DHX8_DROME
ID DHX8_DROME Reviewed; 1242 AA.
AC A1Z9L3; Q8MSQ6;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ATP-dependent RNA helicase DHX8 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P24384};
DE AltName: Full=Peanuts {ECO:0000312|FlyBase:FBgn0086895};
GN Name=pea {ECO:0000312|FlyBase:FBgn0086895};
GN Synonyms=Prp22 {ECO:0000312|FlyBase:FBgn0086895};
GN ORFNames=CG8241 {ECO:0000312|FlyBase:FBgn0086895};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM50025.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50025.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM50025.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:ACH92287.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACH92287.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN THE
RP SPLICEOSOME C COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=18981222; DOI=10.1128/mcb.01415-08;
RA Herold N., Will C.L., Wolf E., Kastner B., Urlaub H., Luhrmann R.;
RT "Conservation of the protein composition and electron microscopy structure
RT of Drosophila melanogaster and human spliceosomal complexes.";
RL Mol. Cell. Biol. 29:281-301(2009).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24244416; DOI=10.1371/journal.pone.0079048;
RA Klusza S., Novak A., Figueroa S., Palmer W., Deng W.M.;
RT "Prp22 and spliceosome components regulate chromatin dynamics in germ-line
RT polyploid cells.";
RL PLoS ONE 8:E79048-E79048(2013).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC (PubMed:18981222, PubMed:24244416). Facilitates nuclear export of
CC spliced mRNA by releasing the RNA from the spliceosome (By similarity).
CC Before and after egg-chamber formation, required for nurse-cell
CC chromatin dispersal (NCCD) probably by playing a role in spliceosome
CC localization to chromatin/interchromatin spaces (PubMed:24244416).
CC {ECO:0000250|UniProtKB:Q14562, ECO:0000269|PubMed:24244416,
CC ECO:0000303|PubMed:18981222}.
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.
CC {ECO:0000269|PubMed:18981222}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18981222}.
CC -!- DISRUPTION PHENOTYPE: Lethal. RNAi-mediated knockdown in the germ line
CC results in defective nurse cell morphology.
CC {ECO:0000269|PubMed:24244416}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX8/PRP22 sub-subfamily. {ECO:0000305}.
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DR EMBL; AE013599; AAF58294.1; -; Genomic_DNA.
DR EMBL; AY118656; AAM50025.1; -; mRNA.
DR EMBL; BT044222; ACH92287.1; -; mRNA.
DR RefSeq; NP_610928.1; NM_137084.3.
DR AlphaFoldDB; A1Z9L3; -.
DR SMR; A1Z9L3; -.
DR IntAct; A1Z9L3; 1.
DR STRING; 7227.FBpp0086647; -.
DR PaxDb; A1Z9L3; -.
DR PRIDE; A1Z9L3; -.
DR EnsemblMetazoa; FBtr0087518; FBpp0086647; FBgn0086895.
DR GeneID; 36561; -.
DR KEGG; dme:Dmel_CG8241; -.
DR UCSC; CG8241-RA; d. melanogaster.
DR CTD; 36561; -.
DR FlyBase; FBgn0086895; pea.
DR VEuPathDB; VectorBase:FBgn0086895; -.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00940000155510; -.
DR HOGENOM; CLU_001832_2_1_1; -.
DR InParanoid; A1Z9L3; -.
DR OMA; DPMVAPE; -.
DR OrthoDB; 354219at2759; -.
DR PhylomeDB; A1Z9L3; -.
DR BioGRID-ORCS; 36561; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36561; -.
DR PRO; PR:A1Z9L3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0086895; Expressed in egg cell and 26 other tissues.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IC:FlyBase.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0005681; C:spliceosomal complex; ISS:FlyBase.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; ISS:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; HMP:FlyBase.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IBA:GO_Central.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
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 1: Evidence at protein level;
KW ATP-binding; DNA condensation; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome;
KW Spliceosome.
FT CHAIN 1..1242
FT /note="ATP-dependent RNA helicase DHX8"
FT /id="PRO_0000444533"
FT DOMAIN 285..356
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 596..759
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 777..957
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 75..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 706..709
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 85..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 609..616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 511
FT /note="K -> R (in Ref. 3; AAM50025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1242 AA; 141936 MW; 1F1B6160E8B4637C CRC64;
MDELQKLEYL SLVSKICTEL DNHLGINDKD LAEFIIDLEN KNRTYDTFRK ALLDNGAEFP
DSLVQNLQRI INLMRPSRPG GASQEKTVGD KKEDKKSQLL KMFPGLALPN DTYSKKEESD
DDEKVKAKPE KHSETHKKTD MSDVDAAMME LEALAPGEGA TLVRPHKEVS SRDRHKRRSR
DRDTKRRSRS REDRHSDRRR SRSRDKERRR RSRSRDNRRR SRSREDRDRD RDRRHKSSSS
RDHHERRRRS RSRSTERRDR RDRSRDCSEK MPPPSAAMTD DPEAGKIYSG KIANIVPFGC
FVQLFGLRKR WEGLVHISQL RAEGRVTDVT EVVTRNQTVK VKVMSITGQK VSLSMKEVDQ
DSGKDLNPLS HAPEDDESLR DRNPDGPFSS STSMLNLQGN GMEGDEHESR KRVTRISSPE
RWEIKQMISS GVLDRSEMPD FDEETGLLPK DEDDEADIEI EIVEEEPPFL SGHGRALHDL
SPVRIVKNPD GSLAQAAMMQ SALSKERREQ KMLQREQEIE AMPTSLNKNW IDPLPEDESR
SLAANMRGMA AAPPEVPEWK KHVIGGKKSS FGKKTDLTLV EQRQSLPIYK LRDDLIKAVT
DNQILIVIGE TGSGKTTQIT QYLGECGFTA RGKIGCTQPR RVAAMSVAKR VAEEYGCRLG
QEVGYTIRFE DCTSPETIIK YMTDGMLLRE CLMEAELKSY SVIMLDEAHE RTIHTDVLFG
LLKTAVQKRP ELKLIVTSAT LDAVKFSQYF FKAPIFTIPG RTFPVEVLYT KEPETDYLDA
SLITVMQIHL REPPGDILLF LTGQEEIDTA CEILYERMKS LGPDVPELII LPVYSALPSE
MQTRIFDPAP AGSRKVVIAT NIAETSLTID GIFYVVDPGF VKQKVYNSKT GMDSLVVTPI
SQAAAKQRAG RAGRTGPGKT YRLYTERAYR DEMLPTPVPE IQRTNLATTV LQLKTMGIND
LLHFDFMDAP PVESLVMALE QLHSLSALDD EGLLTRLGRR MAEFPLEPNL SKMLIMSVAL
QCSDEILTIV SMLSVQNVFY RPKDKQALAD QKKAKFNQAE GDHLTLLAVY NSWKNNKFSN
AWCYENFVQI RTLKRSQDVR KQLLGIMDRH KLDVVSAGKN SVRIQKAICS GFFRNAAKKD
PQEGYRTLVD SQVVYIHPSS ALFNRQPEWV IYHELVQTTK EYMREVTTID PKWLVEFAPS
FFRFSDPTKL SKFKKNQRLE PLYNKYEEPN AWRISRVRRR RN
