DHX30_RAT
ID DHX30_RAT Reviewed; 1194 AA.
AC Q5BJS0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=ATP-dependent RNA helicase DHX30 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q7L2E3};
DE AltName: Full=DEAH box protein 30;
GN Name=Dhx30;
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 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).
RN [2]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP ZC3HAV1.
RX PubMed=21204022; DOI=10.1007/s13238-010-0117-8;
RA Ye P., Liu S., Zhu Y., Chen G., Gao G.;
RT "DEXH-Box protein DHX30 is required for optimal function of the zinc-finger
RT antiviral protein.";
RL Protein Cell 1:956-964(2010).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: RNA-dependent helicase (By similarity). Plays an important
CC role in the assembly of the mitochondrial large ribosomal subunit (By
CC similarity). Associates with mitochondrial DNA (By similarity).
CC Required for optimal function of the zinc-finger antiviral protein
CC ZC3HAV1 (PubMed:21204022). Involved in nervous system development and
CC differentiation through its involvement in the up-regulation of a
CC number of genes which are required for neurogenesis, including GSC,
CC NCAM1, neurogenin, and NEUROD (By similarity).
CC {ECO:0000250|UniProtKB:Q7L2E3, ECO:0000250|UniProtKB:Q99PU8,
CC ECO:0000269|PubMed:21204022}.
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:Q7L2E3};
CC -!- SUBUNIT: Identified in a complex with TFAM and SSBP1 (By similarity).
CC Interacts (via N-terminus) with ZC3HAV1 (via N-terminal domain) in an
CC RNA-independent manner. Found in a complex with GRSF1, DDX28, FASTKD2
CC and FASTKD5 (By similarity). {ECO:0000250|UniProtKB:Q7L2E3,
CC ECO:0000269|PubMed:21204022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L2E3}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q7L2E3}. Mitochondrion matrix,
CC mitochondrion nucleoid {ECO:0000250|UniProtKB:Q7L2E3}. Note=Localizes
CC to mitochondrial RNA granules found in close proximity to the
CC mitochondrial nucleoids. Relocalizes to stress granules upon heat
CC stress. {ECO:0000250|UniProtKB:Q7L2E3}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; BC091359; AAH91359.1; -; mRNA.
DR RefSeq; NP_001013267.1; NM_001013249.1.
DR RefSeq; XP_017451287.1; XM_017595798.1.
DR RefSeq; XP_017451288.1; XM_017595799.1.
DR RefSeq; XP_017451289.1; XM_017595800.1.
DR AlphaFoldDB; Q5BJS0; -.
DR SMR; Q5BJS0; -.
DR BioGRID; 266361; 1.
DR STRING; 10116.ENSRNOP00000043896; -.
DR iPTMnet; Q5BJS0; -.
DR PhosphoSitePlus; Q5BJS0; -.
DR jPOST; Q5BJS0; -.
DR PaxDb; Q5BJS0; -.
DR PRIDE; Q5BJS0; -.
DR GeneID; 367172; -.
DR KEGG; rno:367172; -.
DR UCSC; RGD:1308888; rat.
DR CTD; 22907; -.
DR RGD; 1308888; Dhx30.
DR VEuPathDB; HostDB:ENSRNOG00000029194; -.
DR eggNOG; KOG0920; Eukaryota.
DR InParanoid; Q5BJS0; -.
DR OMA; QYSCTEH; -.
DR OrthoDB; 278674at2759; -.
DR PRO; PR:Q5BJS0; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000029194; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q5BJS0; baseline and differential.
DR Genevisible; Q5BJS0; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0035770; C:ribonucleoprotein granule; 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:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; ISS:UniProtKB.
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; Cytoplasm; Helicase; Hydrolase; Mitochondrion;
KW Mitochondrion nucleoid; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..1194
FT /note="ATP-dependent RNA helicase DHX30"
FT /id="PRO_0000245541"
FT DOMAIN 53..121
FT /note="DRBM"
FT DOMAIN 444..612
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 654..827
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 153..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 559..562
FT /note="DEAH box"
FT BINDING 457..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L2E3"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L2E3"
SQ SEQUENCE 1194 AA; 133997 MW; A453E243EB1A5929 CRC64;
MFTLDSFRKD RTQHRQRQCK LPPPRLPPMC VNPAPGGTIS RASRDLLKEF PQPKNLLNSV
IGRALGISHA KDKLVYVHTN GPKKKKVTLH IKWPKSVEVE GYGSKKIDAE RQAAAAACQL
FKGWGLLGPR NELFDAAKYR VLADRFGSPA DSWWRPEPTM PPTSWRQLNP ENIRPAGTGG
LSRSLGREEE EDEEEELEEG TIDVTEFLSM TQQDSHNPLR DSRGGSFEMT DDDSAIRALT
QFPLPKNLLA KVIQIATSSS TAKNLMQFHT VGTKTKLATL TLLWPCPMTF VAKGRRKAEA
ENKAAALACK KLKSLGLVDR NNEPLTHAMY NLASLRELGE TQRRPCTIQV PEPILRKIEA
FLSHYPVDSS WISPELRLQS DDILPLGKDS GPLSDPITGK PYMPLSEAEE VRLSQSLLEL
WRRRGPIWQE APQLPVDPHR DTILSAIEQH PVVVISGDTG CGKTTRIPQL LLERYVTEGR
GARCNVIITQ PRRISAVSVA QRVSHELGPS LRRNVGFQVR LESKPPARGG ALLFCTVGIL
LRKLQSNPSL EGVSHVIVDE VHERDVNTDF LLILLKGLQR LNPALRLVLM SATGDNERFS
RYFGGCPVIK VPGFMYPVKE HYLEDILAKL GKHQYPHRHR HHESEDECAL DLDLVTDLVL
HIDARGEPGG ILCFLPGWQE IKGVQQRLQE ALGMHESKYL ILPVHSNIPM MDQKAIFQQP
PLGVRKIVLA TNIAETSITV NDIVHVVDSG LHKEERYDLK TKVSCLETVW VSRANVIQRR
GRAGRCQSGF AYHLFPRSRL EKMVPFQVPE ILRTPLENLV LQAKIHMPEK TAVEFLSKAV
DSPNIKAVDE AVILLQEIGV LDQREYLTTL GQRLAHISTD PRLAKAIVLA AIFRCLHPLL
VVVSCLTRDP FSSSLQNRAE VDKVKALLSH DSGSDHLAFV RAVAGWEEVL RWQDRTSREN
YLEENLLYAP SLRFIHGLIK QFSENIYEAF LVGKPSDCTL PSAQCNEYSE EEELVKGVLM
AGLYPNLIQV RQGKVTRQGK FKPNSVTYRT KSGNILLHKS TINREATRLR SRWLTYFMAV
KSNGSVFVRD SSQVHPLAVL LLTDGDVHIR DDGRRATISL SDSDLLRLEG DSRTVRLLRE
LRRALGRMVE RSLRSELAAL PLSVQQEHGQ LLALLAELLR GPCGSFDVRK TADD
