRK SEKARLRKGI NILISTPGRL
VDHIKSTKNL HFNRIRWLIV DEADRILDLG FEKDITVILN AVNAECQKRQ NVLLSATLTE
GVTRLVDISL HNPVSISVLD KNCNQPNPKE VASIQLNSFA IPESLDQHVV LVPSKLRLVC
LAAFILQKCK FEKNQKMIVF FSSCELVEFH YSLFLHTLLC HSGTPTSEHL PSASWPLKFL
RLHGNMEQEE RTSVFHEFSH SETGVLLCTD VASRGLDLPQ VTWIVQYSAP SSPAEYIHRI
GRTARIGCHG SSLLILAPSE AEYVNSLASH KINVGEIKME DILAVLAKDD CFKRRQRGAQ
KSRASGPQEI RERATVLQTV FEDYVHSSQR MVSWAKKALQ SFIRAYATYP KELKSIFHVR
ALHLGHVAKS FGLRDAPRNL SVSAVKKASL KRPHPRRKTQ RKQHLVPAEV LHSEHSSGLE
GGATKCRKQG KQQGLQVAPS KPGPWRE
