GenomeNet

Database: UniProt
Entry: Q9CWT6
LinkDB: Q9CWT6
Original site: Q9CWT6 
ID   DDX28_MOUSE             Reviewed;         540 AA.
AC   Q9CWT6; Q0VBM0; Q3TQM0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   11-DEC-2019, entry version 135.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX28;
DE            EC=3.6.4.13;
DE   AltName: Full=Mitochondrial DEAD box protein 28;
GN   Name=Ddx28;
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=Corpora quadrigemina, and Embryonic stem cell;
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 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).
CC   -!- FUNCTION: Plays an essential role in facilitating the proper assembly
CC       of the mitochondrial large ribosomal subunit and its helicase activity
CC       is essential for this function. May be involved in RNA processing or
CC       transport. Has RNA and Mg(2+)-dependent ATPase activity (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NUL7}.
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: Monomer. Found in a complex with GRSF1, DHX30, FASTKD2 and
CC       FASTKD5. Associates with the 16S mitochondrial rRNA (16S mt-rRNA) and
CC       with the mitochondrial ribosome large subunit (39S).
CC       {ECO:0000250|UniProtKB:Q9NUL7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NUL7}.
CC       Mitochondrion {ECO:0000250|UniProtKB:Q9NUL7}. Mitochondrion matrix,
CC       mitochondrion nucleoid {ECO:0000250|UniProtKB:Q9NUL7}. Mitochondrion
CC       matrix {ECO:0000250|UniProtKB:Q9NUL7}. Note=Transported between these
CC       two compartments. Nuclear localization depends on active RNA polymerase
CC       II transcription. Localizes to mitochondrial RNA granules found in
CC       close proximity to the mitochondrial nucleoids (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NUL7}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
DR   EMBL; AK010396; BAB26907.1; -; mRNA.
DR   EMBL; AK163480; BAE37362.1; -; mRNA.
DR   EMBL; BC120556; AAI20557.1; -; mRNA.
DR   EMBL; BC120582; AAI20583.1; -; mRNA.
DR   CCDS; CCDS22626.1; -.
DR   RefSeq; NP_082314.2; NM_028038.3.
DR   SMR; Q9CWT6; -.
DR   BioGrid; 215075; 1.
DR   STRING; 10090.ENSMUSP00000058950; -.
DR   iPTMnet; Q9CWT6; -.
DR   PhosphoSitePlus; Q9CWT6; -.
DR   EPD; Q9CWT6; -.
DR   MaxQB; Q9CWT6; -.
DR   PaxDb; Q9CWT6; -.
DR   PeptideAtlas; Q9CWT6; -.
DR   PRIDE; Q9CWT6; -.
DR   Ensembl; ENSMUST00000058579; ENSMUSP00000058950; ENSMUSG00000045538.
DR   GeneID; 71986; -.
DR   KEGG; mmu:71986; -.
DR   UCSC; uc009nez.2; mouse.
DR   CTD; 55794; -.
DR   MGI; MGI:1919236; Ddx28.
DR   eggNOG; KOG0330; Eukaryota.
DR   eggNOG; ENOG410XQU7; LUCA.
DR   GeneTree; ENSGT00940000161738; -.
DR   HOGENOM; HOG000008689; -.
DR   InParanoid; Q9CWT6; -.
DR   KO; K20096; -.
DR   OMA; TDYIHRA; -.
DR   OrthoDB; 1223767at2759; -.
DR   TreeFam; TF324977; -.
DR   ChiTaRS; Ddx28; mouse.
DR   PRO; PR:Q9CWT6; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9CWT6; protein.
DR   Bgee; ENSMUSG00000045538; Expressed in 221 organ(s), highest expression level in oocyte.
DR   Genevisible; Q9CWT6; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR   GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; ISS:UniProtKB.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 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.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Mitochondrion; Mitochondrion nucleoid;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..540
FT                   /note="Probable ATP-dependent RNA helicase DDX28"
FT                   /id="PRO_0000055035"
FT   DOMAIN          159..351
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          377..536
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         172..179
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           3..18
FT                   /note="Mitochondrial targeting signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           126..156
FT                   /note="Q motif"
FT   MOTIF           180..191
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           286..289
FT                   /note="DEAD"
FT   MOTIF           520..523
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        13
FT                   /note="A -> V (in Ref. 1; BAB26907)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   540 AA;  59515 MW;  A31891A909354A2E CRC64;
     MALAGPSRLL ALAVRLLLEP RRNLVVRGSD QSLPVVRVPR ALQRRQEQRQ SGRGSLQRPV
     LVRPGPLLVS ARRPELNQPA RLTLGRWERA PLASRGWKHR RSRQDHFSIE RVQQEAPALR
     NLSSRGSFVD LGLEPRVLLA LQEAVPEVVQ PTSVQSKTIP PLLRGRHLLC AAETGSGKTL
     SYLLPLFQRL LRGSDLDSRS FTAPRGLVLV PSRELAEQVQ AVAQSLGGYL GLQVIELGGG
     LGMSRLKLQL YRRPAADVLV ATPGALWKAL KSQLISLQHL NFIVLDEVDT LLDESFLELV
     DYILEKSPIA ESPAELEDPF NPKAQLVLVG ATFPEGLNQL LSKVTSPDSL TTITSSKLHC
     LMPHVRQTFM RLKGADKVTE LVQILKQQDK ASKTEPSGTV LVFCNSASTV NWLGYILDDH
     KIQHLRLQGQ MPASMRAGIF QSFQKGSQNI LVCTDIASRG LDSVHVEVVI NYDFPPTLQD
     YIHRAGRVGR VGSEVPGSVI SFVTHPWDVS LVQKIELAAR RRRSLPGLAS SVGDPLPQKA
//
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