GenomeNet

Database: UniProt
Entry: Q6ZPL9
LinkDB: Q6ZPL9
Original site: Q6ZPL9 
ID   DDX55_MOUSE             Reviewed;         600 AA.
AC   Q6ZPL9; Q149H5; Q3U460; Q8BZR1;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   13-NOV-2019, entry version 114.
DE   RecName: Full=ATP-dependent RNA helicase DDX55;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 55;
GN   Name=Ddx55; Synonyms=Kiaa1595;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cecum;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-594, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-594, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, Pancreas, and Spleen;
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Probable ATP-binding RNA helicase.
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   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98212.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE32574.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AK129402; BAC98212.1; ALT_INIT; mRNA.
DR   EMBL; AK033741; BAC28459.1; -; mRNA.
DR   EMBL; AK154422; BAE32574.1; ALT_INIT; mRNA.
DR   EMBL; BC117786; AAI17787.1; -; mRNA.
DR   EMBL; BC117787; AAI17788.1; -; mRNA.
DR   CCDS; CCDS39281.1; -.
DR   RefSeq; NP_080685.2; NM_026409.4.
DR   SMR; Q6ZPL9; -.
DR   BioGrid; 212478; 1.
DR   IntAct; Q6ZPL9; 2.
DR   STRING; 10090.ENSMUSP00000070279; -.
DR   iPTMnet; Q6ZPL9; -.
DR   PhosphoSitePlus; Q6ZPL9; -.
DR   EPD; Q6ZPL9; -.
DR   jPOST; Q6ZPL9; -.
DR   MaxQB; Q6ZPL9; -.
DR   PaxDb; Q6ZPL9; -.
DR   PeptideAtlas; Q6ZPL9; -.
DR   PRIDE; Q6ZPL9; -.
DR   Ensembl; ENSMUST00000071057; ENSMUSP00000070279; ENSMUSG00000029389.
DR   GeneID; 67848; -.
DR   KEGG; mmu:67848; -.
DR   UCSC; uc008zqc.2; mouse.
DR   CTD; 57696; -.
DR   MGI; MGI:1915098; Ddx55.
DR   eggNOG; KOG0345; Eukaryota.
DR   eggNOG; ENOG410XNT7; LUCA.
DR   GeneTree; ENSGT00550000074969; -.
DR   HOGENOM; HOG000268803; -.
DR   InParanoid; Q6ZPL9; -.
DR   KO; K14809; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; Q6ZPL9; -.
DR   TreeFam; TF314573; -.
DR   ChiTaRS; Ddx55; mouse.
DR   PRO; PR:Q6ZPL9; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000029389; Expressed in 168 organ(s), highest expression level in embryo.
DR   ExpressionAtlas; Q6ZPL9; baseline and differential.
DR   Genevisible; Q6ZPL9; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; RNA-binding.
FT   CHAIN         1    600       ATP-dependent RNA helicase DDX55.
FT                                /FTId=PRO_0000252211.
FT   DOMAIN       40    223       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      254    402       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      53     60       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF         9     37       Q motif.
FT   MOTIF       171    174       DEAD box.
FT   COMPBIAS    487    568       Lys-rich.
FT   MOD_RES     544    544       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     594    594       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   CONFLICT    482    482       D -> H (in Ref. 3; AAI17787/AAI17788).
FT                                {ECO:0000305}.
SQ   SEQUENCE   600 AA;  68465 MW;  7CEBB0F4C33A1469 CRC64;
     MEHVTEGAWE SLQVPLHPRV LGALRELGFP HMTPVQSATI PLFMKNKDVA AEAVTGSGKT
     LAFVIPILEI LLRREEKLKK NQVGAIVITP TRELAIQIDE VLSHFTKHFP QFSQILWIGG
     RNPGEDVERF KQHGGNIIVA TPGRLEDMFR RKAEGLDLAS CVKSLDVLVL DEADRLLDMG
     FEASINTILE FLPKQRRTGL FSATQTQEVE NLVRAGLRNP VRISVKEKGV AASSTQKTPS
     RLENHYMICK ADEKFNQLVH FLRSRQQEKH LVFFSTCACV EYYGKALEAL LKKVKILCIH
     GKMKYKRNKI FMEFRKLQSG ILVCTDVMAR GIDIPEVNWV LQYDPPSNAS AFVHRCGRTA
     RIGHGGSALV FLLPMEEAYI NFLAINQKCP LQEMSLQRNT IDLLPKLRAM ALADRAVFEK
     GMKAFVSFVQ AYAKHECSLI FRLKDLDFAG LARGFALLRM PRMPELRGKQ FPDFVPVDID
     TDTIPFKDKI REKQRQKLLE QKRKERSENE GRKKFIKNKA WSKQKAKKER KKKMNAKRKK
     DEGSDIDDED MEELLNDTRL LKKFKKGKIT EEEFEKGLLT SAKRTVQLTD LGVSDLEEDS
//
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