DD19A_MOUSE
ID DD19A_MOUSE Reviewed; 478 AA.
AC Q61655; Q543M2; Q921R0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=ATP-dependent RNA helicase DDX19A;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9UMR2};
DE AltName: Full=DEAD box RNA helicase DEAD5;
DE Short=mDEAD5;
DE AltName: Full=DEAD box protein 19A;
DE AltName: Full=Eukaryotic translation initiation factor 4A-related sequence 1;
GN Name=Ddx19a; Synonyms=Ddx19, Eif4a-rs1;
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 [MRNA].
RC TISSUE=Erythroleukemia;
RX PubMed=8144024; DOI=10.1016/0378-1119(94)90541-x;
RA Gee S.L., Conboy J.G.;
RT "Mouse erythroid cells express multiple putative RNA helicase genes
RT exhibiting high sequence conservation from yeast to mammals.";
RL Gene 140:171-177(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Stomach;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, Pancreas, Spleen, and Testis;
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: ATP-dependent RNA helicase involved in mRNA export from the
CC nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a
CC remodeler of ribonucleoprotein particles, whereby proteins bound to
CC nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding
CC proteins. {ECO:0000250|UniProtKB:Q9UMR2}.
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:Q9UMR2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UMR2}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UMR2}. Note=Associates
CC with the nuclear pore complex cytoplasmic fibrils.
CC {ECO:0000250|UniProtKB:Q9UMR2}.
CC -!- TISSUE SPECIFICITY: Found in testis, heart, brain, liver, skeletal
CC muscle, and kidney.
CC -!- DOMAIN: The N-terminal extension helix acts as an autoinhibitory
CC domain, preventing ATP hydrolysis, unless the N-terminus of the protein
CC is displaced by RNA binding, allowing cleft closure to bring key side
CC chains into position for catalysis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5
CC subfamily. {ECO:0000305}.
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DR EMBL; L25125; AAA53629.1; -; mRNA.
DR EMBL; AK049467; BAC33762.1; -; mRNA.
DR EMBL; AK146548; BAE27252.1; -; mRNA.
DR EMBL; CH466525; EDL11480.1; -; Genomic_DNA.
DR EMBL; BC011270; AAH11270.1; -; mRNA.
DR CCDS; CCDS22668.1; -.
DR PIR; I49731; I49731.
DR RefSeq; NP_031942.2; NM_007916.2.
DR AlphaFoldDB; Q61655; -.
DR SMR; Q61655; -.
DR BioGRID; 199417; 7.
DR IntAct; Q61655; 1.
DR STRING; 10090.ENSMUSP00000047898; -.
DR iPTMnet; Q61655; -.
DR PhosphoSitePlus; Q61655; -.
DR SwissPalm; Q61655; -.
DR REPRODUCTION-2DPAGE; Q61655; -.
DR EPD; Q61655; -.
DR jPOST; Q61655; -.
DR MaxQB; Q61655; -.
DR PaxDb; Q61655; -.
DR PeptideAtlas; Q61655; -.
DR PRIDE; Q61655; -.
DR ProteomicsDB; 277966; -.
DR Antibodypedia; 16355; 100 antibodies from 19 providers.
DR DNASU; 13680; -.
DR Ensembl; ENSMUST00000040416; ENSMUSP00000047898; ENSMUSG00000015023.
DR GeneID; 13680; -.
DR KEGG; mmu:13680; -.
DR UCSC; uc009nll.2; mouse.
DR CTD; 55308; -.
DR MGI; MGI:99526; Ddx19a.
DR VEuPathDB; HostDB:ENSMUSG00000015023; -.
DR eggNOG; KOG0332; Eukaryota.
DR GeneTree; ENSGT00940000154417; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q61655; -.
DR OMA; MDIPQVN; -.
DR OrthoDB; 608788at2759; -.
DR PhylomeDB; Q61655; -.
DR TreeFam; TF314957; -.
DR BioGRID-ORCS; 13680; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Ddx19a; mouse.
DR PRO; PR:Q61655; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61655; protein.
DR Bgee; ENSMUSG00000015023; Expressed in animal zygote and 254 other tissues.
DR Genevisible; Q61655; MM.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 2.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NUU7"
FT CHAIN 2..478
FT /note="ATP-dependent RNA helicase DDX19A"
FT /id="PRO_0000055023"
FT DOMAIN 124..294
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 305..473
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 2..299
FT /note="N-terminal lobe"
FT /evidence="ECO:0000250"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..67
FT /note="N-terminal helix"
FT /evidence="ECO:0000250"
FT REGION 300..478
FT /note="C-terminal lobe"
FT /evidence="ECO:0000250"
FT MOTIF 91..119
FT /note="Q motif"
FT MOTIF 241..244
FT /note="DEAD box"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 428
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUU7"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY15"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NUU7"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NUU7"
FT CONFLICT 30..32
FT /note="VKA -> AKS (in Ref. 1; AAA53629)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..263
FT /note="ML -> IV (in Ref. 1; AAA53629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 53933 MW; 46BDE331544EDA7E CRC64;
MATDSWALAV DEQEAAVKSM SSLQIKEEKV KADTNGVIKT STTAEKTEEE EKEDRAAQSL
LNKLIRSNLV DNTNQVEVLQ RDPSSPLYSV KSFEELRLKP QLLQGVYAMG FNRPSKIQEN
ALPMMLAEPP QNLIAQSQSG TGKTAAFVLA MLSRVEPADR YPQCLCLSPT YELALQTGKV
IEQMGKFHPE LKLAYAVRGN KLERGQKVSE QIVIGTPGTV LDWCSKLKFI DPKKIKVFVL
DEADVMIATQ GHQDQSIRIQ RMLPRNCQML LFSATFEDSV WKFAQKVVPD PNIIKLKREE
ETLDTIKQYY VLCNNREEKF QALCNLYGAI TIAQAMIFCH TRKTASWLAA ELSKEGHQVA
LLSGEMMVEQ RAAVIERFRE GKEKVLVTTN VCARGIDVEQ VSVVINFDLP VDKDGNPDNE
TYLHRIGRTG RFGKRGLAVN MVDSKHSMNI LNRIQEHFNK KIERLDTDDL DEIEKIAN
