ID DDX25_HUMAN Reviewed; 483 AA.
AC Q9UHL0; B2R6Z0; Q5XVN2; Q86W81; Q8IYP1;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 24-JAN-2024, entry version 188.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC 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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Medulla oblongata;
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 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 307-479.
RX PubMed=20941364; DOI=10.1371/journal.pone.0012791;
RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M.,
RA Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M.,
RA Thorsell A.G., Schuler H.;
RT "Comparative structural analysis of human DEAD-box RNA helicases.";
RL PLoS ONE 5:E12791-E12791(2010).
CC -!- FUNCTION: ATP-dependent RNA helicase. Required for mRNA export and
CC translation regulation during spermatid development (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:10608860}.
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 -!- INTERACTION:
CC Q9UHL0; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-8787165, EBI-10271199;
CC Q9UHL0; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-8787165, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10608860}. Nucleus
CC {ECO:0000250|UniProtKB:Q9QY15}. 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=2;
CC Name=1;
CC IsoId=Q9UHL0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHL0-2; Sequence=VSP_018875;
CC -!- TISSUE SPECIFICITY: Highly expressed in the Leydig and germ cells of
CC the testis and weakly expressed in the pituitary and hypothalamus.
CC {ECO:0000269|PubMed:10608860, ECO:0000269|Ref.2}.
CC -!- INDUCTION: Up-regulated at transcriptional level by chorionic
CC gonadotropin via cyclic AMP-induced androgen formation in the Leydig
CC cell. {ECO:0000269|PubMed:10608860}.
CC -!- PTM: Phosphorylated on threonine residues. The phosphorylated form is
CC found in the cytoplasm but not in the nucleus (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/46826/DDX25";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF155140; AAF21371.2; -; mRNA.
DR EMBL; AY735312; AAU84667.1; -; Genomic_DNA.
DR EMBL; AY735301; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AY735302; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AY735303; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AY735304; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AY735305; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AY735306; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AY735307; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AY735308; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AY735309; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AY735310; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AY735311; AAU84667.1; JOINED; Genomic_DNA.
DR EMBL; AK312772; BAG35637.1; -; mRNA.
DR EMBL; CH471065; EAW67669.1; -; Genomic_DNA.
DR EMBL; BC035388; AAH35388.2; -; mRNA.
DR EMBL; BC050360; AAH50360.2; -; mRNA.
DR CCDS; CCDS44766.1; -. [Q9UHL0-1]
DR CCDS; CCDS81646.1; -. [Q9UHL0-2]
DR RefSeq; NP_001317367.1; NM_001330438.1. [Q9UHL0-2]
DR RefSeq; NP_037396.3; NM_013264.4. [Q9UHL0-1]
DR PDB; 2RB4; X-ray; 2.80 A; A/B=307-479.
DR PDBsum; 2RB4; -.
DR AlphaFoldDB; Q9UHL0; -.
DR SMR; Q9UHL0; -.
DR BioGRID; 118884; 6.
DR IntAct; Q9UHL0; 4.
DR STRING; 9606.ENSP00000263576; -.
DR iPTMnet; Q9UHL0; -.
DR PhosphoSitePlus; Q9UHL0; -.
DR BioMuta; DDX25; -.
DR DMDM; 61222937; -.
DR EPD; Q9UHL0; -.
DR jPOST; Q9UHL0; -.
DR MassIVE; Q9UHL0; -.
DR MaxQB; Q9UHL0; -.
DR PaxDb; 9606-ENSP00000263576; -.
DR PeptideAtlas; Q9UHL0; -.
DR ProteomicsDB; 84372; -. [Q9UHL0-1]
DR ProteomicsDB; 84373; -. [Q9UHL0-2]
DR Antibodypedia; 9318; 87 antibodies from 21 providers.
DR DNASU; 29118; -.
DR Ensembl; ENST00000263576.11; ENSP00000263576.6; ENSG00000109832.14. [Q9UHL0-1]
DR Ensembl; ENST00000525943.1; ENSP00000490224.1; ENSG00000109832.14. [Q9UHL0-2]
DR GeneID; 29118; -.
DR KEGG; hsa:29118; -.
DR MANE-Select; ENST00000263576.11; ENSP00000263576.6; NM_013264.5; NP_037396.3.
DR UCSC; uc001qcz.6; human. [Q9UHL0-1]
DR AGR; HGNC:18698; -.
DR CTD; 29118; -.
DR DisGeNET; 29118; -.
DR GeneCards; DDX25; -.
DR HGNC; HGNC:18698; DDX25.
DR HPA; ENSG00000109832; Tissue enriched (testis).
DR MalaCards; DDX25; -.
DR MIM; 607663; gene.
DR neXtProt; NX_Q9UHL0; -.
DR OpenTargets; ENSG00000109832; -.
DR PharmGKB; PA38644; -.
DR VEuPathDB; HostDB:ENSG00000109832; -.
DR eggNOG; KOG0332; Eukaryota.
DR GeneTree; ENSGT00940000159712; -.
DR InParanoid; Q9UHL0; -.
DR OMA; DFKNLCM; -.
DR OrthoDB; 1087080at2759; -.
DR PhylomeDB; Q9UHL0; -.
DR TreeFam; TF314957; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; Q9UHL0; -.
DR SignaLink; Q9UHL0; -.
DR BioGRID-ORCS; 29118; 7 hits in 1149 CRISPR screens.
DR ChiTaRS; DDX25; human.
DR EvolutionaryTrace; Q9UHL0; -.
DR GenomeRNAi; 29118; -.
DR Pharos; Q9UHL0; Tbio.
DR PRO; PR:Q9UHL0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UHL0; Protein.
DR Bgee; ENSG00000109832; Expressed in left testis and 129 other cell types or tissues.
DR ExpressionAtlas; Q9UHL0; baseline and differential.
DR Genevisible; Q9UHL0; HS.
DR GO; GO:0033391; C:chromatoid body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
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; ISS:UniProtKB.
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 CDD; cd18048; DEADc_DDX25; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 6.10.250.2170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF33; ATP-DEPENDENT RNA HELICASE DDX25; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 3D-structure; Alternative initiation; ATP-binding; Cytoplasm;
KW Developmental protein; Differentiation; Helicase; Hydrolase;
KW mRNA transport; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Spermatogenesis; Translation regulation;
KW Transport.
FT CHAIN 1..483
FT /note="ATP-dependent RNA helicase DDX25"
FT /id="PRO_0000030813"
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 /evidence="ECO:0000250"
FT MOTIF 97..125
FT /note="Q motif"
FT MOTIF 100..114
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
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 VAR_SEQ 1..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_018875"
FT CONFLICT 21
FT /note="H -> N (in Ref. 1; AAF21371/AAU84667)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="I -> T (in Ref. 1; AAF21371/AAU84667)"
FT /evidence="ECO:0000305"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:2RB4"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:2RB4"
FT STRAND 339..344
FT /evidence="ECO:0007829|PDB:2RB4"
FT HELIX 348..359
FT /evidence="ECO:0007829|PDB:2RB4"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2RB4"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:2RB4"
FT HELIX 374..385
FT /evidence="ECO:0007829|PDB:2RB4"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:2RB4"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:2RB4"
FT STRAND 407..414
FT /evidence="ECO:0007829|PDB:2RB4"
FT HELIX 425..432
FT /evidence="ECO:0007829|PDB:2RB4"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:2RB4"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:2RB4"
FT HELIX 453..463
FT /evidence="ECO:0007829|PDB:2RB4"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:2RB4"
SQ SEQUENCE 483 AA; 54692 MW; 32247CDDCA177F48 CRC64;
MASLLWGGDA GAAESERLNS HFSNLSQPRK NLWGIKSTAV RNIDGSINNI NEDDEEDVVD
LAANSLLNKL IHQSLVESSH RVEVLQKDPS SPLYSVKTFE ELRLKEELLK GIYAMGFNRP
SKIQEMALPM MLAHPPQNLI AQSQSGTGKT AAFVLAMLSR VNALELFPQC LCLAPTYELA
LQTGRVVEQM GKFCVDVQVM YAIRGNRIPR GTDITKQIII GTPGTVLDWC FKLKLIDLTK
IRVFVLDEAD VMIDTQGFSD HSIRIQRALP SECQMLLFSA TFEDSVWHFA ERIIPDPNVI
KLRKEELTLN NIRQYYVLCE HRKDKYQALC NIYGSITIGQ AIIFCQTRRN AKWLTVEMIQ
DGHQVSLLSG ELTVEQRASI IQRFRDGKEK VLITTNVCAR GIDVKQVTIV VNFDLPVKQG
EEPDYETYLH RIGRTGRFGK KGLAFNMIEV DELPSLMKIQ DHFNSSIKQL NAEDMDEIEK
IDY
//
