DX39A_RAT
ID DX39A_RAT Reviewed; 427 AA.
AC Q5U216; O70498;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=ATP-dependent RNA helicase DDX39A;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 39;
DE AltName: Full=Nuclear RNA helicase, DECD variant of DEAD box family;
GN Name=Ddx39a; Synonyms=Ddx39, Ddxl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer;
RA Shimizu T.;
RT "Cellular genes modulated by a transactivator Tax of HTLV-1.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD subfamily.
CC {ECO:0000305}.
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DR EMBL; AF063447; AAC16391.1; -; mRNA.
DR EMBL; BC086328; AAH86328.1; -; mRNA.
DR RefSeq; NP_446015.2; NM_053563.2.
DR RefSeq; XP_006255376.1; XM_006255314.3.
DR AlphaFoldDB; Q5U216; -.
DR SMR; Q5U216; -.
DR BioGRID; 250149; 1.
DR STRING; 10116.ENSRNOP00000040666; -.
DR iPTMnet; Q5U216; -.
DR PhosphoSitePlus; Q5U216; -.
DR jPOST; Q5U216; -.
DR PaxDb; Q5U216; -.
DR PRIDE; Q5U216; -.
DR Ensembl; ENSRNOT00000090312; ENSRNOP00000068949; ENSRNOG00000004373.
DR GeneID; 89827; -.
DR KEGG; rno:89827; -.
DR CTD; 10212; -.
DR RGD; 619920; Ddx39a.
DR eggNOG; KOG0329; Eukaryota.
DR GeneTree; ENSGT00940000154912; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q5U216; -.
DR OMA; INFELPM; -.
DR OrthoDB; 779000at2759; -.
DR PhylomeDB; Q5U216; -.
DR TreeFam; TF300442; -.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-72187; mRNA 3'-end processing.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR PRO; PR:Q5U216; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000004373; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5U216; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Helicase; Hydrolase; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; 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_0000055069"
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..35
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 CONFLICT 130
FT /note="K -> T (in Ref. 1; AAC16391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 49109 MW; DB384747418FF290 CRC64;
MAEQDVENEL LDYDEDEEPQ VPQESTPAPP KKDVKGSYVS IHSSGFRDFL LKPELLRAIV
DCGFEHPSEV QHECIPQAIL GMDVLCQAKS GMGKTAVFVL ATLQQIEPIN 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
