DDX46_RAT
ID DDX46_RAT Reviewed; 1032 AA.
AC Q62780;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX46;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 46;
DE AltName: Full=Helicase of 117.4 kDa;
GN Name=Ddx46; Synonyms=Hel117;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1016-1032, AND SUBCELLULAR
RP LOCATION.
RX PubMed=7797571; DOI=10.1074/jbc.270.26.15702;
RA Sukegawa J., Blobel G.;
RT "A putative mammalian RNA helicase with an arginine-serine-rich domain
RT colocalizes with a splicing factor.";
RL J. Biol. Chem. 270:15702-15706(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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-804, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-804, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC subfamily. {ECO:0000305}.
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DR EMBL; U25746; AAC52210.1; -; mRNA.
DR EMBL; BC107590; AAI07591.1; -; mRNA.
DR PIR; A57514; A57514.
DR RefSeq; NP_620798.1; NM_139098.1.
DR AlphaFoldDB; Q62780; -.
DR SMR; Q62780; -.
DR BioGRID; 251453; 1.
DR IntAct; Q62780; 3.
DR STRING; 10116.ENSRNOP00000030772; -.
DR iPTMnet; Q62780; -.
DR PhosphoSitePlus; Q62780; -.
DR jPOST; Q62780; -.
DR PaxDb; Q62780; -.
DR PRIDE; Q62780; -.
DR GeneID; 245957; -.
DR KEGG; rno:245957; -.
DR UCSC; RGD:708480; rat.
DR CTD; 9879; -.
DR RGD; 708480; Ddx46.
DR VEuPathDB; HostDB:ENSRNOG00000021637; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_0_1; -.
DR InParanoid; Q62780; -.
DR OMA; CGLGVQT; -.
DR OrthoDB; 245118at2759; -.
DR PhylomeDB; Q62780; -.
DR TreeFam; TF354236; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q62780; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000021637; Expressed in spleen and 20 other tissues.
DR Genevisible; Q62780; RN.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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; ATP-binding; Coiled coil; Direct protein sequencing; 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_0000055124"
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 MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT MOD_RES 294
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L014"
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:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 904
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q569Z5"
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"
SQ SEQUENCE 1032 AA; 117385 MW; 5A86E159EC742EC7 CRC64;
MGRESRHYRK RSASRGRSGS RSRSRSPSDK RSKRGDDRRS RSRDRDRRRE RSRSRDKRRS
RSRDRKRLRR SRSRERDRSR ERRRSRSRDR RRSRSRSRGR RSRSSSPGSK SKKAENRSRS
KEKAEGGDSS KEKKKDKDDK EDEKEKDAGN FDQNKLEEEM RKRKERVEKW REEQRKKAME
NIGELKKEIE EMKQGKKWSL EDDDDDEDDP AEAEKEGNEM 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 AAPGTSSAPA
PTAGNAEKLE IAKRLALRIN AQKNLGIESQ VDVMQQATNA ILRGGPLLAP TVSAKTIAEQ
LAEKINAKLN YVPLEKQEEE RQEGGQSESF KRYEEELEIN DFPQTARWKV TSKEALQRIS
EYSEAAITIR GTYFPPGKEP KEGERKIYLA IESANELAVQ KAKAEITRLI KEELIRLQNS
YQPTNKGRYK VL
