DDX46_MOUSE
ID DDX46_MOUSE Reviewed; 1032 AA.
AC Q569Z5; Q6ZQ42; Q8R0R6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX46;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 46;
GN Name=Ddx46; Synonyms=Kiaa0801;
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] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Head;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-804, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-294; SER-295; SER-296 AND
RP SER-804, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, 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).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-904, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Plays an essential role in splicing, either prior to, or
CC during A complex formation. {ECO:0000250}.
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: Integral component of the 17S U2 snRNP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus, Cajal
CC body {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q7L014}; Lipid-
CC anchor {ECO:0000250|UniProtKB:Q7L014}. Note=Present in Cajal bodies
CC (CBs) and nuclear speckles. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q569Z5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q569Z5-2; Sequence=VSP_016859;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26492.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH92240.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98030.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129220; BAC98030.2; ALT_INIT; Transcribed_RNA.
DR EMBL; BC026492; AAH26492.1; ALT_INIT; mRNA.
DR EMBL; BC092240; AAH92240.1; ALT_SEQ; mRNA.
DR CCDS; CCDS70464.1; -. [Q569Z5-1]
DR RefSeq; NP_001268984.1; NM_001282055.1. [Q569Z5-1]
DR AlphaFoldDB; Q569Z5; -.
DR SMR; Q569Z5; -.
DR BioGRID; 229365; 4.
DR IntAct; Q569Z5; 1.
DR MINT; Q569Z5; -.
DR STRING; 10090.ENSMUSP00000133245; -.
DR iPTMnet; Q569Z5; -.
DR PhosphoSitePlus; Q569Z5; -.
DR SwissPalm; Q569Z5; -.
DR EPD; Q569Z5; -.
DR jPOST; Q569Z5; -.
DR MaxQB; Q569Z5; -.
DR PaxDb; Q569Z5; -.
DR PeptideAtlas; Q569Z5; -.
DR PRIDE; Q569Z5; -.
DR ProteomicsDB; 279328; -. [Q569Z5-1]
DR ProteomicsDB; 279329; -. [Q569Z5-2]
DR Antibodypedia; 26347; 125 antibodies from 24 providers.
DR DNASU; 212880; -.
DR Ensembl; ENSMUST00000172272; ENSMUSP00000133245; ENSMUSG00000021500. [Q569Z5-1]
DR Ensembl; ENSMUST00000223736; ENSMUSP00000153328; ENSMUSG00000021500. [Q569Z5-1]
DR GeneID; 212880; -.
DR KEGG; mmu:212880; -.
DR UCSC; uc033gma.1; mouse. [Q569Z5-1]
DR CTD; 9879; -.
DR MGI; MGI:1920895; Ddx46.
DR VEuPathDB; HostDB:ENSMUSG00000021500; -.
DR eggNOG; KOG0334; Eukaryota.
DR GeneTree; ENSGT00940000157753; -.
DR HOGENOM; CLU_003041_0_0_1; -.
DR InParanoid; Q569Z5; -.
DR OMA; CGLGVQT; -.
DR OrthoDB; 245118at2759; -.
DR PhylomeDB; Q569Z5; -.
DR TreeFam; TF354236; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 212880; 17 hits in 68 CRISPR screens.
DR ChiTaRS; Ddx46; mouse.
DR PRO; PR:Q569Z5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q569Z5; protein.
DR Bgee; ENSMUSG00000021500; Expressed in embryonic post-anal tail and 243 other tissues.
DR ExpressionAtlas; Q569Z5; baseline and differential.
DR Genevisible; Q569Z5; MM.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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 Acetylation; Alternative splicing; ATP-binding; Coiled coil; Helicase;
KW Hydrolase; Isopeptide bond; Lipoprotein; Membrane; mRNA processing;
KW mRNA splicing; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT CHAIN 2..1032
FT /note="Probable ATP-dependent RNA helicase DDX46"
FT /id="PRO_0000055122"
FT DOMAIN 403..581
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 592..753
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 152..197
FT /evidence="ECO:0000255"
FT MOTIF 372..400
FT /note="Q motif"
FT MOTIF 529..532
FT /note="DEAD box"
FT COMPBIAS 22..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..73
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..107
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..227
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 416..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62780"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT MOD_RES 294
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT MOD_RES 776
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 904
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT CROSSLNK 779
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT CROSSLNK 908
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT CROSSLNK 916
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT VAR_SEQ 516..544
FT /note="RVTNLRRVTYVVLDEADRMFDMGFEPQVM -> KSRVFYYLFSLLFVLDMIF
FT VEADL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_016859"
SQ SEQUENCE 1032 AA; 117448 MW; F690CE9973A079AA CRC64;
MGRESRHYRK RSASRGRSGS RSRSRSPSDK RSKRGDDRRS RSRDRDRRRE RSRSRDKRRS
RSRDRKRLRR SRSRERDRSR ERRRSRSRDR RRSRSRSRGR RSRSSSPGSK TKKTENRSRS
KEKAEGGDSS KEKKKDKDDK EDEKEKDAGN FDQNKLEEEM RKRKERVEKW REEQRKKAME
NIGELKKEIE EMKQGKKWSL EDDDDDEDDP AEAEKEGTEM EDEELDPLDA YMEEVKEEVK
KFNMRSVKGG AGNEKKSGPT VTKVVTVVTT KKAVVDADKK KGELMENDQD AMEYSSEEEE
VDLQTALTGY QTKQRKLLEP VDHGKIEYEP FRKNFYVEVP ELAKMSQEEV NVFRLEMEGI
TVKGKGCPKP IKSWVQCGIS MKILNSLKKH GYEKPTPIQT QAIPAIMSGR DLIGIAKTGS
GKTIAFLLPM FRHIMDQRSL EEGEGPIAVI MTPTRELALQ ITKECKKFSK TLGLRVVCVY
GGTGISEQIA ELKRGAEIIV CTPGRMIDML AANSGRVTNL RRVTYVVLDE ADRMFDMGFE
PQVMRIVDNV RPDRQTVMFS ATFPRAMEAL ARRILSKPIE VQVGGRSVVC SDVEQQVIVI
EEEKKFLKLL ELLGHYQESG SVIIFVDKQE HADGLLKDLM RASYPCMSLH GGIDQYDRDS
IINDFKNGTC KLLVATSVAA RGLDVKHLIL VVNYSCPNHY EDYVHRAGRT GRAGNKGYAY
TFITEDQARY AGDIIKALEL SGTAVPPDLE KLWSDFKDQQ KAEGKIIKKS SGFSGKGFKF
DETEQALANE RKKLQKAALG LQDSDDEDAA VDIDEQIESM FNSKKRVKDM AAPGTSSVPA
PTAGNAEKLE IAKRLALRIN AQKNLGIESQ VDVMQQATNA ILRGGTILAP TVSAKTIAEQ
LAEKINAKLN YVPLEKQEEE RQEGGQSESF KRYEEELEIN DFPQTARWKV TSKEALQRIS
EYSEAAITIR GTYFPPGKEP KEGERKIYLA IESANELAVQ KAKAEITRLI KEELIRLQNS
YQPTNKGRYK VL
