DHX40_MOUSE
ID DHX40_MOUSE Reviewed; 779 AA.
AC Q6PE54; Q8BPH2; Q8CD88; Q9CWN3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable ATP-dependent RNA helicase DHX40;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 40;
GN Name=Dhx40;
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 STRAIN=C57BL/6J; TISSUE=Lung, and Thymus;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase. {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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58276.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB26995.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC25091.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC27210.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC36102.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK004610; BAC25091.1; ALT_FRAME; mRNA.
DR EMBL; AK010512; BAB26995.2; ALT_INIT; mRNA.
DR EMBL; AK031000; BAC27210.1; ALT_FRAME; mRNA.
DR EMBL; AK075991; BAC36102.1; ALT_FRAME; mRNA.
DR EMBL; AL592222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL596111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058276; AAH58276.2; ALT_INIT; mRNA.
DR CCDS; CCDS36268.1; -.
DR RefSeq; NP_080467.3; NM_026191.2.
DR AlphaFoldDB; Q6PE54; -.
DR SMR; Q6PE54; -.
DR BioGRID; 212223; 1.
DR STRING; 10090.ENSMUSP00000018569; -.
DR iPTMnet; Q6PE54; -.
DR PhosphoSitePlus; Q6PE54; -.
DR EPD; Q6PE54; -.
DR MaxQB; Q6PE54; -.
DR PaxDb; Q6PE54; -.
DR PeptideAtlas; Q6PE54; -.
DR PRIDE; Q6PE54; -.
DR ProteomicsDB; 279766; -.
DR Antibodypedia; 52618; 33 antibodies from 13 providers.
DR DNASU; 67487; -.
DR Ensembl; ENSMUST00000018569; ENSMUSP00000018569; ENSMUSG00000018425.
DR GeneID; 67487; -.
DR KEGG; mmu:67487; -.
DR UCSC; uc007ktc.1; mouse.
DR CTD; 79665; -.
DR MGI; MGI:1914737; Dhx40.
DR VEuPathDB; HostDB:ENSMUSG00000018425; -.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00940000158902; -.
DR HOGENOM; CLU_001832_5_11_1; -.
DR InParanoid; Q6PE54; -.
DR OMA; RRKWTNK; -.
DR OrthoDB; 354219at2759; -.
DR PhylomeDB; Q6PE54; -.
DR TreeFam; TF332290; -.
DR BioGRID-ORCS; 67487; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dhx40; mouse.
DR PRO; PR:Q6PE54; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6PE54; protein.
DR Bgee; ENSMUSG00000018425; Expressed in spermatocyte and 257 other tissues.
DR ExpressionAtlas; Q6PE54; baseline and differential.
DR Genevisible; Q6PE54; MM.
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; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
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; PS00690; DEAH_ATP_HELICASE; 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; Reference proteome.
FT CHAIN 1..779
FT /note="Probable ATP-dependent RNA helicase DHX40"
FT /id="PRO_0000252396"
FT DOMAIN 63..231
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 263..442
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 173..176
FT /note="DEAH box"
FT COMPBIAS 10..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 779 AA; 88530 MW; 46B8789EBEB1438D CRC64;
MSRFPAVAGR APRRQEEGER PIELQEERPS AVRIADREEK GCTSQEGGTT PTFPIQKQRK
KLIQAVRDNS FLIVTGNTGS GKTTQLPKYL YEAGFSQHGM IGVTQPRKVA AISVAQRVAE
EMKCTLGSKV GYQVRFDDCS SKETAIKYMT DGCLLKHILG DPNLSKFSVI ILDEAHERTL
TTDILFGLLK KLFQDKSPNR KEHLKVVVMS ATMELAKLSA FFGNCPIFDI PGRLYPVREK
FCNLIGPRDR ENTAYIQAIV KVTMDIHLNE MAGDILVFLT GQFEIEKSCE LLFQMAESVD
YDYDVQDTTL DGLLILPCYG SMTTDQQRRI FLPPPPGIRK CVISTNISAT SLTIDGIRYV
VDGGFVKQLN HNPRLGLDIL EVVPISKSEA LQRSGRAGRT ASGKCFRIYS KEFWSQCMPD
HVIPEIKRTS LTSVVLTLKC LAIHDVIRFP YLDPPNERLI LEALKQLYQC DAIDRSGHVT
RLGLSMVEFP LPPHLTCAVI RAASLDCEDL LLPIAAMLSV ENVFIRPVDP EYQKEAEQRH
RELAAKAGGF NDFATLAVIF EQCKSSGAPA SWCQKHWIHW RCLFSAFRVE AQLRELIRKL
KQQSDFPRET FEGPKHEVLR RCLCAGYFKN VARRSVGRTF CTMDGRGSPV HIHPSSALHE
QETKLEWIIF HEVLVTTKVY ARIVCPIRYE WVRDLLPKLH ELNAHDLSSV ARREMREDAR
RKWTNKENVK QLKDGISKEV LKKMQRRNDD KSISDARARF LERKQQRIQD HSDTLKETG
