DDX42_PONAB
ID DDX42_PONAB Reviewed; 942 AA.
AC Q5R7D1;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=ATP-dependent RNA helicase DDX42;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q86XP3};
DE AltName: Full=DEAD box protein 42;
GN Name=DDX42;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent RNA helicase. Binds to partially double-
CC stranded RNAs (dsRNAs) in order to unwind RNA secondary structures.
CC Unwinding is promoted in the presence of single-strand binding
CC proteins. Mediates also RNA duplex formation thereby displacing the
CC single-strand RNA binding protein. ATP and ADP modulate its activity:
CC ATP binding and hydrolysis by DDX42 triggers RNA strand separation,
CC whereas the ADP-bound form of the protein triggers annealing of
CC complementary RNA strands. Involved in the survival of cells by
CC interacting with TP53BP2 and thereby counteracting the apoptosis-
CC stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm.
CC {ECO:0000250|UniProtKB:Q86XP3}.
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:Q86XP3};
CC -!- SUBUNIT: Component of splicing factor SF3B complex which is composed of
CC at least eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6,
CC PHF5A/SF3B14B, and DDX42/SF3B125. Interacts (via the C-terminus) with
CC TP53BP2; the interaction is not inhibitied by TP53BP2 ubiquitination
CC and is independent of p53/TP53. {ECO:0000250|UniProtKB:Q86XP3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86XP3}. Nucleus
CC {ECO:0000250|UniProtKB:Q86XP3}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX42 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR860187; CAH92329.1; -; mRNA.
DR RefSeq; NP_001126368.1; NM_001132896.1.
DR AlphaFoldDB; Q5R7D1; -.
DR SMR; Q5R7D1; -.
DR STRING; 9601.ENSPPYP00000009583; -.
DR GeneID; 100173349; -.
DR KEGG; pon:100173349; -.
DR CTD; 11325; -.
DR eggNOG; KOG0339; Eukaryota.
DR InParanoid; Q5R7D1; -.
DR OrthoDB; 245118at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; PS00039; DEAD_ATP_HELICASE; 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; Coiled coil; Cytoplasm; Helicase; Hydrolase;
KW Isopeptide bond; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Ubl conjugation.
FT CHAIN 1..942
FT /note="ATP-dependent RNA helicase DDX42"
FT /id="PRO_0000280060"
FT DOMAIN 284..459
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 487..632
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..833
FT /note="Necessary for interaction with TP53BP2"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
FT REGION 783..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 116..157
FT /evidence="ECO:0000255"
FT MOTIF 253..281
FT /note="Q motif"
FT MOTIF 407..410
FT /note="DEAD box"
FT COMPBIAS 35..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 297..304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
FT CROSSLNK 899
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86XP3"
SQ SEQUENCE 942 AA; 103498 MW; 47492B68C09042AF CRC64;
MNWNKGGPGT KRGFGFGGFA ISAGKKEEPK LPQQSHSAFG ATSSSSGFGK SAPPQLPSFY
KIGSKRANFD EENAYFEDEE EDSSNVDLPY IPAENSPTRQ QFHSKPIDSD SDDDPLEAFM
AEVEDQAARD MKRLEEKDKE RKNVKGIRDD IEEEDDQETY FRYMAENPTA GVVQEEEEDN
LEYDSDGNPI APTKKIIDPL PPIDHSEIDY PPFEKNFYNE HEEITNLTPQ QLIDLRHKLN
LRVSGAAPPR PGSSFAHFGF DEQLMHQIRK SEYTQPTPIQ CQGVPVALSG RDMIGIAKTG
SGKTAAFIWP MLIHIMDQKE LEPGDGPIAV IVCPTRELCQ QIHAEGKRFG KAYNLRSVAV
YGGGSMWEQA KALQEGAEIV VCTPGRLIDH VKKKATNLQR VSYLVFDEAD RMFDMGFEYQ
VRSIASHVRP DRQTLLFSAT FRKKIEKLAR DILIDPIRVV QGDIGEANED VTQIVEILHS
GPSKWNWLTR RLVEFTSSGS VLLFVTKKAN AEELANNLKQ EGHNLGLLHG DMDQSERNKV
ISDFKKKDIP VLVATDVAAR GLDIPSIKTV INYDVARDID THTHRIGRTG RAGEKGVAYT
LLTPKDSNFA GDLVRNLEGA NQHVSKELLD LAMQNAWFRK SRFKGGKGKK LNIGGGGLGY
RERPGLGSEN MDRGNNNVMS NYEAYKPSTG AMGDRLTAMK AAFQSQYKSH FVAASLSNQK
AGSSAAGASG WTSAGSLNSV PTNSAQQGHN SPDSPITSAT KGIPGFGNIG NISGAPVTYP
SAGAQGVNNT ASGNNSREGT GGSNGKRERY TENRGSSRHS HGETGNRHSD SPRHGDGGRH
GDGYRHPESS SRHTDGHRHG ENRHGGSAGR HGENRGANDG RNGESRKEAC NRESKMEPKM
EPKMEPKVDS NKMDKVDSKT DKTADGFAVP EPPKRKKSRW DS
