DDX25_MOUSE
ID DDX25_MOUSE Reviewed; 484 AA.
AC Q9QY15; Q53Z03; Q7TMB5; Q8R1B6;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=ATP-dependent RNA helicase DDX25;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 25;
DE AltName: Full=Gonadotropin-regulated testicular RNA helicase;
GN Name=Ddx25; Synonyms=Grth;
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=BALB/cJ; TISSUE=Testis;
RX PubMed=10608860; DOI=10.1074/jbc.274.53.37932;
RA Tang P.-Z., Tsai-Morris C.-H., Dufau M.L.;
RT "A novel gonadotropin-regulated testicular RNA helicase: a new member of
RT the DEAD-box family.";
RL J. Biol. Chem. 274:37932-37940(1999).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS, ALTERNATIVE INITIATION, AND TISSUE
RP SPECIFICITY.
RA Tang P.-Z., Tsai-Morris C.-H., Dufau M.L.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=129/SvJ;
RX PubMed=15096601; DOI=10.1073/pnas.0401855101;
RA Tsai-Morris C.-H., Sheng Y., Lee E., Lei K.-J., Dufau M.L.;
RT "Gonadotropin-regulated testicular RNA helicase (GRTH/Ddx25) is essential
RT for spermatid development and completion of spermatogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6373-6378(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Testis;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=16968703; DOI=10.1074/jbc.m605086200;
RA Sheng Y., Tsai-Morris C.-H., Gutti R., Maeda Y., Dufau M.L.;
RT "Gonadotropin-regulated testicular RNA helicase (GRTH/Ddx25) is a transport
RT protein involved in gene-specific mRNA export and protein translation
RT during spermatogenesis.";
RL J. Biol. Chem. 281:35048-35056(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49, AND IDENTIFICATION BY
RP 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).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=32665638; DOI=10.1038/s41598-020-67834-5;
RA Snyder E., Chukrallah L., Seltzer K., Goodwin L., Braun R.E.;
RT "ADAD1 and ADAD2, testis-specific adenosine deaminase domain-containing
RT proteins, are required for male fertility.";
RL Sci. Rep. 10:11536-11536(2020).
CC -!- FUNCTION: ATP-dependent RNA helicase. Required for mRNA export and
CC translation regulation during spermatid development.
CC {ECO:0000269|PubMed:16968703}.
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:15096601,
CC ECO:0000269|PubMed:16968703}. Nucleus {ECO:0000269|PubMed:15096601,
CC ECO:0000269|PubMed:16968703}. Note=Detected in both cytoplasm and
CC nucleus of testicular cells. Also detected in chromatoid bodies of
CC round spermatids. {ECO:0000269|PubMed:15096601,
CC ECO:0000269|PubMed:16968703, ECO:0000269|PubMed:32665638}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QY15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QY15-2; Sequence=VSP_018876;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in germ cells. Isoform 2 is
CC expressed in Leydig cells and in round spermatids of adult testis upon
CC gonadotropin stimulation. {ECO:0000269|Ref.2}.
CC -!- PTM: Phosphorylated on threonine residues. The phosphorylated form is
CC found in the cytoplasm but not in the nucleus.
CC {ECO:0000269|PubMed:16968703}.
CC -!- DISRUPTION PHENOTYPE: Male mice display normal sexual behavior but are
CC sterile with testes that are 25% smaller than the wild-type. Round
CC spermatids arrest at step 8 and fail to elongate. Chromatoid bodies are
CC unusually condensed, greatly reduced in size and lack the typical
CC amorphous texture throughout all steps of spermiogenesis.
CC {ECO:0000269|PubMed:15096601}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR EMBL; AF142630; AAF21361.2; -; mRNA.
DR EMBL; AY380091; AAR26239.1; -; Genomic_DNA.
DR EMBL; AY380080; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AY380081; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AY380082; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AY380083; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AY380084; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AY380085; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AY380086; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AY380087; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AY380088; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AY380089; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AY380090; AAR26239.1; JOINED; Genomic_DNA.
DR EMBL; AK050693; BAC34384.1; -; mRNA.
DR EMBL; AK078340; BAC37227.1; -; mRNA.
DR EMBL; BC024852; AAH24852.1; -; mRNA.
DR EMBL; BC061130; AAH61130.2; -; mRNA.
DR CCDS; CCDS52753.1; -. [Q9QY15-1]
DR RefSeq; NP_038960.2; NM_013932.4. [Q9QY15-1]
DR AlphaFoldDB; Q9QY15; -.
DR SMR; Q9QY15; -.
DR BioGRID; 206034; 1.
DR IntAct; Q9QY15; 1.
DR MINT; Q9QY15; -.
DR STRING; 10090.ENSMUSP00000034612; -.
DR iPTMnet; Q9QY15; -.
DR PhosphoSitePlus; Q9QY15; -.
DR MaxQB; Q9QY15; -.
DR PaxDb; Q9QY15; -.
DR PeptideAtlas; Q9QY15; -.
DR PRIDE; Q9QY15; -.
DR ProteomicsDB; 279180; -. [Q9QY15-1]
DR ProteomicsDB; 279181; -. [Q9QY15-2]
DR Antibodypedia; 9318; 67 antibodies from 20 providers.
DR DNASU; 30959; -.
DR Ensembl; ENSMUST00000034612; ENSMUSP00000034612; ENSMUSG00000032101. [Q9QY15-1]
DR GeneID; 30959; -.
DR KEGG; mmu:30959; -.
DR UCSC; uc012gqi.1; mouse. [Q9QY15-1]
DR CTD; 29118; -.
DR MGI; MGI:1353582; Ddx25.
DR VEuPathDB; HostDB:ENSMUSG00000032101; -.
DR eggNOG; KOG0332; Eukaryota.
DR GeneTree; ENSGT00940000159712; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q9QY15; -.
DR OMA; DFKNLCM; -.
DR OrthoDB; 608788at2759; -.
DR PhylomeDB; Q9QY15; -.
DR TreeFam; TF314957; -.
DR BRENDA; 3.6.4.13; 3474.
DR BioGRID-ORCS; 30959; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Ddx25; mouse.
DR PRO; PR:Q9QY15; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9QY15; protein.
DR Bgee; ENSMUSG00000032101; Expressed in seminiferous tubule of testis and 149 other tissues.
DR Genevisible; Q9QY15; MM.
DR GO; GO:0033391; C:chromatoid body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IDA:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IDA: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; 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; 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 Alternative initiation; ATP-binding; Cytoplasm; Developmental protein;
KW Differentiation; Helicase; Hydrolase; mRNA transport; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Spermatogenesis;
KW Translation regulation; Transport.
FT CHAIN 1..484
FT /note="ATP-dependent RNA helicase DDX25"
FT /id="PRO_0000030815"
FT DOMAIN 131..301
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 312..479
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 62..75
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 98..126
FT /note="Q motif"
FT MOTIF 101..115
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 248..251
FT /note="DEAD box"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..115
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018876"
FT CONFLICT 463
FT /note="H -> P (in Ref. 5; AAH24852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 54876 MW; D4971BFA338D8BE0 CRC64;
MASLLWGGDA GAAESERLNS HFSNLVHPRK NLRGIRSTTV PNIDGSLNTE DDDDDEDDVV
DLAANSLLNK LIRQSLIESS HRVEVLQKDP SSPLYSVKTF EELRLKEELL KGIYAMGFNR
PSKIQEMALP MMLAHPPQNL IAQSQSGTGK TAAFVLAMLS RVNALELFPQ CLCLAPTYEL
ALQTGRVVER MGKFCVDVEV MYAIRGNRIP RGTEVTKQII IGTPGTVLDW CFKRKLIDLT
KIRVFVLDEA DVMIDTQGFS DQSIRIQRAL PSECQMLLFS ATFEDSVWQF AERIIPDPNV
IKLRKEELTL NNIRQYYVLC ENRKGKYQAL CNIYGGITIG QAIIFCQTRR NAKWLTVEMM
QDGHQVSLLS GELTVEQRAS IIQRFRDGKE KVLITTNVCA RGIDVKQVTI VVNFDLPVNQ
SEEPDYETYL HRIGRTGRFG KKGLAFNMIE VDKLPLLMKI QDHFNSNIKQ LDPEDMDEIE
KIEY
