DDX41_MOUSE
ID DDX41_MOUSE Reviewed; 622 AA.
AC Q91VN6; Q3U0E0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX41;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 41;
GN Name=Ddx41;
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=NOD; TISSUE=Spleen;
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=NMRI; TISSUE=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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-23 AND TYR-33, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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. Is required during post-
CC transcriptional gene expression. May be involved in pre-mRNA splicing.
CC {ECO:0000250|UniProtKB:Q9UJV9}.
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: Identified in the spliceosome C complex (By similarity).
CC Interacts with ERCC6 (By similarity). Interacts with FAM50A (By
CC similarity). {ECO:0000250|UniProtKB:Q9UJV9}.
CC -!- INTERACTION:
CC Q91VN6; Q3TBT3: Sting1; NbExp=4; IntAct=EBI-2551902, EBI-3862093;
CC Q91VN6; Q62191: Trim21; NbExp=6; IntAct=EBI-2551902, EBI-6840982;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJV9}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX41 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK156957; BAE33914.1; -; mRNA.
DR EMBL; BC011308; AAH11308.1; -; mRNA.
DR CCDS; CCDS26549.1; -.
DR RefSeq; NP_598820.2; NM_134059.2.
DR AlphaFoldDB; Q91VN6; -.
DR SMR; Q91VN6; -.
DR BioGRID; 215656; 19.
DR IntAct; Q91VN6; 6.
DR MINT; Q91VN6; -.
DR STRING; 10090.ENSMUSP00000021956; -.
DR iPTMnet; Q91VN6; -.
DR PhosphoSitePlus; Q91VN6; -.
DR EPD; Q91VN6; -.
DR jPOST; Q91VN6; -.
DR MaxQB; Q91VN6; -.
DR PaxDb; Q91VN6; -.
DR PeptideAtlas; Q91VN6; -.
DR PRIDE; Q91VN6; -.
DR ProteomicsDB; 279327; -.
DR Antibodypedia; 17469; 298 antibodies from 31 providers.
DR DNASU; 72935; -.
DR Ensembl; ENSMUST00000021956; ENSMUSP00000021956; ENSMUSG00000021494.
DR GeneID; 72935; -.
DR KEGG; mmu:72935; -.
DR UCSC; uc007qro.2; mouse.
DR CTD; 51428; -.
DR MGI; MGI:1920185; Ddx41.
DR VEuPathDB; HostDB:ENSMUSG00000021494; -.
DR eggNOG; KOG0341; Eukaryota.
DR GeneTree; ENSGT00940000156333; -.
DR HOGENOM; CLU_003041_16_5_1; -.
DR InParanoid; Q91VN6; -.
DR OrthoDB; 447398at2759; -.
DR PhylomeDB; Q91VN6; -.
DR TreeFam; TF300340; -.
DR Reactome; R-MMU-1834941; STING mediated induction of host immune responses.
DR Reactome; R-MMU-3134975; Regulation of innate immune responses to cytosolic DNA.
DR BioGRID-ORCS; 72935; 30 hits in 76 CRISPR screens.
DR ChiTaRS; Ddx41; mouse.
DR PRO; PR:Q91VN6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q91VN6; protein.
DR Bgee; ENSMUSG00000021494; Expressed in ectoplacental cone and 213 other tissues.
DR ExpressionAtlas; Q91VN6; baseline and differential.
DR Genevisible; Q91VN6; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; 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:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR CDD; cd17951; DEADc_DDX41; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044113; DEADc_DDX41.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
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; 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; Helicase; Hydrolase; Isopeptide bond; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Spliceosome;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..622
FT /note="Probable ATP-dependent RNA helicase DDX41"
FT /id="PRO_0000054971"
FT DOMAIN 212..396
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 407..567
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 580..597
FT /note="CCHC-type"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 181..209
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 344..347
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJV9"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 33
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJV9"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UJV9"
FT CONFLICT 562
FT /note="V -> G (in Ref. 2; AAH11308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 69820 MW; 85829CA9BDD0F4E1 CRC64;
MEDSEPERKR ARADEATAGG SRSEDEDEDD EDYVPYVPLR QRRQLLLQKL LQRRRKGATE
EEQQDSGSEP RGDEDDIPLG PQSNVSLLDQ HQHLKEKAEA RKESAKEKQL KEEEKILESV
AEGRALMSVK EMAKGITYDD PIKTSWTPPR YVLSMSEERH ERVRKKYHIL VEGDGIPPPI
KSFKEMKFPA AILRGLKKKG ILHPTPIQIQ GIPTILSGRD MIGIAFTGSG KTLVFTLPVI
MFCLEQEKRL PFSKREGPYG LIICPSRELA RQTHGILEYY CRLLQEDSSP LLRCALCIGG
MSVKEQMETI RHGVHMMVAT PGRLMDLLQK KMVSLDICRY LALDEADRMI DMGFEGDIRT
IFSYFKGQRQ TLLFSATMPK KIQNFAKSAL VKPVTINVGR AGAASLDVIQ EVEYVKEEAK
MVYLLECLQK TPPPVLIFAE KKADVDAIHE YLLLKGVEAV AIHGGKDQEE RTKAIEAFRE
GKKDVLVATD VASKGLDFPA IQHVINYDMP EEIENYVHRI GRTGRSGNTG IATTFINKAC
DESVLMDLKA LLLEAKQKVP PVLQVLHCGD ESMLDIGGER GCAFCGGLGH RITDCPKLEA
MQTKQVSNIG RKDYLAHSSM DF
