RTEL1_DROME
ID RTEL1_DROME Reviewed; 985 AA.
AC Q9W484; A9YIV5; A9YIV6; A9YIW4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Regulator of telomere elongation helicase 1 homolog {ECO:0000255|HAMAP-Rule:MF_03065};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03065};
GN Name=Rtel1 {ECO:0000303|PubMed:34644293, ECO:0000312|FlyBase:FBgn0029798};
GN ORFNames=CG4078 {ECO:0000312|FlyBase:FBgn0029798};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-305, AND VARIANTS ASP-81; THR-95
RP AND GLN-294 DEL.
RC STRAIN=ZW104, ZW106, ZW109, ZW122, ZW123, ZW133, ZW136, ZW139, ZW140,
RC ZW141, ZW142, and ZW143;
RX PubMed=17989248; DOI=10.1101/gr.6691007;
RA Andolfatto P.;
RT "Hitchhiking effects of recurrent beneficial amino acid substitutions in
RT the Drosophila melanogaster genome.";
RL Genome Res. 17:1755-1762(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-874, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=34644293; DOI=10.1371/journal.pgen.1009834;
RA Yang Y., Kong R., Goh F.G., Somers W.G., Hime G.R., Li Z., Cai Y.;
RT "dRTEL1 is essential for the maintenance of Drosophila male germline stem
RT cells.";
RL PLoS Genet. 17:e1009834-e1009834(2021).
CC -!- FUNCTION: ATP-dependent DNA helicase implicated in DNA repair and the
CC maintenance of genomic stability. Acts as an anti-recombinase to
CC counteract toxic recombination and limit crossover during meiosis.
CC Regulates meiotic recombination and crossover homeostasis by physically
CC dissociating strand invasion events and thereby promotes noncrossover
CC repair by meiotic synthesis dependent strand annealing (SDSA) as well
CC as disassembly of D loop recombination intermediates (By similarity).
CC In male germline stem cells (GSCs), plays a role in GSCs maintenance
CC during larval germline development by modulating the expression of
CC genes such as Stat92E and preventing DNA damage-induced checkpoint
CC activation (PubMed:34644293). May play a role in female germline stem
CC cell maintenance (PubMed:34644293). {ECO:0000255|HAMAP-Rule:MF_03065,
CC ECO:0000269|PubMed:34644293}.
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=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03065};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065,
CC ECO:0000269|PubMed:34644293}. Chromosome {ECO:0000269|PubMed:34644293}.
CC -!- TISSUE SPECIFICITY: Expressed in both male germline and somatic cells
CC (at protein level) (PubMed:34644293). Expressed in ovarian germline
CC stem cells (at protein level) (PubMed:34644293). Expressed in adult
CC testes (at protein level) (PubMed:34644293). Expressed in the germarium
CC including germline stem cells (PubMed:34644293).
CC {ECO:0000269|PubMed:34644293}.
CC -!- DISRUPTION PHENOTYPE: In males, RNAi-mediated knockdown in germ cells
CC results in loss of male germline stem cells (GSCs) at day 14,
CC appearance of branched fusomes and down regulation of a number of genes
CC including Stat92E expression in adult testes (PubMed:34644293). In
CC females, RNAi-mediated knockdown in germ cells results in a decrease in
CC germline stem cells in the germaria (PubMed:34644293). RNAi-mediated
CC knockdown in somatic cells or in differentiating spermatogonia does not
CC affect GSC number in larval and adult testes or female germaria
CC (PubMed:34644293). In the germline, simultaneous RNAi-mediated
CC knockdown of Rtel1 and grp results in partial rescue of loss of
CC germline stem cell (PubMed:34644293). In the germline, RNAi-mediated
CC knockdown of Rtel1 in a lok mutant background results in partial rescue
CC of loss of germline stem cell, including restored levels of Stat92E
CC expression (PubMed:34644293). {ECO:0000269|PubMed:34644293}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03065}.
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DR EMBL; AE014298; AAF46074.1; -; Genomic_DNA.
DR EMBL; BT021290; AAX33438.1; -; mRNA.
DR EMBL; EU217688; ABW92607.1; -; Genomic_DNA.
DR EMBL; EU217689; ABW92608.1; -; Genomic_DNA.
DR EMBL; EU217690; ABW92609.1; -; Genomic_DNA.
DR EMBL; EU217691; ABW92610.1; -; Genomic_DNA.
DR EMBL; EU217692; ABW92611.1; -; Genomic_DNA.
DR EMBL; EU217693; ABW92612.1; -; Genomic_DNA.
DR EMBL; EU217694; ABW92613.1; -; Genomic_DNA.
DR EMBL; EU217695; ABW92614.1; -; Genomic_DNA.
DR EMBL; EU217696; ABW92615.1; -; Genomic_DNA.
DR EMBL; EU217697; ABW92616.1; -; Genomic_DNA.
DR EMBL; EU217698; ABW92617.1; -; Genomic_DNA.
DR EMBL; EU217699; ABW92618.1; -; Genomic_DNA.
DR RefSeq; NP_001259262.1; NM_001272333.1.
DR RefSeq; NP_572254.1; NM_132026.2.
DR AlphaFoldDB; Q9W484; -.
DR SMR; Q9W484; -.
DR BioGRID; 57997; 5.
DR IntAct; Q9W484; 6.
DR STRING; 7227.FBpp0304672; -.
DR iPTMnet; Q9W484; -.
DR PaxDb; Q9W484; -.
DR EnsemblMetazoa; FBtr0070807; FBpp0070773; FBgn0029798.
DR EnsemblMetazoa; FBtr0332398; FBpp0304672; FBgn0029798.
DR GeneID; 31497; -.
DR KEGG; dme:Dmel_CG4078; -.
DR UCSC; CG4078-RA; d. melanogaster.
DR FlyBase; FBgn0029798; Rtel1.
DR VEuPathDB; VectorBase:FBgn0029798; -.
DR eggNOG; KOG1132; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; Q9W484; -.
DR OMA; GNCATIV; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; Q9W484; -.
DR BioGRID-ORCS; 31497; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 31497; -.
DR PRO; PR:Q9W484; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029798; Expressed in gastric caecum (Drosophila) and 49 other tissues.
DR ExpressionAtlas; Q9W484; baseline and differential.
DR Genevisible; Q9W484; DM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0070182; F:DNA polymerase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:2001021; P:negative regulation of response to DNA damage stimulus; IMP:FlyBase.
DR GO; GO:1904430; P:negative regulation of t-circle formation; IBA:GO_Central.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0090657; P:telomeric loop disassembly; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_03065; RTEL1; 1.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR010614; DEAD_2.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR InterPro; IPR030845; RTEL1.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; ATP-binding; Chromosome; DNA damage; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..985
FT /note="Regulator of telomere elongation helicase 1 homolog"
FT /id="PRO_0000370623"
FT DOMAIN 7..303
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 863..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 252..255
FT /note="DEAH box"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 146
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 173
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 209
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOD_RES 874
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VARIANT 81
FT /note="G -> D (in strain: ZW104)"
FT /evidence="ECO:0000269|PubMed:17989248"
FT VARIANT 95
FT /note="A -> T (in strain: ZW141)"
FT /evidence="ECO:0000269|PubMed:17989248"
FT VARIANT 294
FT /note="Missing (in strain: ZW104 and ZW141)"
FT /evidence="ECO:0000269|PubMed:17989248"
SQ SEQUENCE 985 AA; 109683 MW; 84CFDDC26EF255DC CRC64;
MPESLIAGIP VHFPFEPYPV QRAYMEKVIH CLRDGTNGVL ESPTGTGKTL SLLCSSLAWI
RTRQSEHQKQ MVKMEKADFS GLGGGAPGGD LSELAKTMGR ANNWGVPKVI YASRTHSQLT
QAMRELKRTA YANMRSVVLG SRDQLCIHPE VMREQGNSNK TNMCKLRVHS KTCSFQMRVE
SRKDHPDLRG PTIMDIEDLV KVGQRLKICP YFASRELVPQ ADITFMPYNY LLDPKARKAN
KIELGNTIVI LDEAHNIEKI CEESASVQIK SSDVAMAIED VTHIMQVFAS GESQDMAGDE
PKDFTLDDLT LLKEMLLELE KAIDAIVVDN AVDGTTFPAS MMYELLGKAN FTYGNVATIV
SLLDKLVQYL LVASQQMSIR KGGTFTLLSD LLTIVFANKE DVMSKVYASF KVHVLVEESK
QGHGKQQGAK QQGGWLGKGT IAAATGLSKV AKIINFWCFN PGFGMEQLLN TQVRSVILTS
GTLAPLKPLI AELAIPVAQH LENPHIVDQS QVYVKIIGTG PDRQQLISNY ANRDNPKYIS
SLGQTILNVA RIVPDGLLVF FPSYPMLNKC VDAWQASGLW ADISCKKPIF LEPRSKDQFT
STMEEFYQAI RDSKGAVFMA VCRGKVSEGL DFADRNGRAV IITGLPFPPL KDPKVILKRR
YLEANRTREN QLLSGQEWYN LDATRAVNQA IGRVIRHRND YGAILLCDSR FKDASQVQQL
SKWIRGHLGD RPQCSPFGPI VRELRQFFKN AEANMKLPDE RETDSPLETV CKTEDEPLAA
IPKVKREPGS NATFKSANES AIKVEMANSI KTWTPADYAS AAGHKLGGAA PNAMDFMSRL
DSNVSSIDFN CCTDSKSGSS GLVKIHKRER SSPTAPESSS QVTKKRYKLV ENIKVEPSSS
QAKEAPEERA AFLRELRSLV TQDQFRRFGK ALLEYKNGTY ESFQALMAIL LDVLSAPKVR
YMLVGMRKYL KNEHKDEFDR RVGNL
