DX39A_MOUSE
ID DX39A_MOUSE Reviewed; 427 AA.
AC Q8VDW0; Q3UJV4; Q8C2C2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=ATP-dependent RNA helicase DDX39A;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 39;
GN Name=Ddx39a {ECO:0000312|MGI:MGI:1915528};
GN Synonyms=Ddx39 {ECO:0000312|MGI:MGI:1915528};
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] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ, C57BL/6J, and NOD; TISSUE=Bone marrow, Liver, and Thymus;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, 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: Involved in pre-mRNA splicing. Required for the export of
CC mRNA out of the nucleus (By similarity). {ECO:0000250}.
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: Binds ALYREF/THOC4 and DDX39B/BAT1 (By similarity). Interacts
CC with SARNP (By similarity). Interacts with MX1 (By similarity).
CC Interacts with MCM3AP (By similarity). {ECO:0000250|UniProtKB:O00148}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Can translocate to the cytoplasm in the presence of MX1.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VDW0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VDW0-2; Sequence=VSP_013064;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC {ECO:0000305}.
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DR EMBL; AK088894; BAC40637.1; -; mRNA.
DR EMBL; AK145927; BAE26758.1; -; mRNA.
DR EMBL; AK146294; BAE27051.1; -; mRNA.
DR EMBL; AK150997; BAE30021.1; -; mRNA.
DR EMBL; AK162752; BAE37049.1; -; mRNA.
DR EMBL; AK168079; BAE40052.1; -; mRNA.
DR EMBL; BC020134; AAH20134.1; -; mRNA.
DR CCDS; CCDS22460.1; -. [Q8VDW0-1]
DR RefSeq; NP_932099.2; NM_197982.3. [Q8VDW0-1]
DR RefSeq; XP_006531395.1; XM_006531332.3.
DR AlphaFoldDB; Q8VDW0; -.
DR SMR; Q8VDW0; -.
DR BioGRID; 212781; 19.
DR STRING; 10090.ENSMUSP00000019576; -.
DR iPTMnet; Q8VDW0; -.
DR PhosphoSitePlus; Q8VDW0; -.
DR SwissPalm; Q8VDW0; -.
DR EPD; Q8VDW0; -.
DR jPOST; Q8VDW0; -.
DR MaxQB; Q8VDW0; -.
DR PaxDb; Q8VDW0; -.
DR PeptideAtlas; Q8VDW0; -.
DR PRIDE; Q8VDW0; -.
DR ProteomicsDB; 275415; -. [Q8VDW0-1]
DR ProteomicsDB; 275416; -. [Q8VDW0-2]
DR TopDownProteomics; Q8VDW0-1; -. [Q8VDW0-1]
DR Antibodypedia; 13684; 148 antibodies from 26 providers.
DR DNASU; 68278; -.
DR Ensembl; ENSMUST00000019576; ENSMUSP00000019576; ENSMUSG00000005481. [Q8VDW0-1]
DR Ensembl; ENSMUST00000109810; ENSMUSP00000105435; ENSMUSG00000005481. [Q8VDW0-1]
DR Ensembl; ENSMUST00000172396; ENSMUSP00000132222; ENSMUSG00000005481. [Q8VDW0-1]
DR Ensembl; ENSMUST00000212949; ENSMUSP00000148329; ENSMUSG00000005481. [Q8VDW0-1]
DR GeneID; 68278; -.
DR KEGG; mmu:68278; -.
DR UCSC; uc009mla.2; mouse. [Q8VDW0-1]
DR CTD; 10212; -.
DR MGI; MGI:1915528; Ddx39a.
DR VEuPathDB; HostDB:ENSMUSG00000005481; -.
DR eggNOG; KOG0329; Eukaryota.
DR GeneTree; ENSGT00940000154912; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q8VDW0; -.
DR OMA; INFELPM; -.
DR OrthoDB; 779000at2759; -.
DR PhylomeDB; Q8VDW0; -.
DR TreeFam; TF300442; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 68278; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Ddx39; mouse.
DR PRO; PR:Q8VDW0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8VDW0; protein.
DR Bgee; ENSMUSG00000005481; Expressed in cleaving embryo and 257 other tissues.
DR ExpressionAtlas; Q8VDW0; baseline and differential.
DR Genevisible; Q8VDW0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; ISO:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:MGI.
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; Alternative splicing; ATP-binding; Cytoplasm; Helicase;
KW Hydrolase; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT CHAIN 2..427
FT /note="ATP-dependent RNA helicase DDX39A"
FT /id="PRO_0000055068"
FT DOMAIN 75..248
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 260..421
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 44..72
FT /note="Q motif"
FT MOTIF 195..198
FT /note="DECD box"
FT COMPBIAS 1..21
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT MOD_RES 35
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT CROSSLNK 31
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT CROSSLNK 162
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00148"
FT VAR_SEQ 1..245
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013064"
SQ SEQUENCE 427 AA; 49067 MW; 4A94699142FCABA8 CRC64;
MAEQDVENEL LDYDEDEEPQ APQESTPAPP KKDVKGSYVS IHSSGFRDFL LKPELLRAIV
DCGFEHPSEV QHECIPQAIL GMDVLCQAKS GMGKTAVFVL ATLQQIEPVN GQVSVLVMCH
TRELAFQISK EYERFSKYMP SVKVSVFFGG LSIKKDEDVL KKNCPHVVVG TPGRILALVR
SRSLNLRNVK HFVLDECDKM LEQLDMRRDV QEIFRLTPHE KQCMMFSATL SKEIRPVCRK
FMQDPMEVFV DDETKLTLHG LQQYYVKLKD SEKNRKLFDL LDVLEFNQVV IFVKSVQRCM
ALAQLLVEQN FPAIAIHRGM AQEERLSRYQ QFKDFQRRIL VATNLFGRGM DIERVNIVFN
YDMPEDSDTY LHRVARAGRF GTKGLAVTFV SDENDAKILN DVQDRFEVNV AELPEEIDIS
TYIEQSR
