ID D3ZHW0_RAT Unreviewed; 1366 AA.
AC D3ZHW0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 2.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=ATP-dependent RNA helicase DHX29 {ECO:0000256|HAMAP-Rule:MF_03068};
DE EC=3.6.4.13 {ECO:0000256|HAMAP-Rule:MF_03068};
DE AltName: Full=DEAH box protein 29 {ECO:0000256|HAMAP-Rule:MF_03068};
GN Name=Dhx29 {ECO:0000313|Ensembl:ENSRNOP00000013854.6,
GN ECO:0000313|RGD:2318361};
GN Synonyms=DHX29 {ECO:0000256|HAMAP-Rule:MF_03068}, LOC100362324
GN {ECO:0000313|RGD:2318361};
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 {ECO:0000313|Ensembl:ENSRNOP00000013854.6, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000013854.6, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000013854.6,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000013854.6}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000013854.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|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:0000256|ARBA:ARBA00001556, ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-Rule:MF_03068}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03068}.
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DR RefSeq; XP_002725935.1; XM_002725889.5.
DR RefSeq; XP_002729053.2; XM_002729007.5.
DR AlphaFoldDB; D3ZHW0; -.
DR SMR; D3ZHW0; -.
DR STRING; 10116.ENSRNOP00000013854; -.
DR PhosphoSitePlus; D3ZHW0; -.
DR jPOST; D3ZHW0; -.
DR PaxDb; 10116-ENSRNOP00000013854; -.
DR PeptideAtlas; D3ZHW0; -.
DR Ensembl; ENSRNOT00000013854.9; ENSRNOP00000013854.6; ENSRNOG00000010369.9.
DR GeneID; 100362324; -.
DR KEGG; rno:100362324; -.
DR AGR; RGD:2318361; -.
DR CTD; 54505; -.
DR RGD; 2318361; Dhx29.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000157286; -.
DR HOGENOM; CLU_001832_1_4_1; -.
DR InParanoid; D3ZHW0; -.
DR OMA; SWFANMS; -.
DR OrthoDB; 1095660at2759; -.
DR TreeFam; TF324744; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000010369; Expressed in Ammon's horn and 20 other cell types or tissues.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:RGD.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; ISO:RGD.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISO:RGD.
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:RGD.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001731; P:formation of translation preinitiation complex; ISO:RGD.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0042255; P:ribosome assembly; ISO:RGD.
DR CDD; cd17975; DEXHc_DHX29; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF145; ATP-DEPENDENT RNA HELICASE DHX29; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 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; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03068}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_03068};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03068};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_03068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03068};
KW Initiation factor {ECO:0000256|HAMAP-Rule:MF_03068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03068}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03068};
KW Proteomics identification {ECO:0007829|PeptideAtlas:D3ZHW0};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT DOMAIN 582..755
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 849..1026
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..65
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 237..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 281..308
FT /evidence="ECO:0000256|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"
SQ SEQUENCE 1366 AA; 154119 MW; F8B513F3164A5476 CRC64;
MGGKNKKHKA PGAAAMRAAV SASRARSAEA GAVGEAQSKK PVARPAPAVP TSAREPRVKQ
GPKIYSFNSA NDSGGSANLD KSILKVVINN KLEQRIIGVI NEHKKQNNDR GVISGRLSAK
KLQDLYMALQ AFSFKTKDIE DAMTNTLLHG GDLHSALDWL CLNLSDDALP EGFSQEFEEQ
QPKSRPKFQS VQIQATLSPP LQTKTKRQEE DPKIKPKKEE KSMEVNMKEW ILRYAEQQNE
EEKSEGSKGS EDEDKFDPNQ RYLNLAARLL DAKEQAAAFK VEKNKQGQKE AQEKIRKFQR
EMETLEDHPI FNPAIKISHQ QNERKKAPLA TDGESALNFN LFEKPAAATE EEKGKKKEPH
DVRNFDYTAR SWTGKSPKQF LIDWVRKNLP KSPNPSFEKV PVGRYWKCRV RVVKSEDDVL
VVCPTILTED GMQAQHLGAT LALYRLVKGQ SVHQLLPPTY RDVWVEWSDE EKKKEELNKM
ETNKPRDLFI AKLLSKLKQQ QQLQQQRQHP ENKTETAEDP EESWENLVSD EDLSALSLEP
TGAEDLEPVR NLFRRLQSTP KYQRLLKERQ QLPVFKHRAS IVETLKRHRV VVVAGETGSG
KSTQVPHFLL EDLLLNDCGA RKCNIVCTQP RRISAVSLAT RVCEELGCEG GPGGRNSLCG
YQIRMESRAS ESTRLLYCTT GVLLRKLQED GLLADVSHVI VDEVHERSVQ SDFLLVILKE
ILQKRSDLHL ILMSATVDSD KFSTYFTHCP ILRISGRSYP VEVFHLEDIV EETGFILEKD
SEYCQKFLEE EEEITINVTS KAGGIKKYQE CIPVQSGASP ELSPFYQKYS SRTQYAVLYM
NPHKINLDLI LELLVYLDKS PQFRNIEGAV LIFLPGLAHI QQLYDLLSND RRFYSERYQL
IALHSVLSTQ DQAAAFMLPP PGVRKIVLAT NIAETGITIP DVVFVIDTGR TKENKYHESS
QMSSLVETFV SKASALQRQG RAGRVRDGFC FRLYTRERFE GFLEYSVPEI LRVPLEELCL
HIMKCDLGSP EDFLSKALDP PQPQVISNAM NLLRKIGACE PSEPKLTPLG QHLAALPVNV
KIGKMLIFGA IFGCLEPVAT LAAVMTEKSP FITPIGRKDE ADLAKSSLAV ADSDHLTIYN
AYLGWKKAQQ EGGFRSEISY CQRNFLNRTS LLTLEDVKQE LMKLVRAAGF SSSTSWEGKK
GPQALSFQDI ALLKAVLAAG LYDSVGKIMC TKSVDVTEKL ACMVETAQGK AQVHPSSVNR
DLQTYGWLLY QEKVRYARVY LRETTLITPF PVLLFGGDIE VQHRERLLSV DGWIYFQAPV
KIAVIFKQLR VLIDSVLRKK LENPKMSLEN DKILQIITEL IKTENN
//
