DDX18_MOUSE
ID DDX18_MOUSE Reviewed; 660 AA.
AC Q8K363; Q3MIB0; Q8BVZ2; Q9D2E0;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ATP-dependent RNA helicase DDX18;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 18;
GN Name=Ddx18;
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=Testis, and Tongue;
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 STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 RNA-dependent helicase.
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 NOL8; the interaction is RNA-dependent.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9NVP1}. Chromosome
CC {ECO:0000250|UniProtKB:Q9NVP1}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1
CC subfamily. {ECO:0000305}.
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DR EMBL; AK075864; BAC36015.1; -; mRNA.
DR EMBL; AK019845; BAB31877.1; -; mRNA.
DR EMBL; BC028246; AAH28246.1; -; mRNA.
DR EMBL; BC103776; AAI03777.1; -; mRNA.
DR CCDS; CCDS15240.1; -.
DR RefSeq; NP_080136.2; NM_025860.3.
DR AlphaFoldDB; Q8K363; -.
DR SMR; Q8K363; -.
DR BioGRID; 211826; 10.
DR CORUM; Q8K363; -.
DR STRING; 10090.ENSMUSP00000001724; -.
DR iPTMnet; Q8K363; -.
DR PhosphoSitePlus; Q8K363; -.
DR SwissPalm; Q8K363; -.
DR EPD; Q8K363; -.
DR MaxQB; Q8K363; -.
DR PaxDb; Q8K363; -.
DR PRIDE; Q8K363; -.
DR ProteomicsDB; 279611; -.
DR Antibodypedia; 33358; 95 antibodies from 23 providers.
DR DNASU; 66942; -.
DR Ensembl; ENSMUST00000001724; ENSMUSP00000001724; ENSMUSG00000001674.
DR GeneID; 66942; -.
DR KEGG; mmu:66942; -.
DR UCSC; uc007cjw.2; mouse.
DR CTD; 8886; -.
DR MGI; MGI:1914192; Ddx18.
DR VEuPathDB; HostDB:ENSMUSG00000001674; -.
DR eggNOG; KOG0342; Eukaryota.
DR GeneTree; ENSGT00680000100037; -.
DR HOGENOM; CLU_003041_26_5_1; -.
DR InParanoid; Q8K363; -.
DR OMA; EYEFPAN; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q8K363; -.
DR TreeFam; TF300471; -.
DR BioGRID-ORCS; 66942; 26 hits in 74 CRISPR screens.
DR ChiTaRS; Ddx18; mouse.
DR PRO; PR:Q8K363; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8K363; protein.
DR Bgee; ENSMUSG00000001674; Expressed in embryonic post-anal tail and 78 other tissues.
DR ExpressionAtlas; Q8K363; baseline and differential.
DR Genevisible; Q8K363; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR CDD; cd17942; DEADc_DDX18; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044773; DDX18/Has1_DEADc.
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 1: Evidence at protein level;
KW ATP-binding; Chromosome; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; RNA-binding.
FT CHAIN 1..660
FT /note="ATP-dependent RNA helicase DDX18"
FT /id="PRO_0000055002"
FT DOMAIN 200..375
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 389..559
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 15..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 169..197
FT /note="Q motif"
FT MOTIF 323..326
FT /note="DEAD box"
FT COMPBIAS 27..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 259
FT /note="G -> D (in Ref. 1; BAB31877)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="Y -> C (in Ref. 1; BAC36015)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="K -> R (in Ref. 1; BAC36015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 74181 MW; F80EFC0E741C2D7A CRC64;
MSQLQMKLLR RKIEKRNAKL RQRNLKLQET SDTSLSQPQN GDVPKETGKG GKVKKALKRS
VPVDSAEAQS GGMPEETLEN GKVKKSPQKL TTLANGEAAP TPPPDSEVKK KKKKKRKMAN
DAGPDTKKAK TEESAEACEE PEDDVKKADD SEVPSLPLGL TGAFEDTSFA SLSNLVNENT
LKAIEEMGFK RMTEIQHKSI RPLLEGRDLL AAAKTGSGKT LAFLIPVIEL IVKLKFMPRN
GTGVLILSPT RELAMQTFGV LKELMTHHVH TYGLIMGGSN RSAEVQKLLN GINIIVATPG
RLLDHMQNTP GFMYKNLQCL VIDEADRILD VGFEEELKQI IKLLPARRQT MLFSATQTRK
VEDLARISLK KEPLYVGVDD DKEVATVDGL EQGYVVCPSE KRFLLLFTFL KKNRKKKVMV
FFSSCMSVKY HYELLNYIDL PVLAIHGKQK QNKRTTTFFQ FCNADSGILL CTDVAARGLD
IPEVDWIVQY DPPDDPKEYI HRVGRTARGL NGRGHALLIL RPEELGFLRY LKQSKVPLNQ
FDFSWSKVSD IQSQLEKLIE KNYFLHKSAQ EAYKSYIRAY DSHSLKQIFN VNNLNLPQVA
LSFGFKVPPF VDLNVSSHDG KLKKRGGGGG FGYQKTKKVE KSKIFKHISK KPADRRQFSH
