GenomeNet

Database: UniProt
Entry: Q5BJS0
LinkDB: Q5BJS0
Original site: Q5BJS0 
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   16-OCT-2019, entry version 110.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   project: 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-
RT   finger antiviral protein.";
RL   Protein Cell 1:956-964(2010).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: RNA-dependent helicase (By similarity). Plays an
CC       important role in the assembly of the mitochondrial large
CC       ribosomal subunit (By similarity). Associates with mitochondrial
CC       DNA (By similarity). Required for optimal function of the zinc-
CC       finger antiviral protein ZC3HAV1 (PubMed:21204022). Involved in
CC       nervous system development and differentiation through its
CC       involvement in the up-regulation of a number of genes which are
CC       required for neurogenesis, including GSC, NCAM1, neurogenin, and
CC       NEUROD (By similarity). {ECO:0000250|UniProtKB:Q7L2E3,
CC       ECO:0000250|UniProtKB:Q99PU8, 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
CC       similarity). Interacts (via N-terminus) with ZC3HAV1 (via N-
CC       terminal domain) in an RNA-independent manner. Found in a complex
CC       with GRSF1, DDX28, FASTKD2 and FASTKD5 (By similarity).
CC       {ECO:0000250|UniProtKB:Q7L2E3, ECO:0000269|PubMed:21204022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q7L2E3}.
CC       Mitochondrion {ECO:0000250|UniProtKB:Q7L2E3}. Mitochondrion
CC       matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q7L2E3}.
CC       Note=Localizes to mitochondrial RNA granules found in close
CC       proximity to the mitochondrial nucleoids. Relocalizes to stress
CC       granules upon heat stress. {ECO:0000250|UniProtKB:Q7L2E3}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. {ECO:0000305}.
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   SMR; Q5BJS0; -.
DR   STRING; 10116.ENSRNOP00000043896; -.
DR   iPTMnet; Q5BJS0; -.
DR   PhosphoSitePlus; Q5BJS0; -.
DR   jPOST; Q5BJS0; -.
DR   PaxDb; Q5BJS0; -.
DR   PRIDE; Q5BJS0; -.
DR   Ensembl; ENSRNOT00000048764; ENSRNOP00000043896; ENSRNOG00000029194.
DR   GeneID; 367172; -.
DR   KEGG; rno:367172; -.
DR   UCSC; RGD:1308888; rat.
DR   CTD; 22907; -.
DR   RGD; 1308888; Dhx30.
DR   eggNOG; KOG0920; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   GeneTree; ENSGT00940000158279; -.
DR   HOGENOM; HOG000112212; -.
DR   InParanoid; Q5BJS0; -.
DR   KO; K13185; -.
DR   OMA; FIRDSSA; -.
DR   OrthoDB; 278674at2759; -.
DR   PRO; PR:Q5BJS0; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000029194; Expressed in 10 organ(s), highest expression level in testis.
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:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
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   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Ribosome biogenesis; RNA-binding.
FT   CHAIN         1   1194       ATP-dependent RNA helicase DHX30.
FT                                /FTId=PRO_0000245541.
FT   DOMAIN       53    121       DRBM.
FT   DOMAIN      444    612       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      654    827       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     457    464       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       559    562       DEAH box.
FT   COMPBIAS    188    199       Poly-Glu.
FT   COMPBIAS   1010   1013       Poly-Glu.
FT   MOD_RES       6      6       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q7L2E3}.
FT   MOD_RES     226    226       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     380    380       Phosphoserine.
FT                                {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
//
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