DDX55_MOUSE
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 03-AUG-2022, entry version 127.
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; 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 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: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT 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., 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 [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 project:
RT 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 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 box
CC family of RNA helicases and controls ATP binding and 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};
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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 AlphaFoldDB; Q6ZPL9; -.
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 ProteomicsDB; 277971; -.
DR Antibodypedia; 19284; 169 antibodies from 25 providers.
DR DNASU; 67848; -.
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 VEuPathDB; HostDB:ENSMUSG00000029389; -.
DR eggNOG; KOG0331; Eukaryota.
DR eggNOG; KOG0345; Eukaryota.
DR GeneTree; ENSGT00550000074969; -.
DR InParanoid; Q6ZPL9; -.
DR OMA; DRAIHDK; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q6ZPL9; -.
DR TreeFam; TF314573; -.
DR BioGRID-ORCS; 67848; 27 hits in 78 CRISPR screens.
DR ChiTaRS; Ddx55; mouse.
DR PRO; PR:Q6ZPL9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6ZPL9; protein.
DR Bgee; ENSMUSG00000029389; Expressed in retinal neural layer and 151 other tissues.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 2.
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; Helicase; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..600
FT /note="ATP-dependent RNA helicase DDX55"
FT /id="PRO_0000252211"
FT DOMAIN 40..223
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 254..402
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 499..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..37
FT /note="Q motif"
FT MOTIF 171..174
FT /note="DEAD box"
FT COMPBIAS 499..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..535
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 482
FT /note="D -> H (in Ref. 3; AAI17787/AAI17788)"
FT /evidence="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
