DDX10_MOUSE
ID DDX10_MOUSE Reviewed; 875 AA.
AC Q80Y44;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX10;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 10;
GN Name=Ddx10;
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].
RC TISSUE=Eye;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-587, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-587, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-587 AND SER-783, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-556, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Putative ATP-dependent RNA helicase. {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 -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC049261; AAH49261.1; ALT_INIT; mRNA.
DR CCDS; CCDS52796.1; -.
DR RefSeq; NP_084212.2; NM_029936.2.
DR AlphaFoldDB; Q80Y44; -.
DR SMR; Q80Y44; -.
DR BioGRID; 218780; 7.
DR IntAct; Q80Y44; 1.
DR MINT; Q80Y44; -.
DR STRING; 10090.ENSMUSP00000065198; -.
DR iPTMnet; Q80Y44; -.
DR PhosphoSitePlus; Q80Y44; -.
DR EPD; Q80Y44; -.
DR MaxQB; Q80Y44; -.
DR PaxDb; Q80Y44; -.
DR PeptideAtlas; Q80Y44; -.
DR PRIDE; Q80Y44; -.
DR ProteomicsDB; 279322; -.
DR Antibodypedia; 1401; 50 antibodies from 17 providers.
DR Ensembl; ENSMUST00000065630; ENSMUSP00000065198; ENSMUSG00000053289.
DR GeneID; 77591; -.
DR KEGG; mmu:77591; -.
DR UCSC; uc009plz.2; mouse.
DR CTD; 1662; -.
DR MGI; MGI:1924841; Ddx10.
DR VEuPathDB; HostDB:ENSMUSG00000053289; -.
DR eggNOG; KOG0343; Eukaryota.
DR GeneTree; ENSGT00550000074980; -.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; Q80Y44; -.
DR OMA; FLWRQKQ; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q80Y44; -.
DR TreeFam; TF315215; -.
DR BioGRID-ORCS; 77591; 26 hits in 77 CRISPR screens.
DR ChiTaRS; Ddx10; mouse.
DR PRO; PR:Q80Y44; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80Y44; protein.
DR Bgee; ENSMUSG00000053289; Expressed in embryonic post-anal tail and 232 other tissues.
DR Genevisible; Q80Y44; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0097065; P:anterior head development; IMP:MGI.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
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; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 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 Acetylation; ATP-binding; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..875
FT /note="Probable ATP-dependent RNA helicase DDX10"
FT /id="PRO_0000055084"
FT DOMAIN 100..274
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 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..97
FT /note="Q motif"
FT MOTIF 222..225
FT /note="DEAD box"
FT COMPBIAS 20..39
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13206"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13206"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13206"
FT MOD_RES 556
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 587
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 652
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13206"
SQ SEQUENCE 875 AA; 100739 MW; 07D6574185AC3646 CRC64;
MGKTVASLGQ GTRPDPVRSF NRWKKKHSHR QHQKKERRKQ LKKPEWQVER EGISRLMQNY
EKINVNEITR FSDFPLSKKT LKGLQEAQYR LVTEIQKQTI GLALQGKDVL GAAKTGSGKT
LAFLVPVLEA LYRLQWTSTD GLGVLIISPT RELAYQTFEV LRKVGKNHDF SAGLIIGGKD
LKHEAERINN INILVCTPGR LLQHMDETIC FHATNLQMLV LDEADRILDM GFADTMNAII
ENLPKKRQTL LFSATQTKSV KDLARLSLKD PEYVWVHEKA KYSTPATLEQ NYIICELHQK
ISVLFSFLRS HLKKKSIVFF SSCKEVQYLY RVFCRLRPGI SILALHGRQQ QMRRMEVYNE
FVRKRAAVLF ATDIAARGLD FPAVNWVLQF DCPEDANTYI HRAGRTARYK EDGEALLILL
PSEEQGMVQQ LLQKKVPVKE IKINPEKLID VQKKLESFLA QDQDLKERAQ RCFVSYIRSV
YLMKDKEVFN VSKLPITEYA LSLGLAVAPR IRFLQKLEKQ PSTELVKNPV TEAVPPRAPS
LPNDEADESP AYVSEKMSVL HKSGERLEET EHRLASGDGD EEQDEETEDE ETEDHLGKAR
EPHTESVVSI EEAQKVKEVS VQFLNRDDDD EDGPDADFLT VKRRDVFGLD LKENEALSKK
EPSKSSVKKK LTKVAEAKKV MKRSFKVNKK ITFTDEGELV QQWPQIQKCA IKDVEEEDDT
GGINLDKAKE RLQEEDKFDK EEYRKKIKAK HRERRLKERE ARREANKRQA KARDEEEAFL
DWSDEDDGGF DPSTLPDPDK HRSSEESESE DTNHKMSDTK KKQETRKRNN TEDDDVRPRS
RHGKKAKWET VEPLDTGLSL AEDEELVLHL LKSQN
