DHX8_MOUSE
ID DHX8_MOUSE Reviewed; 1244 AA.
AC A2A4P0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ATP-dependent RNA helicase DHX8;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P24384};
DE AltName: Full=DEAH box protein 8;
GN Name=Dhx8;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the
CC spliceosome. Facilitates nuclear export of spliced mRNA by releasing
CC the RNA from the spliceosome. {ECO:0000250|UniProtKB:Q14562}.
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 Evidence={ECO:0000250|UniProtKB:P24384};
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with ARRB2;
CC the interaction is detected in the nucleus upon OR1D2 stimulation.
CC {ECO:0000250|UniProtKB:Q14562}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14562}.
CC -!- DOMAIN: The RS domain confers a nuclear localization signal, and
CC appears to facilitate the interaction with the spliceosome.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX8/PRP22 sub-subfamily. {ECO:0000305}.
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DR EMBL; BC132445; AAI32446.1; -; mRNA.
DR EMBL; AL590994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25479.1; -.
DR RefSeq; NP_659080.2; NM_144831.2.
DR AlphaFoldDB; A2A4P0; -.
DR SMR; A2A4P0; -.
DR BioGRID; 229862; 13.
DR IntAct; A2A4P0; 1.
DR MINT; A2A4P0; -.
DR STRING; 10090.ENSMUSP00000037251; -.
DR iPTMnet; A2A4P0; -.
DR PhosphoSitePlus; A2A4P0; -.
DR EPD; A2A4P0; -.
DR jPOST; A2A4P0; -.
DR MaxQB; A2A4P0; -.
DR PaxDb; A2A4P0; -.
DR PeptideAtlas; A2A4P0; -.
DR PRIDE; A2A4P0; -.
DR ProteomicsDB; 279534; -.
DR Antibodypedia; 29563; 195 antibodies from 25 providers.
DR DNASU; 217207; -.
DR Ensembl; ENSMUST00000039152; ENSMUSP00000037251; ENSMUSG00000034931.
DR GeneID; 217207; -.
DR KEGG; mmu:217207; -.
DR UCSC; uc007lpr.1; mouse.
DR CTD; 1659; -.
DR MGI; MGI:1306823; Dhx8.
DR VEuPathDB; HostDB:ENSMUSG00000034931; -.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00940000155510; -.
DR InParanoid; A2A4P0; -.
DR OMA; DPMVAPE; -.
DR OrthoDB; 354219at2759; -.
DR PhylomeDB; A2A4P0; -.
DR TreeFam; TF300509; -.
DR BioGRID-ORCS; 217207; 25 hits in 76 CRISPR screens.
DR ChiTaRS; Dhx8; mouse.
DR PRO; PR:A2A4P0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; A2A4P0; protein.
DR Bgee; ENSMUSG00000034931; Expressed in humerus cartilage element and 214 other tissues.
DR ExpressionAtlas; A2A4P0; baseline and differential.
DR Genevisible; A2A4P0; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; 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:0042802; F:identical protein 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:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IBA:GO_Central.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR044762; DHX8/Prp22_DEXHc.
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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 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.
DR PROSITE; PS50126; S1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Helicase; Hydrolase; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome; Ubl conjugation.
FT CHAIN 1..1244
FT /note="ATP-dependent RNA helicase DHX8"
FT /id="PRO_0000330831"
FT DOMAIN 289..360
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 599..762
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 780..960
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 152..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 709..712
FT /note="DEAH box"
FT COMPBIAS 180..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..250
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 612..619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14562"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14562"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14562"
FT CROSSLNK 423
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14562"
SQ SEQUENCE 1244 AA; 142572 MW; 8FD07949CCCB4DD2 CRC64;
MAVAVAAAGV LMGSEPGPAE ELAKLEYLSL VSKVCTELDN HLGINDKDLA EFVISLAEKN
TTFDTFKASL VKNGAEFTDS LISNLLRLIQ TMRPPAKPST SKDPVVKPKT EKEKLRELFP
VLCQPDNPSA RTMLDEEDVK VAVDVLKELE ALMPSAAGQE KQRDPEHRDR TKKKKRSRSR
DRDRDRDRDR DRDRDRDRDR DKDRERDRDR ERDRERDRER DHKRRHRSRS RSHSRTRERT
KGKSRYRSRS RSQSPFKDRK DREKYGERNL DRWRDKHVDR PPPEEPAIGD IYNGKVTSIM
QFGCFVQLEG LRKRWEGLVH ISELRREGRV ANVADVVSKG QRVKVKVLSF TGTKTSLSMK
DVDQETGEDL NPNRRRNLVG ETNEETSMRN PDRPTHLSLV SAPEVEDDSL ERKRLTRISD
PEKWEIKQMI AANVLSKEEF PDFDEETGIL PKVDDEEDED LEIELVEEEP PFLRGHTKQS
MDMSPIKIVK NPDGSLSQAA MMQSALAKER RELKQAQREA EMDSIPMGLN KHWVDPLPDA
EGRQIAANMR GIGMMPNDIP EWKKHAFGGN KASYGKKTQM SILEQRESLP IYKLKEQLVQ
AVHDNQILIV IGETGSGKTT QITQYLAEAG YTSRGKIGCT QPRRVAAMSV AKRVSEEFGC
CLGQEVGYTI RFEDCTSPET VIKYMTDGML LRECLIDPDL TQYAIIMLDE AHERTIHTDV
LFGLLKKTVQ KRQDMKLIVT SATLDAVKFS QYFYEAPIFT IPGRTYPVEI LYTKEPETDY
LDASLITVMQ IHLTEPPGDI LVFLTGQEEI DTACEILYER MKSLGPDVPE LIILPVYSAL
PSEMQTRIFD PAPPGSRKVV IATNIAETSL TIDGIYYVVD PGFVKQKVYN SKTGIDQLVV
TPISQAQAKQ RAGRAGRTGP GKCYRLYTER AYRDEMLTTN VPEIQRTNLA STVLSLKAMG
INDLLSFDFM DAPPMETLIT AMEQLYTLGA LDDEGLLTRL GRRMAEFPLE PMLCKMLIMS
VHLGCSEEML TIVSMLSVQN VFYRPKDKQA LADQKKAKFH QTEGDHLTLL AVYNSWKNNK
FSNPWCYENF IQARSLRRAQ DIRKQMLGIM DRHKLDVVSC GKSTVRVQKA ICSGFFRNAA
KKDPQEGYRT LIDQQVVYIH PSSALFNRQP EWVVYHELVL TTKEYMREVT TIDPRWLVEF
APAFFKVSDP TKLSKQKKQQ RLEPLYNRYE EPNAWRISRA FRRR
