DHX33_MOUSE
ID DHX33_MOUSE Reviewed; 698 AA.
AC Q80VY9; Q8BS50;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ATP-dependent RNA helicase DHX33 {ECO:0000305};
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 33;
GN Name=Dhx33 {ECO:0000312|MGI:MGI:2445102};
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=Embryo;
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 MRNA].
RC TISSUE=Embryonic limb;
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 [3]
RP FUNCTION, INTERACTION WITH UBTF, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-94.
RX PubMed=21930779; DOI=10.1128/mcb.05832-11;
RA Zhang Y., Forys J.T., Miceli A.P., Gwinn A.S., Weber J.D.;
RT "Identification of DHX33 as a mediator of rRNA synthesis and cell growth.";
RL Mol. Cell. Biol. 31:4676-4691(2011).
RN [4]
RP FUNCTION, DOUBLE-STRANDED RNA-BINDING, AND INTERACTION WITH MAVS.
RX PubMed=24037184; DOI=10.1038/cmi.2013.40;
RA Liu Y., Lu N., Yuan B., Weng L., Wang F., Liu Y.J., Zhang Z.;
RT "The interaction between the helicase DHX33 and IPS-1 as a novel pathway to
RT sense double-stranded RNA and RNA viruses in myeloid dendritic cells.";
RL Cell. Mol. Immunol. 11:49-57(2014).
RN [5]
RP FUNCTION, MUTAGENESIS OF LYS-94, AND INTERACTION WITH DDX3X; EIF3G; EIF3H;
RP RPL3; RPL7; RPL26 AND RPL27.
RX PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA Zhang Y., You J., Wang X., Weber J.;
RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL Mol. Cell. Biol. 35:2918-2931(2015).
RN [6]
RP UBIQUITINATION, AND DEUBIQUITINATION BY USP36.
RX PubMed=29273634; DOI=10.1074/jbc.m117.788430;
RA Fraile J.M., Campos-Iglesias D., Rodriguez F., Astudillo A.,
RA Vilarrasa-Blasi R., Verdaguer-Dot N., Prado M.A., Paulo J.A., Gygi S.P.,
RA Martin-Subero J.I., Freije J.M.P., Lopez-Otin C.;
RT "Loss of the deubiquitinase USP36 destabilizes the RNA helicase DHX33 and
RT causes preimplantation lethality in mice.";
RL J. Biol. Chem. 293:2183-2194(2018).
CC -!- FUNCTION: Implicated in nucleolar organization, ribosome biogenesis,
CC protein synthesis and cytoplasmic dsRNA sensing (By similarity)
CC (PubMed:21930779). Stimulates RNA polymerase I transcription of the 47S
CC precursor rRNA. Associates with ribosomal DNA (rDNA) loci where it is
CC involved in POLR1A recruitment (PubMed:21930779). In the cytoplasm,
CC promotes elongation-competent 80S ribosome assembly at the late stage
CC of mRNA translation initiation (PubMed:26100019). Senses cytosolic
CC dsRNA mediating NLRP3 inflammasome formation in macrophages and type I
CC interferon production in myeloid dendritic cells (By similarity).
CC Required for NLRP3 activation induced by viral dsRNA and bacterial RNA
CC (By similarity). In dendritic cells, required for induction of type I
CC interferon production induced by cytoplasmic dsRNA via the activation
CC of MAPK and NF-kappa-B signaling pathways (PubMed:24037184).
CC {ECO:0000250|UniProtKB:Q9H6R0, ECO:0000269|PubMed:21930779,
CC ECO:0000269|PubMed:24037184, ECO:0000269|PubMed:26100019}.
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 UBTF (PubMed:21930779). Interacts with DDX3X,
CC EIF3G and EIF3H; the interaction is independent of RNA
CC (PubMed:26100019). Interacts (via HA2 region and Helicase C-terminal
CC domain) with the components of the large ribosomal subunit RPL3, RPL7,
CC RPL26 and RPL27 (PubMed:26100019). Binds to mRNA (PubMed:26100019).
CC Interacts (via the helicase C-terminal domain) with MAVS
CC (PubMed:24037184). Binds to double-stranded RNA (via the helicase C-
CC terminal domain) (PubMed:24037184). {ECO:0000269|PubMed:21930779,
CC ECO:0000269|PubMed:24037184, ECO:0000269|PubMed:26100019}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21930779}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H6R0}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H6R0}. Nucleus {ECO:0000250|UniProtKB:Q9H6R0}.
CC Inflammasome {ECO:0000250|UniProtKB:Q9H6R0}. Note=Predominantly in the
CC nucleolus. During mitosis, localizes with the nucleolar organizing
CC regions. Upon dsRNA-binding, localizes in the inflammasome.
CC {ECO:0000250|UniProtKB:Q9H6R0}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome
CC (PubMed:29273634). Deubiquitinated by USP36 (PubMed:29273634).
CC {ECO:0000269|PubMed:29273634}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; AK035177; BAC28969.1; -; mRNA.
DR EMBL; BC052172; AAH52172.1; -; mRNA.
DR CCDS; CCDS24971.1; -.
DR RefSeq; NP_848144.3; NM_178367.4.
DR AlphaFoldDB; Q80VY9; -.
DR SMR; Q80VY9; -.
DR BioGRID; 229816; 4.
DR STRING; 10090.ENSMUSP00000104167; -.
DR iPTMnet; Q80VY9; -.
DR PhosphoSitePlus; Q80VY9; -.
DR EPD; Q80VY9; -.
DR jPOST; Q80VY9; -.
DR MaxQB; Q80VY9; -.
DR PaxDb; Q80VY9; -.
DR PeptideAtlas; Q80VY9; -.
DR PRIDE; Q80VY9; -.
DR ProteomicsDB; 279531; -.
DR Antibodypedia; 23699; 81 antibodies from 11 providers.
DR DNASU; 216877; -.
DR Ensembl; ENSMUST00000108527; ENSMUSP00000104167; ENSMUSG00000040620.
DR GeneID; 216877; -.
DR KEGG; mmu:216877; -.
DR UCSC; uc007jxg.1; mouse.
DR CTD; 56919; -.
DR MGI; MGI:2445102; Dhx33.
DR VEuPathDB; HostDB:ENSMUSG00000040620; -.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00940000156747; -.
DR HOGENOM; CLU_001832_5_11_1; -.
DR InParanoid; Q80VY9; -.
DR OMA; HIHRTTP; -.
DR OrthoDB; 354219at2759; -.
DR PhylomeDB; Q80VY9; -.
DR TreeFam; TF354245; -.
DR BioGRID-ORCS; 216877; 29 hits in 76 CRISPR screens.
DR ChiTaRS; Dhx33; mouse.
DR PRO; PR:Q80VY9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q80VY9; protein.
DR Bgee; ENSMUSG00000040620; Expressed in embryonic post-anal tail and 229 other tissues.
DR ExpressionAtlas; Q80VY9; baseline and differential.
DR Genevisible; Q80VY9; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0072559; C:NLRP3 inflammasome complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0000182; F:rDNA binding; IDA:UniProtKB.
DR GO; GO:0043023; F:ribosomal large subunit binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISS:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; IMP:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Inflammasome;
KW Nucleotide-binding; Nucleus; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..698
FT /note="ATP-dependent RNA helicase DHX33"
FT /id="PRO_0000055165"
FT DOMAIN 75..243
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 271..441
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..71
FT /note="Required for nucleolar location"
FT /evidence="ECO:0000250|UniProtKB:Q9H6R0"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..553
FT /note="HA2; required for interaction with EIF3G and RPL26"
FT /evidence="ECO:0000250|UniProtKB:Q9H6R0"
FT MOTIF 185..188
FT /note="DEAH box"
FT MOTIF 536..550
FT /note="Critical for rDNA-binding"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 94
FT /note="K->N,R: Loss of stimulation of rRNA synthesis. Loss
FT of protein synthesis promotion. No effect on interaction
FT with DDX3X, EIF3G, EIF3H and RPL27."
FT /evidence="ECO:0000269|PubMed:21930779,
FT ECO:0000269|PubMed:26100019"
FT CONFLICT 470
FT /note="G -> V (in Ref. 1; BAC28969)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 78347 MW; 7DFF1F220C69544E CRC64;
MPEEASLPPA KRFRPGSCPP GRRVVMLLTA GGGGGAGGGR RQTPPLAQPS ASPYREALEL
QRRSLPIFRA RGQLLAQLRN LDNAVLIGET GSGKTTQIPQ YLYEGGISRQ GIIAVTQPRR
VAAISLATRV SDEKRTELGK LVGYTVRFED VTSEDTRIKF LTDGMLLREA ISDSLLRKYS
CVILDEAHER TIHTDVLFGV VKTAQKRRKE LGKLPLKVIV MSATMDVDLF SQYFNRAPVL
YLEGRQHPIQ IFYTKQPQQD YLHAALVSVF QIHQEAPASQ DILVFLTGQE EIEAMSKTCR
DIARHLPDGC PSMLVLPLYA SLPYSQQLRV FQGAPKGYRK VIISTNIAET SITITGIKYV
VDTGMVKAKK YNPDSGLEVL AVQRVSKTQA WQRTGRAGRE DSGICYRLYT EDEFEKFEKM
TVPEIQRCNL ASVILQLLAM KVPNVLTFDF MSKPSPDHIE AAIAQLDLLG ALEHKDDQLT
LTPIGRKMAA FPLEPRFAKT ILLSSKFHCT EEILTIVSLL SVDSVLYNPP ARRDEVQSVR
KKFISSEGDH ITLLNIYRTF KNIGGNKDWC KENFVNSKNM LLVAEVRAQL REICLKMSMP
IMSSRGDMES VRRCMAHSLF MNTAELQTDG TYATTDTHQP VAIHPSSVLF HCKPACVVYT
SLLYTNKCYM RDLCVVDAEW LYEAAPDYFR RKLRTARN
