DHX34_MOUSE
ID DHX34_MOUSE Reviewed; 1145 AA.
AC Q9DBV3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable ATP-dependent RNA helicase DHX34 {ECO:0000305};
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 34 {ECO:0000312|MGI:MGI:1918973};
DE AltName: Full=DExH-box helicase 34 {ECO:0000250|UniProtKB:Q14147};
GN Name=Dhx34 {ECO:0000312|MGI:MGI:1918973};
GN Synonyms=Ddx34 {ECO:0000312|MGI:MGI:1918973}, Kiaa0134;
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 TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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-binding RNA helicase (By similarity). Required
CC for nonsense-mediated decay (NMD) degradation of mRNA transcripts
CC containing premature stop codons (By similarity). Promotes the
CC phosphorylation of UPF1 along with its interaction with key NMD pathway
CC proteins UPF2 and EIF4A3 (By similarity). Negatively regulates the
CC nucleotide binding ability and ATP hydrolysis of the RUVBL1-RUVBL2
CC complex via induction of N-terminus conformation changes of the RUVBL2
CC subunits (By similarity). {ECO:0000250|UniProtKB:A2BIE5,
CC ECO:0000250|UniProtKB:Q14147}.
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: Forms a complex with RUVBL1 and RUVBL2 (By similarity). Part
CC of a complex composed of SMG1, DHX34 and UPF1; within the complex DHX34
CC acts as a scaffolding protein to facilitate SMG1 phosphorylation of
CC UPF1 (By similarity). Interacts with UPF1, MOV10, EIF4A3, XRN2, SMG6,
CC SMG7, SMG9, UPF3A, UPF3B, CASC3/MLN51, XRN1, DIS3 and DCP1A; the
CC interactions are RNA-independent (By similarity). Interacts with
CC NCBP1/CPB80; the interaction is RNA-dependent (By similarity).
CC Interacts (via C-terminus) with SMG1; the interaction is RNA-
CC independent (By similarity). {ECO:0000250|UniProtKB:Q14147}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97872.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129062; BAC97872.1; ALT_INIT; mRNA.
DR EMBL; AK004733; BAB23515.1; -; mRNA.
DR CCDS; CCDS39783.1; -.
DR RefSeq; NP_001272860.1; NM_001285931.1.
DR RefSeq; NP_001272861.1; NM_001285932.1.
DR RefSeq; NP_082159.3; NM_027883.3.
DR RefSeq; XP_006540432.1; XM_006540369.3.
DR RefSeq; XP_017167800.1; XM_017312311.1.
DR AlphaFoldDB; Q9DBV3; -.
DR SMR; Q9DBV3; -.
DR STRING; 10090.ENSMUSP00000113393; -.
DR iPTMnet; Q9DBV3; -.
DR PhosphoSitePlus; Q9DBV3; -.
DR EPD; Q9DBV3; -.
DR MaxQB; Q9DBV3; -.
DR PaxDb; Q9DBV3; -.
DR PRIDE; Q9DBV3; -.
DR ProteomicsDB; 279532; -.
DR DNASU; 71723; -.
DR GeneID; 71723; -.
DR KEGG; mmu:71723; -.
DR CTD; 9704; -.
DR MGI; MGI:1918973; Dhx34.
DR eggNOG; KOG0922; Eukaryota.
DR InParanoid; Q9DBV3; -.
DR OrthoDB; 278674at2759; -.
DR BioGRID-ORCS; 71723; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Dhx34; mouse.
DR PRO; PR:Q9DBV3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9DBV3; protein.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex 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:2000623; P:negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; ISO:MGI.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0042327; P:positive regulation of phosphorylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1145
FT /note="Probable ATP-dependent RNA helicase DHX34"
FT /id="PRO_0000055167"
FT DOMAIN 174..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 370..538
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 281..284
FT /note="DEAH box"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14147"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14147"
FT CONFLICT 82
FT /note="K -> E (in Ref. 2; BAB23515)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="A -> V (in Ref. 2; BAB23515)"
FT /evidence="ECO:0000305"
FT CONFLICT 756
FT /note="K -> E (in Ref. 2; BAB23515)"
FT /evidence="ECO:0000305"
FT CONFLICT 948
FT /note="A -> V (in Ref. 2; BAB23515)"
FT /evidence="ECO:0000305"
FT CONFLICT 973
FT /note="V -> M (in Ref. 2; BAB23515)"
FT /evidence="ECO:0000305"
FT CONFLICT 995
FT /note="A -> V (in Ref. 2; BAB23515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1145 AA; 128507 MW; 88E58CE002FE588E CRC64;
MPPPRTREGR GHRDRDHHRA PREEEAPEKW DWNCPETRCL LEDVFFRDED YIRRGSEECQ
KFWAFFERLQ RFQHLKTSQK KKKDPGMPKH GIAALADLPL TYDPRYRINL SILSPDTRGR
HGPGRGLPPE RVSEFRRALL HYLDFQQKQA FGRLAKLQRE RAALPIAQYG NRILQTLKEH
QVVVVAGDTG CGKSTQVPQY LLAAGFSHVA CTQPRRIACI SLAKRVGFES LSQYGSQVGY
QIRFESTRSA ATKIVFLTVG LLLRQIQREP SLPQYQVLIV DEVHERHLHN DFLLGVLQRL
LPQRPDLKVI LMSATINISL FSSYFSHAPV VQVPGRLFPI TVVYQPQEAD QTASKSEKLD
PRPFLRVLEA IDNKYPPEER GDLLVFLSGM AEITTVLDAA QAYASLTQRW VVLPLHSALS
VSDQDKVFDV APAGVRKCIL STNIAETSVT IDGIRFVVDS GKVKEMSYDP QAKLQRLQEF
WISQASAEQR KGRAGRTGPG VCYRLYAESD YDAFAPYPVP EIRRVALDAL VLQMKSMSVG
DPRTFPFIEP PPPASVETAI LYLQEQGALD SSEALTPIGS LLAQLPVDVV IGKMLILGSM
FSLAEPVLTI AAALSVQSPF TRSAQSNLDC ATARRPLESD QGDPFTLFNV FNAWVQVKSE
RSGNSRKWCR RRGVEEHRLY EMANLRRQFK ELLEDHGLLS GAQVVAPGDS YSRLQQRRER
RALHQLKRQH EEGGGRRRKV LRLQEDGCSS DEEDRKGSTS QRADSVDIQD VKFKLRHNLE
QLQAAASSAQ DLTRDQLALL KLVLGRGLYP QLAVPDAFNS GRKDSDQIFH TQAKQGTVLH
PTCVFANSPE VLHTQGQEAS GQEGSQDGRD QMSCKHQLLA FVSLLETNKP YLVNCVRIPA
LQSLLLFSRS IDTNGDCSRL VADGWLELQL ADSESAVRLL ATSLRLRAHW ESALDRQLAR
QAQRRKLEQE EDVGSPAVSP QEVAALSREL LQFMAAKVPY RLRRLTGLEA QNLYVGPQTI
TTAPSLPGLF GNSTLSPHPT KGGYAVSDYL TYNCLTSDTD LYSDCLRSFW TCPHCGLHMP
FTPLERIAHE NTCPEAPGDD PGSEEAAPAP PQKTSALQRP YHCQVCGQDF LFTPTEVLRH
RRQHV
