DDX25_RAT
ID DDX25_RAT Reviewed; 483 AA.
AC Q9QY16;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 140.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; 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 NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO N-TERMINUS, ALTERNATIVE
RP INITIATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12734186; DOI=10.1074/jbc.m302411200;
RA Sheng Y., Tsai-Morris C.-H., Dufau M.L.;
RT "Cell-specific and hormone-regulated expression of gonadotropin-regulated
RT testicular RNA helicase gene (GRTH/Ddx25) resulting from alternative
RT utilization of translation initiation codons in the rat testis.";
RL J. Biol. Chem. 278:27796-27803(2003).
RN [3]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, NUCLEAR EXPORT SIGNAL, NUCLEAR
RP LOCALIZATION SIGNAL, AND MUTAGENESIS OF LEU-66; LEU-67; LEU-70; ARG-103;
RP LEU-104; LYS-105; LEU-108 AND LEU-109.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: ATP-dependent RNA helicase. Required for mRNA export and
CC translation regulation during spermatid development (By similarity).
CC {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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16968703}. Nucleus
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 (By similarity). {ECO:0000250|UniProtKB:Q9QY15}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=1;
CC IsoId=Q9QY16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QY16-2; Sequence=VSP_018877;
CC Name=3;
CC IsoId=Q9QY16-3; Sequence=VSP_018878;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in germ cells. Isoform 2 is
CC highly expressed in Leydig cells and weakly expressed in the pituitary
CC and hypothalamus. Isoform 3 is weakly expressed only in germ cells.
CC {ECO:0000269|PubMed:12734186}.
CC -!- DEVELOPMENTAL STAGE: Expressed in pubertal and adult animals but not in
CC immature animals. {ECO:0000269|PubMed:12734186}.
CC -!- INDUCTION: By gonadotropin in Leydig cells. Inhibited by flutamine.
CC {ECO:0000269|PubMed:12734186}.
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 -!- MISCELLANEOUS: [Isoform 3]: May start at Met-200 rather than Met-190.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR EMBL; AF142629; AAF21360.2; -; mRNA.
DR RefSeq; NP_113818.2; NM_031630.2. [Q9QY16-1]
DR AlphaFoldDB; Q9QY16; -.
DR SMR; Q9QY16; -.
DR STRING; 10116.ENSRNOP00000017307; -.
DR iPTMnet; Q9QY16; -.
DR PhosphoSitePlus; Q9QY16; -.
DR PaxDb; Q9QY16; -.
DR PRIDE; Q9QY16; -.
DR GeneID; 58856; -.
DR KEGG; rno:58856; -.
DR UCSC; RGD:68381; rat. [Q9QY16-1]
DR CTD; 29118; -.
DR RGD; 68381; Ddx25.
DR eggNOG; KOG0332; Eukaryota.
DR InParanoid; Q9QY16; -.
DR OrthoDB; 608788at2759; -.
DR PhylomeDB; Q9QY16; -.
DR BRENDA; 3.6.4.12; 5301.
DR BRENDA; 3.6.4.13; 5301.
DR PRO; PR:Q9QY16; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0033391; C:chromatoid body; ISS: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; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; IDA:RGD.
DR GO; GO:0003724; F:RNA helicase activity; IDA:RGD.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; 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; 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..483
FT /note="ATP-dependent RNA helicase DDX25"
FT /id="PRO_0000030817"
FT DOMAIN 130..300
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 311..478
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 61..74
FT /note="Nuclear export signal"
FT MOTIF 97..125
FT /note="Q motif"
FT MOTIF 100..114
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:16968703"
FT MOTIF 247..250
FT /note="DEAD box"
FT BINDING 143..150
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:0000250|UniProtKB:Q9QY15"
FT VAR_SEQ 1..189
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018878"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018877"
FT MUTAGEN 66
FT /note="L->A: Enhances nuclear expression; when associated
FT with A-67 and A-70."
FT /evidence="ECO:0000269|PubMed:16968703"
FT MUTAGEN 67
FT /note="L->A: Enhances nuclear expression; when associated
FT with A-66 and A-70."
FT /evidence="ECO:0000269|PubMed:16968703"
FT MUTAGEN 70
FT /note="L->A: Enhances nuclear expression; when associated
FT with A-66 and A-67."
FT /evidence="ECO:0000269|PubMed:16968703"
FT MUTAGEN 103
FT /note="R->A: Abolishes nuclear expression."
FT /evidence="ECO:0000269|PubMed:16968703"
FT MUTAGEN 104
FT /note="L->A: Decreases nuclear expression; when associated
FT with A-108 and A-109."
FT /evidence="ECO:0000269|PubMed:16968703"
FT MUTAGEN 105
FT /note="K->A: Abolishes nuclear expression."
FT /evidence="ECO:0000269|PubMed:16968703"
FT MUTAGEN 108
FT /note="L->A: Decreases nuclear expression; when associated
FT with A-104 and A-109."
FT /evidence="ECO:0000269|PubMed:16968703"
FT MUTAGEN 109
FT /note="L->A: Decreases nuclear expression; when associated
FT with A-104 and A-108."
FT /evidence="ECO:0000269|PubMed:16968703"
SQ SEQUENCE 483 AA; 54791 MW; 17F596DAD9E529FC CRC64;
MASLLWGGDA GAAESERLNS HFSNLVHPRK NLRGIRSTTV PNIDGSLNTE EDDDEDDVVD
LAANSLLNKL IRQSLVESSH RVEVLQKDPS SPLYSVKTFE ELRLKEELLK GIYAMGFNRP
SKIQEMALPM MLAHPPQNLI AQSQSGTGKT AAFVLAMLNR VNALELFPQC LCLAPTYELA
LQTGRVVERM GKFCVDVEVM YAIRGNRIPR GTDVTKQIVI GTPGTVLDWC FKRKLIDLTK
IRVFVLDEAD VMIDTQGFSD QSIRIQRALP SECQMLLFSA TFEDSVWQFA ERIIPDPNVI
KLRKEELTLN NIRQYYVLCE NRKDKYQALC NIYGGITIGQ AIIFCQTRRN AKWLTVEMMQ
DGHQVSLLSG ELTVEQRASI IQRFRDGKEK VLITTNVCAR GIDVKQVTIV VNFDLPVNQS
EEPDYETYLH RIGRTGRFGK KGLAFNMIEV DKLPLLMKIQ DHFNSSIKQL DPEDMDEIEK
IEY
