DDX3Y_MOUSE
ID DDX3Y_MOUSE Reviewed; 658 AA.
AC Q62095; Q9QWS9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=ATP-dependent RNA helicase DDX3Y;
DE EC=3.6.4.13;
DE AltName: Full=D1Pas1-related sequence 1;
DE AltName: Full=DEAD box protein 3, Y-chromosomal;
DE AltName: Full=DEAD-box RNA helicase DEAD2;
DE Short=mDEAD2;
GN Name=Ddx3y; Synonyms=D1Pas1-rs1, Dead2;
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].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=9736773; DOI=10.1093/hmg/7.11.1713;
RA Mazeyrat S., Saut N., Sargent C.A., Grimmond S., Longepied G.,
RA Ehrmann I.E., Ellis P.S., Greenfield A., Affara N.A., Mitchell M.J.;
RT "The mouse Y chromosome interval necessary for spermatogonial proliferation
RT is gene dense with syntenic homology to the human AZFa region.";
RL Hum. Mol. Genet. 7:1713-1724(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 283-527, AND TISSUE SPECIFICITY.
RC TISSUE=Erythroleukemia;
RX PubMed=8144024; DOI=10.1016/0378-1119(94)90541-x;
RA Gee S.L., Conboy J.G.;
RT "Mouse erythroid cells express multiple putative RNA helicase genes
RT exhibiting high sequence conservation from yeast to mammals.";
RL Gene 140:171-177(1994).
RN [4]
RP PROTEIN SEQUENCE OF 428-439.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15383328; DOI=10.1016/j.yexcr.2004.07.005;
RA Sekiguchi T., Iida H., Fukumura J., Nishimoto T.;
RT "Human DDX3Y, the Y-encoded isoform of RNA helicase DDX3, rescues a hamster
RT temperature-sensitive ET24 mutant cell line with a DDX3X mutation.";
RL Exp. Cell Res. 300:213-222(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Pancreas;
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 [7]
RP FUNCTION.
RX PubMed=30475900; DOI=10.1371/journal.ppat.1007397;
RA Szappanos D., Tschismarov R., Perlot T., Westermayer S., Fischer K.,
RA Platanitis E., Kallinger F., Novatchkova M., Lassnig C., Mueller M.,
RA Sexl V., Bennett K.L., Foong-Sobis M., Penninger J.M., Decker T.;
RT "The RNA helicase DDX3X is an essential mediator of innate antimicrobial
RT immunity.";
RL PLoS Pathog. 14:E1007397-E1007397(2018).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=30613052; DOI=10.1262/jrd.2018-145;
RA Matsumura T., Endo T., Isotani A., Ogawa M., Ikawa M.;
RT "An azoospermic factor gene, Ddx3y and its paralog, Ddx3x are dispensable
RT in germ cells for male fertility.";
RL J. Reprod. Dev. 65:121-128(2019).
CC -!- FUNCTION: Probable ATP-dependent RNA helicase. During immune response,
CC may enhance IFNB1 expression via IRF3/IRF7 pathway (PubMed:30475900).
CC {ECO:0000269|PubMed:30475900}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15383328}. Nucleus
CC {ECO:0000269|PubMed:15383328}. Note=Shuttles between the nucleus and
CC the cytoplasm in an XPO1-dependent manner.
CC -!- TISSUE SPECIFICITY: Found in heart, brain, liver, skeletal muscle,
CC kidney and testis. Low expression detected in lung. In testis,
CC expressed in all types of spermatogenic cells including spermatogonia,
CC spermatocytes, spermatids and somatic Sertoli cells within the
CC seminiferous tubules. Also expressed in Leydig cells and other
CC interstitial cells. {ECO:0000269|PubMed:15383328,
CC ECO:0000269|PubMed:8144024}.
CC -!- DISRUPTION PHENOTYPE: Knockout males show normal spermatogenesis,
CC produce morphologically normal spermatozoa and sire healthy offspring
CC (PubMed:30613052). DDX3X and DDX3Y double knockout is embryonic lethal
CC (PubMed:30613052). DDX3X and DDX3Y double knockout germ cells can
CC differentiate into spermatozoa (PubMed:30613052).
CC {ECO:0000269|PubMed:30613052}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ007376; CAA07483.1; -; mRNA.
DR EMBL; BC021453; AAH21453.1; -; mRNA.
DR EMBL; L25337; AAA53631.1; -; mRNA.
DR CCDS; CCDS30543.1; -.
DR RefSeq; NP_036138.1; NM_012008.2.
DR AlphaFoldDB; Q62095; -.
DR SMR; Q62095; -.
DR BioGRID; 205050; 9.
DR ELM; Q62095; -.
DR IntAct; Q62095; 1.
DR MINT; Q62095; -.
DR STRING; 10090.ENSMUSP00000088729; -.
DR iPTMnet; Q62095; -.
DR PhosphoSitePlus; Q62095; -.
DR SwissPalm; Q62095; -.
DR EPD; Q62095; -.
DR jPOST; Q62095; -.
DR MaxQB; Q62095; -.
DR PaxDb; Q62095; -.
DR PRIDE; Q62095; -.
DR ProteomicsDB; 279902; -.
DR Antibodypedia; 5485; 227 antibodies from 30 providers.
DR DNASU; 26900; -.
DR Ensembl; ENSMUST00000091190; ENSMUSP00000088729; ENSMUSG00000069045.
DR GeneID; 26900; -.
DR KEGG; mmu:26900; -.
DR UCSC; uc009uzm.2; mouse.
DR CTD; 8653; -.
DR MGI; MGI:1349406; Ddx3y.
DR VEuPathDB; HostDB:ENSMUSG00000069045; -.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000154443; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q62095; -.
DR OMA; NHGNSRL; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; Q62095; -.
DR TreeFam; TF300364; -.
DR BioGRID-ORCS; 26900; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ddx3y; mouse.
DR PRO; PR:Q62095; -.
DR Proteomes; UP000000589; Chromosome Y.
DR RNAct; Q62095; protein.
DR Bgee; ENSMUSG00000069045; Expressed in median eminence of neurohypophysis and 225 other tissues.
DR ExpressionAtlas; Q62095; baseline and differential.
DR Genevisible; Q62095; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; 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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
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 Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Helicase;
KW Hydrolase; Isopeptide bond; Methylation; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT CHAIN 2..658
FT /note="ATP-dependent RNA helicase DDX3Y"
FT /id="PRO_0000055012"
FT DOMAIN 210..402
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 413..574
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 179..207
FT /note="Q motif"
FT MOTIF 346..349
FT /note="DEAD box"
FT COMPBIAS 19..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 199..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 223..230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 101
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 104
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 110
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 590
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 615
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 628
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT CONFLICT 527
FT /note="R -> S (in Ref. 3; AAA53631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 658 AA; 73428 MW; C64668326B2C3BB9 CRC64;
MSQVAAESTA GLDQQFVGLD LKSSDNQNGG GNTESKGRYI PPHLRNRETS KGVCDKDSSG
WSCSKDKDAY SSFGSRDSRG KPNYFSDRGS GSRGRFDDHG RNDYDGIGGR DRTGFGKFER
SGHSRWSDRS DEDDWSKPLP PSERLEQELF SGGNTGINFE KYDDIPVEAT GNNCPPHIEN
FSDIEMGEII MGNIELTRYT RPTPVQKHAI PIIKEKRDLM ACAQTGSGKT AAFLLPILSQ
IYTDGPGEAL KAMKENGRYG RRKQYPISLV LAPTRELAVQ IYEEARKFSY RSRVRPCVVY
GGADTVQQIR DLERGCHLLV ATPGRLVDMM ERGKIGLDFC KYLVLDEADR MLDMGFEPQI
RRIVEQDTMP PKGVRHTMMF SATFPKEIQM LARDFLDEYI FLAVGRVGST SENITQKVVW
VEELDKRSFL LDLLNATGKD SLTLVFVETK KGADSLENFL FQERYACTSI HGDRSQKDRE
EALHQFRSGR KPILVATAVA ARGLDISNVK HVINFDLPSD IEEYVHRIGR TGRVGNLGLA
TSFFNERNLN ITKDLLDLLV EAKQEVPSWL ESMAYEHHYK GSSRGRSKSR FSGGFGARDY
RQSSGSANAG FNSNRANSSR SSGSSHNRGF GGGGYGGFYN NDGYGGNYNS QAVDWWGN
