DHX36_RAT
ID DHX36_RAT Reviewed; 1000 AA.
AC D4A2Z8;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=ATP-dependent DNA/RNA helicase DHX36 {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9H2U1};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=DEAD/H box polypeptide 36 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=DEAH-box protein 36 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=G4-resolvase-1 {ECO:0000250|UniProtKB:Q9H2U1};
DE Short=G4R1 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=MLE-like protein 1 {ECO:0000250|UniProtKB:Q9H2U1};
DE AltName: Full=RNA helicase associated with AU-rich element protein {ECO:0000250|UniProtKB:Q9H2U1};
GN Name=Dhx36 {ECO:0000312|RGD:1308767};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION, PRE-MIR-134 RNA-BINDING, SUBCELLULAR LOCATION, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND DOMAIN.
RX PubMed=23651854; DOI=10.1101/gad.211243.112;
RA Bicker S., Khudayberdiev S., Weiss K., Zocher K., Baumeister S.,
RA Schratt G.;
RT "The DEAH-box helicase DHX36 mediates dendritic localization of the
RT neuronal precursor-microRNA-134.";
RL Genes Dev. 27:991-996(2013).
CC -!- FUNCTION: Multifunctional ATP-dependent helicase that unwinds G-
CC quadruplex (G4) structures (By similarity). Plays a role in many
CC biological processes such as genomic integrity, gene expression
CC regulations and as a sensor to initiate antiviral responses
CC (PubMed:23651854). G4 structures correspond to helical structures
CC containing guanine tetrads (By similarity). Binds with high affinity to
CC and unwinds G4 structures that are formed in nucleic acids (G4-ADN and
CC G4-RNA) (By similarity). Plays a role in genomic integrity. Converts
CC the G4-RNA structure present in telomerase RNA template component
CC (TREC) into a double-stranded RNA to promote P1 helix formation that
CC acts as a template boundary ensuring accurate reverse transcription (By
CC similarity). Plays a role in transcriptional regulation. Resolves G4-
CC DNA structures in promoters of genes, such as YY1, KIT/c-kit and ALPL
CC and positively regulates their expression (By similarity). Plays a role
CC in post-transcriptional regulation. Unwinds a G4-RNA structure located
CC in the 3'-UTR polyadenylation site of the pre-mRNA TP53 and stimulates
CC TP53 pre-mRNA 3'-end processing in response to ultraviolet (UV)-induced
CC DNA damage (By similarity). Binds to the precursor-microRNA-134 (pre-
CC miR-134) terminal loop and regulates its transport into the synapto-
CC dendritic compartment (PubMed:23651854). Involved in the pre-miR-134-
CC dependent inhibition of target gene expression and the control of
CC dendritic spine size (PubMed:23651854). Plays a role in the regulation
CC of cytoplasmic mRNA translation and mRNA stability. Binds to both G4-
CC RNA structures and alternative non-quadruplex-forming sequence within
CC the 3'-UTR of the PITX1 mRNA regulating negatively PITX1 protein
CC expression. Binds to both G4-RNA structure in the 5'-UTR and AU-rich
CC elements (AREs) localized in the 3'-UTR of NKX2-5 mRNA to either
CC stimulate protein translation or induce mRNA decay in an ELAVL1-
CC dependent manner, respectively. Binds also to ARE sequences present in
CC several mRNAs mediating exosome-mediated 3'-5' mRNA degradation.
CC Involved in cytoplasmic urokinase-type plasminogen activator (uPA) mRNA
CC decay (By similarity). Component of a multi-helicase-TICAM1 complex
CC that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA)
CC and plays a role in the activation of a cascade of antiviral responses
CC including the induction of pro-inflammatory cytokines via the adapter
CC molecule TICAM1. Required for the early embryonic development and
CC hematopoiesis. Involved in the regulation of cardioblast
CC differentiation and proliferation during heart development. Involved in
CC spermatogonia differentiation. May play a role in ossification (By
CC similarity). {ECO:0000250|UniProtKB:Q05B79,
CC ECO:0000250|UniProtKB:Q8VHK9, ECO:0000250|UniProtKB:Q9H2U1,
CC ECO:0000269|PubMed:23651854}.
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=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q9H2U1};
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:Q9H2U1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q05B79};
CC -!- ACTIVITY REGULATION: ATPase activity is enhanced in the presence of
CC homomeric poly(U) RNAs, but not by double-stranded DNA (dsDNA), double-
CC stranded RNA (dsRNA) and tRNA. {ECO:0000250|UniProtKB:Q9H2U1}.
CC -!- SUBUNIT: Found in a multi-helicase-TICAM1 complex at least composed of
CC DHX36, DDX1, DDX21 and TICAM1; this complex exists in resting cells
CC with or without dsRNA poly(I:C) ligand stimulation. Interacts (via C-
CC terminus) with TICAM1 (via TIR domain). Interacts (via C-terminus) with
CC DDX21; this interaction serves as bridges to TICAM1 (By similarity).
CC Interacts with TERT; this interaction is dependent on the ability of
CC DHX36 to bind to the G-quadruplex RNA (G4-RNA) structure present in the
CC telomerase RNA template component (TERC). Interacts with DKC1; this
CC interaction is dependent on the ability of DHX36 to bind to the G4-RNA
CC structure present in TERC. Interacts with PARN; this interaction
CC stimulates PARN to enhance uPA mRNA decay. Interacts with EXOSC3; this
CC interaction occurs in a RNase-insensitive manner. Interacts with
CC EXOSC10; this interaction occurs in a RNase-insensitive manner.
CC Interacts with ILF3; this interaction occurs in a RNA-dependent manner.
CC Interacts with ELAVL1; this interaction occurs in an RNA-dependent
CC manner. Interacts with DDX5; this interaction occurs in a RNA-dependent
CC manner. Interacts with DDX17; this interaction occurs in a RNA-
CC dependent manner. Interacts with HDAC1; this interaction occurs in a
CC RNA-dependent manner (By similarity). Interacts with HDAC3; this
CC interaction occurs in a RNA-dependent manner (By similarity). Interacts
CC with HDAC4 (By similarity). Interacts with AGO1. Interacts with AGO2
CC (By similarity). Interacts with ERCC6 (By similarity).
CC {ECO:0000250|UniProtKB:Q8VHK9, ECO:0000250|UniProtKB:Q9H2U1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H2U1}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8VHK9}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q9H2U1}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9H2U1}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q9H2U1}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q8VHK9}. Perikaryon
CC {ECO:0000269|PubMed:23651854}. Cell projection, dendrite
CC {ECO:0000269|PubMed:23651854}. Cell projection, axon
CC {ECO:0000269|PubMed:23651854}. Note=Predominantly localized in the
CC nucleus. Colocalizes with SRSF2 in nuclear speckles. Colocalizes with
CC DDX5 in nucleolar caps upon transcription inhibition. Accumulates and
CC colocalized with TIA1 in cytoplasmic stress granules (SGs) in an
CC arsenite-, heat shock- and RNA-binding-dependent manner. Shuttles into
CC and out of SGs in an ATPase-dependent manner (By similarity).
CC Colocalizes in the cytosol with the multi-helicase-TICAM1 complex that
CC translocates to the mitochondria upon poly(I:C) stimulation (By
CC similarity). {ECO:0000250|UniProtKB:Q8VHK9,
CC ECO:0000250|UniProtKB:Q9H2U1}.
CC -!- DOMAIN: The DHX36-specific motif (DSM) form folds into a DNA-binding-
CC induced alpha-helix that together with the oligonucleotide and
CC oligosaccharide-binding-fold-like (OB-fold-like) subdomain bind to Myc-
CC promoter G4-DNA-containing structure in an ATP-dependent manner. Upon
CC G4-DNA-binding, DHX36 pulls on DSM in the 3'-direction, inducing
CC rearrangement of the RecA-like 1 and 2 and the degenerate-winged-helix
CC (WH) regions; these rearrangements are probably responsible for the
CC ATP-independent repetitive G4-DNA unfolding activity, one residue at a
CC time. Upon resolving of G4-DNA into separate nucleotide strands, and
CC ATP hydrolysis, the apoprotein of DHX36 seems incompatible with G4-DNA-
CC binding (By similarity). The N-terminus is necessary for its
CC recruitment to cytoplasmic stress granules (SGs) upon arsenite-induced
CC treatment (By similarity). {ECO:0000250|UniProtKB:Q05B79,
CC ECO:0000250|UniProtKB:Q9H2U1}.
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DR EMBL; AABR07010822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07010823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474003; EDM14820.1; -; Genomic_DNA.
DR RefSeq; NP_001101148.1; NM_001107678.1.
DR AlphaFoldDB; D4A2Z8; -.
DR SMR; D4A2Z8; -.
DR STRING; 10116.ENSRNOP00000019824; -.
DR iPTMnet; D4A2Z8; -.
DR PhosphoSitePlus; D4A2Z8; -.
DR jPOST; D4A2Z8; -.
DR PaxDb; D4A2Z8; -.
DR PeptideAtlas; D4A2Z8; -.
DR PRIDE; D4A2Z8; -.
DR Ensembl; ENSRNOT00000019824; ENSRNOP00000019824; ENSRNOG00000014599.
DR GeneID; 310461; -.
DR KEGG; rno:310461; -.
DR UCSC; RGD:1308767; rat.
DR CTD; 170506; -.
DR RGD; 1308767; Dhx36.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000156903; -.
DR HOGENOM; CLU_001832_1_4_1; -.
DR InParanoid; D4A2Z8; -.
DR OMA; GKMILMS; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; D4A2Z8; -.
DR TreeFam; TF324744; -.
DR Reactome; R-RNO-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR PRO; PR:D4A2Z8; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000234681; Chromosome 2.
DR Bgee; ENSRNOG00000014599; Expressed in thymus and 20 other tissues.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:RGD.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0051880; F:G-quadruplex DNA binding; ISS:UniProtKB.
DR GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
DR GO; GO:0070883; F:pre-miRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:RGD.
DR GO; GO:0070034; F:telomerase RNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1903843; P:cellular response to arsenite ion; ISO:RGD.
DR GO; GO:0034605; P:cellular response to heat; ISO:RGD.
DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0044806; P:G-quadruplex DNA unwinding; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:UniProtKB.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1901534; P:positive regulation of hematopoietic progenitor cell differentiation; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:RGD.
DR GO; GO:1904582; P:positive regulation of intracellular mRNA localization; IMP:UniProtKB.
DR GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; ISO:RGD.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:RGD.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:RGD.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0043330; P:response to exogenous dsRNA; ISO:RGD.
DR GO; GO:0009615; P:response to virus; ISO:RGD.
DR GO; GO:0010501; P:RNA secondary structure unwinding; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0090669; P:telomerase RNA stabilization; ISO:RGD.
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 Acetylation; Activator; Antiviral defense; ATP-binding; Cell projection;
KW Chromosome; Cytoplasm; Developmental protein; Differentiation; DNA-binding;
KW Helicase; Hydrolase; Immunity; Innate immunity; Magnesium; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Telomere;
KW Transcription; Transcription regulation; Translation regulation; Transport.
FT CHAIN 1..1000
FT /note="ATP-dependent DNA/RNA helicase DHX36"
FT /id="PRO_0000445445"
FT DOMAIN 209..379
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 469..639
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..192
FT /note="Necessary for nuclear and nucleolar caps
FT localizations"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 1..96
FT /note="Required for the pre-miR-134 transport"
FT /evidence="ECO:0000269|PubMed:23651854"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..43
FT /note="Required for recruitment to cytoplasmic stress
FT granules"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 45..97
FT /note="Required for G4-DNA- and G4-RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 45..67
FT /note="DSM (DHX36-specific motif)"
FT /evidence="ECO:0000250|UniProtKB:Q05B79,
FT ECO:0000250|UniProtKB:Q9H2U1"
FT REGION 98..378
FT /note="RecA-like domain 1"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 257..309
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 379..620
FT /note="RecA-like domain 2"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 490..549
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 621..690
FT /note="WH domain"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 630..689
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 833..897
FT /note="OB-fold-like subdomains"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 841..852
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT REGION 862..892
FT /note="Necessary for interaction with single-stranded DNA
FT at the 3'-end of the G4-DNA structure"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT MOTIF 326..329
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOTIF 509..520
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT BINDING 225..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT BINDING 549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT BINDING 594..597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q05B79"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
FT MOD_RES 939
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2U1"
SQ SEQUENCE 1000 AA; 113843 MW; B117F354EB148DE6 CRC64;
MSYDYHQSWS RDGGPRGSGQ GSGGGGGGSR GSGGGGGGRG GRGRHPAHLK GREIGLWYAK
KQTQKNKEAE RQERAVVHMD ERREEQIVQL LNSVQAKNDK DSEAQISWFA PEDHGYGTEV
SSEKKINSEK KLDNQEKKLL NQEKKTYRIT DKSYIDRDSE YLLQQNEPNL GLDQQLLEDL
QKKKTDPRYI EMQRFRKKLP SYGMQKELVN LINNHQVTVI SGETGCGKTT QVTQFILDNY
IERGIGSACR IVCTQPRRIS AISVAERVAA ERAESCGNGN STGYQIRLQS RLPRKQGSIL
YCTTGIILQW LQSDSRLSSV SHIVLDEIHE RNLQSDVLMT VIKDLLHFRS DLKVILMSAT
LNAEKFSEYF GNCPMIHIPG FTFPVVEYLL EDIIEKIRYF PEQKEHRSQF KRGFMQGHVN
RQEKEEKEAI YKERWPAYIK ELQTRYSAST IDVLEMMDDD KVDLNLIAAL IRYIVLEEED
GAILVFLPGW DNISTLHDLL MSQVMFKSDR FLIIPLHSLM PTVNQTQVFK KTPPGVRKIV
IATNIAETSI TIDDVVYVID GGKIKETHFD TQNNISTMSA EWVSKANAKQ RKGRAGRVQP
GHCYHLYNGL RASLLDDYQL PEILRTPLEE LCLQIKILRL GGIAYFLSRL MDPPSDEAVV
LSIKHLMELS ALDKQEELTP LGVHLARLPV EPHIGKMILF GALFCCLDPV LTIAASLSFK
DPFVIPLGKE KIADARRKEL AKETRSDHLT VVNAFEGWEE AKRRGFRYEK DYCWEYFLSS
NTLQMLHNMK GQFAEHLLGA GFVSSRSPKD PKANINSDNE KIIKAVICAG LYPKVAKIRL
NLGKKRKMVK VHTKSDGLVS IHPKSVNVEQ TDFHYNWLIY HLKMRTSSIY LYDCTEVSPY
CLLFFGGDIS IQKDKDQEII AVDEWIVFQS PERIAHLVKG LRKELDILLQ EKIECPHPVD
WNDTKSRDCA VLSAILDLIK TQEKAIPRNL PPRSQDGYYS
