DHX29_MOUSE
ID DHX29_MOUSE Reviewed; 1365 AA.
AC Q6PGC1; Q8BQJ4; Q8BT01; Q8C9B7; Q8C9H9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ATP-dependent RNA helicase DHX29 {ECO:0000255|HAMAP-Rule:MF_03068};
DE EC=3.6.4.13 {ECO:0000255|HAMAP-Rule:MF_03068};
DE AltName: Full=DEAH box protein 29 {ECO:0000255|HAMAP-Rule:MF_03068};
GN Name=Dhx29 {ECO:0000255|HAMAP-Rule:MF_03068};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-469 AND 745-1365.
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Thymus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and 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: ATP-binding RNA helicase involved in translation initiation.
CC Part of the 43S pre-initiation complex that is required for efficient
CC initiation on mRNAs of higher eukaryotes with structured 5'-UTRs by
CC promoting efficient NTPase-dependent 48S complex formation.
CC Specifically binds to the 40S ribosome near the mRNA entrance. Does not
CC possess a processive helicase activity. {ECO:0000255|HAMAP-
CC Rule:MF_03068}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_03068};
CC -!- SUBUNIT: Part of the 43S pre-initiation complex (PIC) that contains at
CC least Met-tRNA, EIF1, EIF1A (EIF1AX or EIF1AY), EIF2S1, EIF2S2, EIF2S3,
CC EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J,
CC EIF3K, EIF3L, EIF3M, DHX29 and the 40S ribosomal subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03068}.
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DR EMBL; BC057112; AAH57112.1; -; mRNA.
DR EMBL; BC082319; AAH82319.1; -; mRNA.
DR EMBL; AK028342; BAC25894.1; -; mRNA.
DR EMBL; AK042066; BAC31148.2; -; mRNA.
DR EMBL; AK042497; BAC31274.2; -; mRNA.
DR EMBL; AK049530; BAC33796.1; -; mRNA.
DR CCDS; CCDS26779.1; -.
DR RefSeq; NP_766182.2; NM_172594.2.
DR AlphaFoldDB; Q6PGC1; -.
DR SMR; Q6PGC1; -.
DR BioGRID; 230051; 41.
DR IntAct; Q6PGC1; 1.
DR MINT; Q6PGC1; -.
DR STRING; 10090.ENSMUSP00000035244; -.
DR iPTMnet; Q6PGC1; -.
DR PhosphoSitePlus; Q6PGC1; -.
DR EPD; Q6PGC1; -.
DR jPOST; Q6PGC1; -.
DR MaxQB; Q6PGC1; -.
DR PaxDb; Q6PGC1; -.
DR PeptideAtlas; Q6PGC1; -.
DR PRIDE; Q6PGC1; -.
DR ProteomicsDB; 279530; -.
DR Antibodypedia; 11081; 95 antibodies from 21 providers.
DR DNASU; 218629; -.
DR Ensembl; ENSMUST00000038574; ENSMUSP00000035244; ENSMUSG00000042426.
DR GeneID; 218629; -.
DR KEGG; mmu:218629; -.
DR UCSC; uc007rwx.1; mouse.
DR CTD; 54505; -.
DR MGI; MGI:2145374; Dhx29.
DR VEuPathDB; HostDB:ENSMUSG00000042426; -.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000157286; -.
DR HOGENOM; CLU_001832_1_4_1; -.
DR InParanoid; Q6PGC1; -.
DR OMA; HQQNEKK; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; Q6PGC1; -.
DR TreeFam; TF324744; -.
DR BioGRID-ORCS; 218629; 16 hits in 74 CRISPR screens.
DR ChiTaRS; Dhx29; mouse.
DR PRO; PR:Q6PGC1; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6PGC1; protein.
DR Bgee; ENSMUSG00000042426; Expressed in superior cervical ganglion and 235 other tissues.
DR ExpressionAtlas; Q6PGC1; baseline and differential.
DR Genevisible; Q6PGC1; MM.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISO:MGI.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008494; F:translation activator activity; ISO:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001731; P:formation of translation preinitiation complex; ISO:MGI.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0042255; P:ribosome assembly; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_03068; DHX29; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR034730; DHX29.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Helicase; Hydrolase;
KW Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..1365
FT /note="ATP-dependent RNA helicase DHX29"
FT /id="PRO_0000245536"
FT DOMAIN 581..754
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT DOMAIN 848..1025
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 281..308
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT MOTIF 701..704
FT /note="DEAH box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT COMPBIAS 184..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 594..601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03068"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z478"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z478"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1365 AA; 153975 MW; 4143A705CB092280 CRC64;
MGGKNKKHKA PGAAAMRAAV SASRARSAEA GAVGEAQSKK PVARPAPAVP TGAREPRVKQ
GPKIYSFNSA NDSGGSANLD KSILKVVINN KLEQRIIGVI NEHKKQNSDR GAISGRLSAK
KLQDLYMALQ AFSFKTKDIE DAMTNTLLHG GDLHSALDWL CLNLSDDALP EGFSQEFEEQ
QPKSRPKFQS VQIQATLSPP QQTKTKRQEE DPKIKPKKEE TTVEVNMKEW ILRYAEQQDE
EEKGEGSKGL EEEEKFDPNQ RYLNLAARLL DAKEQAAAFK LEKNKQGQKE AQEKIRKFQR
EMETLEDHPI FNPAIKISHQ QNEKKKPAPA TEAESALNLN LFEKSAAATE EEKGKKKEPH
DVRNFDYTAR SWTGKSPKQF LIDWVRKNLP KSPNPSFEKV AVGRYWKCRV RVVRSEDDVL
VVCPTILTED GMQAQHLGAT LALYRLVKGQ SVHQLLPPTY RDVWLEWSDE EKKREELNKM
ETNKPRDLFI AKLLNKLKQQ QQQQQQQRPE SEKGGSEDPE ESWENLVSDE DLAALSLEPT
SAEDLAPVRS LFRRLQSTPK YQRLLKERQQ LPVFKHRDSI VETLKRHRVV VVAGETGSGK
STQVPHFLLE DLLLDECGAR KCNIVCTQPR RISAVSLATR VCEELGCESG PGGRNSLCGY
QIRMESRASE STRLLYCTTG VLLRKLQEDG LLADVSHVIV DEVHERSVQS DFLLVILKEI
LQKRSDLHLI LMSATVDSDK FSTYFTHCPI LRISGRSYPV EVFHLEDIVE ETGFVLEKDS
EYCQKFLEEE EEITINVTSK AGGVKKYQEY IPVQSGASPE LNPFYQKYSS RTQHAILYMN
PHKINLDLIL ELLVYLDKSP QFRNIEGAVL IFLPGLAHIQ QLYDLLSSDR RFYSERYQVI
ALHSVLSTQD QAAAFMFPPP GVRKIVLATN IAETGITIPD VVFVIDTGRT KENKYHESSQ
MSSLVETFVS KASALQRQGR AGRVRDGFCF RLYTRERFEG FLDYSVPEIL RVPLEELCLH
IMKCDLGSPE DFLSKALDPP QLQVISNAMN LLRKIGACEP NEPKLTPLGQ HLAALPVNVK
IGKMLIFGAI FGCLEPVATL AAVMTEKSPF ITPIGRKDEA DLAKSSLAVA DSDHLTIYNA
YLGWKKAQQE GGFRSEISYC QRNFLNRTSL LTLEDVKQEL MKLVKAAGFS SSPSWEGRKG
PQTLSFQDIA LLKAVLAAGL YDSVGKIMCT KSVDVTEKLA CMVETAQGKA QVHPSSVNRD
LQTYGWLLYQ EKVRYTRVYL RETTLITPFP VLLFGGDIEV QHRERLLSVD GWIYFQAPVK
IAVIFKQLRV LIDSVLRKKL ENPKMSLEND KILQIITELI KTENN
