DDX3L_MOUSE
ID DDX3L_MOUSE Reviewed; 660 AA.
AC P16381;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Putative ATP-dependent RNA helicase Pl10;
DE EC=3.6.4.13;
GN Name=D1Pas1; Synonyms=Pl10;
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 TISSUE=Testis;
RX PubMed=2720782; DOI=10.1016/0092-8674(89)90125-6;
RA Leroy P., Alzari P., Sassoon D., Wolgemuth D., Fellous M.;
RT "The protein encoded by a murine male germ cell-specific transcript is a
RT putative ATP-dependent RNA helicase.";
RL Cell 57:549-559(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Putative ATP-dependent RNA helicase. Possible role in a key
CC step of the spermatogenic process.
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 -!- TISSUE SPECIFICITY: Testis.
CC -!- DEVELOPMENTAL STAGE: High levels of PL10 during the meiotic and haploid
CC stages of spermatogenesis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; J04847; AAA39942.1; -; mRNA.
DR EMBL; AK029542; BAC26505.1; -; mRNA.
DR CCDS; CCDS15603.1; -.
DR PIR; A32378; A32378.
DR RefSeq; NP_149068.1; NM_033077.3.
DR AlphaFoldDB; P16381; -.
DR SMR; P16381; -.
DR BioGRID; 226052; 10.
DR IntAct; P16381; 3.
DR STRING; 10090.ENSMUSP00000035261; -.
DR iPTMnet; P16381; -.
DR PhosphoSitePlus; P16381; -.
DR SwissPalm; P16381; -.
DR jPOST; P16381; -.
DR MaxQB; P16381; -.
DR PaxDb; P16381; -.
DR PRIDE; P16381; -.
DR ProteomicsDB; 279326; -.
DR DNASU; 110957; -.
DR Ensembl; ENSMUST00000045108; ENSMUSP00000035261; ENSMUSG00000039224.
DR GeneID; 110957; -.
DR KEGG; mmu:110957; -.
DR UCSC; uc007dzs.1; mouse.
DR CTD; 110957; -.
DR MGI; MGI:91842; D1Pas1.
DR VEuPathDB; HostDB:ENSMUSG00000039224; -.
DR eggNOG; KOG0335; Eukaryota.
DR GeneTree; ENSGT00940000154443; -.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; P16381; -.
DR OMA; CYRSWVR; -.
DR OrthoDB; 595675at2759; -.
DR PhylomeDB; P16381; -.
DR TreeFam; TF300364; -.
DR BioGRID-ORCS; 110957; 6 hits in 75 CRISPR screens.
DR PRO; PR:P16381; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P16381; protein.
DR Bgee; ENSMUSG00000039224; Expressed in seminiferous tubule of testis and 17 other tissues.
DR ExpressionAtlas; P16381; baseline and differential.
DR Genevisible; P16381; MM.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0043186; C:P granule; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0043273; F:CTPase activity; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0003678; F:DNA helicase activity; ISO:MGI.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; ISO:MGI.
DR GO; GO:0043015; F:gamma-tubulin binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISO:MGI.
DR GO; GO:0008143; F:poly(A) binding; ISO:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003724; F:RNA helicase activity; ISO:MGI.
DR GO; GO:0035613; F:RNA stem-loop binding; ISO:MGI.
DR GO; GO:0033592; F:RNA strand annealing activity; ISO:MGI.
DR GO; GO:0031369; F:translation initiation factor binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; ISO:MGI.
DR GO; GO:0071470; P:cellular response to osmotic stress; ISO:MGI.
DR GO; GO:0098586; P:cellular response to virus; ISO:MGI.
DR GO; GO:0007059; P:chromosome segregation; ISO:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0007276; P:gamete generation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0055088; P:lipid homeostasis; ISO:MGI.
DR GO; GO:0042256; P:mature ribosome assembly; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISO:MGI.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:1901985; P:positive regulation of protein acetylation; ISO:MGI.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0034157; P:positive regulation of toll-like receptor 7 signaling pathway; ISO:MGI.
DR GO; GO:0034161; P:positive regulation of toll-like receptor 8 signaling pathway; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
DR GO; GO:0036493; P:positive regulation of translation in response to endoplasmic reticulum stress; ISO:MGI.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISO:MGI.
DR GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0009615; P:response to virus; ISO:MGI.
DR GO; GO:0010501; P:RNA secondary structure unwinding; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0034063; P:stress granule assembly; ISO:MGI.
DR GO; GO:0006413; P:translational initiation; ISO:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:MGI.
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; Developmental protein; Differentiation;
KW DNA-binding; Helicase; Hydrolase; Isopeptide bond; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Spermatogenesis; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT CHAIN 2..660
FT /note="Putative ATP-dependent RNA helicase Pl10"
FT /id="PRO_0000055008"
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..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..632
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..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..626
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 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 100
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 103
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62167"
FT MOD_RES 109
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 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00571"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62095"
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 610
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 630
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"
SQ SEQUENCE 660 AA; 73141 MW; 50AD4E6A131AE603 CRC64;
MSHVAEEDEL GLDQQLAGLD LTSRDSQSGG STASKGRYIP PHLRNREAAK AFYDKDGSRW
SKDKDAYSSF GSRSDTRAKS SFFSDRGGSG SRGRFDERGR SDYESVGSRG GRSGFGKFER
GGNSRWCDKA DEDDWSKPLP PSERLEQELF SGGNTGINFE KYDDIPVEAT GNNCPPHIES
FSDVEMGEII MGNIELTRYT RPTPVQKHAI PIIKEKRDLM ACAQTGSGKT AAFLLPILSQ
IYTDGPGEAL RAMKENGKYG RRKQYPISLV LAPTRELAVQ IYEEARKFSY RSRVRPCVVY
GGADIGQQIR DLERGCHLLV ATPGRLVDMM ERGKIGLDFC KYLVLDEADR MLDMGFEPQI
RRIVEQDTMP PKGVRHTMMF SATFPKEIQM LARDFLDEYI FLAVGRVGST SENITQKVVW
VEEADKRSFL LDLLNATGKD SLILVFVETK KGADSLEDFL YHEGYACTSI HGDRSQRDRE
EALHQFRSGK SPILVATAVA ARGLDISNVK HVINFDLPSD IEEYVHRIGR TGRVGNLGLA
TSFFNERNIN ITKDLLDLLV EAKQEVPSWL ENMAFEHHYK GGSRGRSKSR FSGGFGARDY
RQSSGASSSS FSSGRASNSR SGGGSHGSSR GFGGGSYGGF YNSDGYGGNY SSQGVDWWGN
