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   27-MAR-2024, entry version 193.
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; 10090-ENSMUSP00000047898; -.
DR   PeptideAtlas; Q61655; -.
DR   ProteomicsDB; 277966; -.
DR   Pumba; Q61655; -.
DR   Antibodypedia; 16355; 123 antibodies from 19 providers.
DR   DNASU; 13680; -.
DR   Ensembl; ENSMUST00000040416.8; ENSMUSP00000047898.8; ENSMUSG00000015023.8.
DR   GeneID; 13680; -.
DR   KEGG; mmu:13680; -.
DR   UCSC; uc009nll.2; mouse.
DR   AGR; MGI:99526; -.
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; LPMHAET; -.
DR   OrthoDB; 1087080at2759; -.
DR   PhylomeDB; Q61655; -.
DR   TreeFam; TF314957; -.
DR   BioGRID-ORCS; 13680; 24 hits in 78 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 258 other cell types or tissues.
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   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 6.10.250.2170; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF175; ATP-DEPENDENT RNA HELICASE DDX19A; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
DR   Genevisible; Q61655; MM.
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
//