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Database: UniProt
Entry: Q29024
LinkDB: Q29024
Original site: Q29024 
ID   DX39B_PIG               Reviewed;         428 AA.
AC   Q29024;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   16-OCT-2019, entry version 134.
DE   RecName: Full=Spliceosome RNA helicase DDX39B;
DE            EC=3.6.4.13;
DE   AltName: Full=56 kDa U2AF65-associated protein;
DE   AltName: Full=DEAD box protein UAP56;
GN   Name=DDX39B; Synonyms=BAT1, UAP56;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7601445; DOI=10.1016/0888-7543(95)80203-x;
RA   Peelman L., Chardon P., Nunes M., Renard C., Geffrotin C., Vaiman M.,
RA   van Zeveren A., Coppieters W., van de Weghe A., Bouquet Y., Choy W.,
RA   Strominger J., Spies T.;
RT   "The BAT1 gene in the MHC encodes an evolutionarily conserved putative
RT   nuclear RNA helicase of the DEAD family.";
RL   Genomics 26:210-218(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Large white; TISSUE=Fibroblast;
RX   PubMed=11169259; DOI=10.1034/j.1399-0039.2001.057001055.x;
RA   Chardon P., Rogel-Gaillard C., Cattolico L., Duprat S., Vaiman M.,
RA   Renard C.;
RT   "Sequence of the swine major histocompatibility complex region
RT   containing all non-classical class I genes.";
RL   Tissue Antigens 57:55-65(2001).
CC   -!- FUNCTION: Involved in nuclear export of spliced and unspliced
CC       mRNA. Assembling component of the TREX complex which is thought to
CC       couple mRNA transcription, processing and nuclear export, and
CC       specifically associates with spliced mRNA and not with unspliced
CC       pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-
CC       independent mechanism, binds to mRNA upstream of the exon-junction
CC       complex (EJC) and is recruited in a splicing- and cap-dependent
CC       manner to a region near the 5' end of the mRNA where it functions
CC       in mRNA export to the cytoplasm via the TAP/NFX1 pathway. May
CC       undergo several rounds of ATP hydrolysis during assembly of TREX
CC       to drive subsequent loading of components such as ALYREF/THOC and
CC       CHTOP onto mRNA. Also associates with pre-mRNA independent of
CC       ALYREF/THOC4 and the THO complex. Involved in the nuclear export
CC       of intronless mRNA; the ATP-bound form is proposed to recruit
CC       export adapter ALYREF/THOC4 to intronless mRNA; its ATPase
CC       activity is cooperatively stimulated by RNA and ALYREF/THOC4 and
CC       ATP hydrolysis is thought to trigger the dissociation from RNA to
CC       allow the association of ALYREF/THOC4 and the NXF1-NXT1
CC       heterodimer. Involved in transcription elongation and genome
CC       stability (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Splice factor that is required for the first ATP-
CC       dependent step in spliceosome assembly and for the interaction of
CC       U2 snRNP with the branchpoint. Has both RNA-stimulated ATP
CC       binding/hydrolysis activity and ATP-dependent RNA unwinding
CC       activity. Even with the stimulation of RNA, the ATPase activity is
CC       weak. Can only hydrolyze ATP but not other NTPs. The RNA
CC       stimulation of ATPase activity does not have a strong preference
CC       for the sequence and length of the RNA. However, ssRNA stimulates
CC       the ATPase activity much more strongly than dsRNA. Can unwind 5'
CC       or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and
CC       helicase activities are not influenced by U2AF2; the effect of
CC       ALYREF/THOC4 is reported conflictingly (By similarity).
CC       {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: Homodimer, and heterodimer with DDX39A. Component of the
CC       transcription/export (TREX) complex at least composed of
CC       ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex;
CC       TREX seems to have dynamic structure involving ATP-dependent
CC       remodeling; in the complex bridges ALYREF/THOC4 and the THO
CC       complex, and, in a ATP-dependent manner, ALYREF/THOC4 and
CC       SARNP/CIP29. Component of the spliceosome. Interacts directly with
CC       U2AF2. Interacts with RBM8A, RNPS1 and SRRM1, FYTTD1/UIF, THOC1,
CC       MX1 and POLDIP3. Interacts with LUZP4 (By similarity).
CC       {ECO:0000250|UniProtKB:Q13838}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle
CC       {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Can translocate to
CC       the cytoplasm in the presence of MX1. {ECO:0000250}.
CC   -!- DOMAIN: The helicase C-terminal domain mediates interaction with
CC       ALYREF/THOC4. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD
CC       subfamily. {ECO:0000305}.
DR   EMBL; Z34846; CAA84355.1; -; Genomic_DNA.
DR   EMBL; AJ251914; CAB63856.1; -; Genomic_DNA.
DR   PIR; I47126; I47126.
DR   RefSeq; NP_001005157.1; NM_001005157.1.
DR   RefSeq; XP_005665850.1; XM_005665793.2.
DR   RefSeq; XP_005665851.1; XM_005665794.2.
DR   SMR; Q29024; -.
DR   STRING; 9823.ENSSSCP00000001487; -.
DR   PaxDb; Q29024; -.
DR   PeptideAtlas; Q29024; -.
DR   PRIDE; Q29024; -.
DR   Ensembl; ENSSSCT00070048206; ENSSSCP00070040698; ENSSSCG00070024145.
DR   GeneID; 448813; -.
DR   KEGG; ssc:448813; -.
DR   CTD; 7919; -.
DR   eggNOG; KOG0329; Eukaryota.
DR   eggNOG; COG0513; LUCA.
DR   GeneTree; ENSGT00940000160110; -.
DR   InParanoid; Q29024; -.
DR   KO; K12812; -.
DR   OrthoDB; 779000at2759; -.
DR   TreeFam; TF300442; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Bgee; ENSSSCG00000001400; Expressed in 6 organ(s), highest expression level in lung.
DR   Genevisible; Q29024; SS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000346; C:transcription export complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:2000002; P:negative regulation of DNA damage checkpoint; ISS:UniProtKB.
DR   GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Helicase;
KW   Hydrolase; Isopeptide bond; mRNA processing; mRNA splicing;
KW   mRNA transport; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; Spliceosome; Transport;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q13838}.
FT   CHAIN         2    428       Spliceosome RNA helicase DDX39B.
FT                                /FTId=PRO_0000055075.
FT   DOMAIN       76    249       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      261    422       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      89     96       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        45     73       Q motif.
FT   MOTIF       196    199       DECD box.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q13838}.
FT   MOD_RES      36     36       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q13838}.
FT   MOD_RES      38     38       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13838}.
FT   MOD_RES      41     41       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q13838}.
FT   MOD_RES     172    172       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q13838}.
FT   CROSSLNK     36     36       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:Q13838}.
FT   CONFLICT     30     30       Missing (in Ref. 1; CAA84355).
FT                                {ECO:0000305}.
FT   CONFLICT    235    235       I -> V (in Ref. 1; CAA84355).
FT                                {ECO:0000305}.
FT   CONFLICT    339    339       R -> G (in Ref. 1; CAA84355).
FT                                {ECO:0000305}.
SQ   SEQUENCE   428 AA;  48991 MW;  7A55167BF576FB6F CRC64;
     MAENDVDNEL LDYEDDEVET AAGGDGAEAP AKKDVKGSYV SIHSSGFRDF LLKPELLRAI
     VDCGFEHPSE VQHECIPQAI LGMDVLCQAK SGMGKTAVFV LATLQQLEPV TGQVSVLVMC
     HTRELAFQIS KEYERFSKYM PNVKVAVFFG GLSIKKDEEV LKKNCPHIVV GTPGRILALA
     RNKSLNLKHI KHFILDECDK MLEQLDMRRD VQEIFRMTPH EKQVMMFSAT LSKEIRPVCR
     KFMQDPMEIF VDDETKLTLH GLQQYYVKLK DNEKNRKLFD LLDVLEFNQV VIFVKSVQRC
     IALAQLLVEQ NFPAIAIHRG MPQEERLSRY QQFKDFQRRI LVATNLFGRG MDIERVNIAF
     NYDMPEDSDT YLHRVARAGR FGTKGLAITF VSDENDAKIL NDVQDRFEVN ISELPDEIDI
     SSYIEQTR
//
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