DDX20_MOUSE
ID DDX20_MOUSE Reviewed; 825 AA.
AC Q9JJY4; Q059Z6; Q9JIK4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX20;
DE EC=3.6.1.15 {ECO:0000250|UniProtKB:Q9UHI6};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9UHI6};
DE AltName: Full=Component of gems 3;
DE AltName: Full=DEAD box protein 20;
DE AltName: Full=DEAD box protein DP 103;
DE AltName: Full=Gemin-3;
DE AltName: Full=Regulator of steroidogenic factor 1;
DE Short=ROSF-1;
GN Name=Ddx20; Synonyms=Dp103, Gemin3;
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], AND INTERACTION WITH SMN1.
RX PubMed=10767334; DOI=10.1093/hmg/9.7.1093;
RA Campbell L., Hunter K.M., Mohaghegh P., Tinsley J.M., Brasch M.A.,
RA Davies K.E.;
RT "Direct interaction of Smn with dp103, a putative RNA helicase: a role for
RT Smn in transcription regulation?";
RL Hum. Mol. Genet. 9:1093-1100(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=11145740; DOI=10.1210/mend.15.1.0580;
RA Ou Q., Mouillet J.F., Yan X., Dorn C., Crawford P.A., Sadovsky Y.;
RT "The DEAD box protein DP103 is a regulator of steroidogenic factor-1.";
RL Mol. Endocrinol. 15:69-79(2001).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 INTERACTION WITH FOXL2.
RX PubMed=16153597; DOI=10.1016/j.bbrc.2005.08.184;
RA Lee K., Pisarska M.D., Ko J.J., Kang Y., Yoon S., Ryou S.M., Cha K.Y.,
RA Bae J.;
RT "Transcriptional factor FOXL2 interacts with DP103 and induces apoptosis.";
RL Biochem. Biophys. Res. Commun. 336:876-881(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, 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: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play
CC a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs)
CC (By similarity). {ECO:0000250|UniProtKB:Q9UHI6}.
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:Q9UHI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI6};
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP
CC (By similarity). Part of the SMN-Sm complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
CC STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC SNRPF and SNRPG (By similarity). Interacts with SMN1; the interaction
CC is direct (PubMed:10767334). Interacts with GEMIN4; the interaction is
CC direct (By similarity). Interacts with GEMIN5 (By similarity).
CC Interacts with SNUPN; the interaction is direct (By similarity).
CC Interacts with PPP4R2 (By similarity). Interacts with FOXL2
CC (PubMed:16153597). Interacts with NANOS1 and PUM2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UHI6, ECO:0000269|PubMed:10767334,
CC ECO:0000269|PubMed:16153597}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHI6}.
CC Nucleus, gem {ECO:0000250|UniProtKB:Q9UHI6}. Note=Localized in
CC subnuclear structures next to coiled bodies, called Gemini of Cajal
CC bodies (Gems). {ECO:0000250|UniProtKB:Q9UHI6}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX20 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ250027; CAB86201.1; -; mRNA.
DR EMBL; AF220454; AAF76301.1; -; mRNA.
DR EMBL; CH466608; EDL07549.1; -; Genomic_DNA.
DR EMBL; BC125471; AAI25472.1; -; mRNA.
DR EMBL; BC137721; AAI37722.1; -; mRNA.
DR CCDS; CCDS38581.1; -.
DR RefSeq; NP_059093.3; NM_017397.3.
DR RefSeq; XP_006501764.1; XM_006501701.3.
DR AlphaFoldDB; Q9JJY4; -.
DR SMR; Q9JJY4; -.
DR BioGRID; 207545; 11.
DR IntAct; Q9JJY4; 2.
DR MINT; Q9JJY4; -.
DR STRING; 10090.ENSMUSP00000088176; -.
DR iPTMnet; Q9JJY4; -.
DR PhosphoSitePlus; Q9JJY4; -.
DR EPD; Q9JJY4; -.
DR jPOST; Q9JJY4; -.
DR MaxQB; Q9JJY4; -.
DR PaxDb; Q9JJY4; -.
DR PeptideAtlas; Q9JJY4; -.
DR PRIDE; Q9JJY4; -.
DR ProteomicsDB; 279323; -.
DR Antibodypedia; 1125; 358 antibodies from 36 providers.
DR DNASU; 53975; -.
DR Ensembl; ENSMUST00000090680; ENSMUSP00000088176; ENSMUSG00000027905.
DR GeneID; 53975; -.
DR KEGG; mmu:53975; -.
DR UCSC; uc008qva.1; mouse.
DR CTD; 11218; -.
DR MGI; MGI:1858415; Ddx20.
DR VEuPathDB; HostDB:ENSMUSG00000027905; -.
DR eggNOG; KOG4284; Eukaryota.
DR GeneTree; ENSGT00940000158400; -.
DR HOGENOM; CLU_019966_0_0_1; -.
DR InParanoid; Q9JJY4; -.
DR OMA; ECISGSM; -.
DR OrthoDB; 453219at2759; -.
DR PhylomeDB; Q9JJY4; -.
DR TreeFam; TF101524; -.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR BioGRID-ORCS; 53975; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Ddx20; mouse.
DR PRO; PR:Q9JJY4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JJY4; protein.
DR Bgee; ENSMUSG00000027905; Expressed in otic placode and 253 other tissues.
DR ExpressionAtlas; Q9JJY4; baseline and differential.
DR Genevisible; Q9JJY4; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:BHF-UCL.
DR GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0048477; P:oogenesis; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IMP:MGI.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA-binding; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..825
FT /note="Probable ATP-dependent RNA helicase DDX20"
FT /id="PRO_0000055026"
FT DOMAIN 94..265
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 300..449
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 27..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 63..91
FT /note="Q motif"
FT MOTIF 212..215
FT /note="DEAD box"
FT COMPBIAS 465..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 110..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 552
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 689
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT MOD_RES 706
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI6"
FT CONFLICT 5
FT /note="A -> T (in Ref. 2; AAF76301)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="P -> R (in Ref. 2; AAF76301)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="Q -> H (in Ref. 1; CAB86201)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="V -> I (in Ref. 2; AAF76301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 825 AA; 91710 MW; B5BCD0754D4075C3 CRC64;
MAAAAFEVPA ALTTSESTMA AERAAAPVQA VEPTPASPWT QRTAHDIGGP RTRTGDVVLA
EPADFESLLL SRPVLEGLRA AGFERPSPVQ LKAIPLGRCG LDLIVQAKSG TGKTCVFSTI
ALDSLILENY STQILILAPT REIAVQIHSV ITAIGIKMEG LECHVFIGGT PLSQDKTRLK
KCHIAVGSPG RIKQLIELDY LNPGSIRLFI LDEADKLLEE GSFQEQINWI YSSLPASKQM
LAVSATYPEV LANALTRYMR DPTFVRLNPS DPSLIGLKQY YQVVNSYPLA HKIFEEKTQH
LQELFSKVPF NQALVFSNLH SRAQHLADIL SSKGFPTECI SGNMNQNQRL DAMAKLKQFH
CRVLISTDLT SRGIDAEKVN LVVNLDVPLD WETYMHRIGR AGRFGTLGLT VTYCCRGEEE
NMMMKIAQKC NINLLPLPDP IPPGLMEECL NWDVEVKAAM HTYSSPTVAT QSPKKQVQKL
ERAFQSQRTP GNQTPSPRNT SASALSARPK HSKPKLPVKS HSECGVLEKA APPQESGCPA
QLEEQVKNSV QTSVEDSSSN SQHQAKDSSP GSLPKIPCLS SFKVHQPSTL TFAELVDDYE
HYIKEGLEKP VEIIRHYTGP EAQTGNPQNG FVRNRVSEDR AQMLVSSSQS GDSESDSDSC
SSRTSSQSKG NKSYLEGSSD TQLKDTECTP VGGPLSLEQV QNGNDTPTQV EYQEAPETQV
KARHKEGANQ RSKQSRRNPA RRSSYRVQSE PQEESWYDCH RETTASFSDT YQDYEEYWRA
YYRAWQEYYA AASHSYYWNA QRHPSWMAAY HMNTVYLQEM MRGNQ
