ID RTEL1_RAT Reviewed; 1274 AA. AC Q5RJZ1; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 29-MAY-2024, entry version 119. DE RecName: Full=Regulator of telomere elongation helicase 1 {ECO:0000255|HAMAP-Rule:MF_03065}; DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03065}; GN Name=Rtel1; 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 [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-1274 (ISOFORM 2). RC TISSUE=Ovary; 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). CC -!- FUNCTION: ATP-dependent DNA helicase implicated in telomere-length CC regulation, DNA repair and the maintenance of genomic stability. Acts CC as an anti-recombinase to counteract toxic recombination and limit CC crossover during meiosis. Regulates meiotic recombination and crossover CC homeostasis by physically dissociating strand invasion events and CC thereby promotes noncrossover repair by meiotic synthesis dependent CC strand annealing (SDSA) as well as disassembly of D loop recombination CC intermediates. Also disassembles T loops and prevents telomere CC fragility by counteracting telomeric G4-DNA structures, which together CC ensure the dynamics and stability of the telomere. {ECO:0000255|HAMAP- CC Rule:MF_03065}. 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 -!- SUBUNIT: Interacts with TERF1. Interacts (via PIP-box) with PCNA; the CC interaction is direct and essential for suppressing telomere fragility. CC Interacts with MMS19; the interaction mediates the association of RTEL1 CC with the cytosolic iron-sulfur protein assembly (CIA) complex. CC {ECO:0000255|HAMAP-Rule:MF_03065}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065}. CC Note=Colocalizes with PCNA within the replication foci in S-phase CC cells. {ECO:0000255|HAMAP-Rule:MF_03065}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5RJZ1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5RJZ1-2; Sequence=VSP_036956, VSP_036957; CC -!- DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates the CC interaction with PCNA and localization to replication foci. CC {ECO:0000255|HAMAP-Rule:MF_03065}. CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_03065}. CC -!- SEQUENCE CAUTION: CC Sequence=EDL88727.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; CH474066; EDL88727.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC086436; AAH86436.1; -; mRNA. DR RefSeq; NP_001178786.1; NM_001191857.1. [Q5RJZ1-1] DR AlphaFoldDB; Q5RJZ1; -. DR SMR; Q5RJZ1; -. DR STRING; 10116.ENSRNOP00000051909; -. DR iPTMnet; Q5RJZ1; -. DR PhosphoSitePlus; Q5RJZ1; -. DR PaxDb; 10116-ENSRNOP00000051909; -. DR Ensembl; ENSRNOT00000055030.4; ENSRNOP00000051909.3; ENSRNOG00000027513.7. [Q5RJZ1-1] DR Ensembl; ENSRNOT00055001941; ENSRNOP00055001521; ENSRNOG00055001164. [Q5RJZ1-1] DR Ensembl; ENSRNOT00060001846; ENSRNOP00060001057; ENSRNOG00060001279. [Q5RJZ1-1] DR Ensembl; ENSRNOT00065022925; ENSRNOP00065017816; ENSRNOG00065013888. [Q5RJZ1-1] DR GeneID; 362288; -. DR KEGG; rno:362288; -. DR UCSC; RGD:1306721; rat. [Q5RJZ1-1] DR AGR; RGD:1306721; -. DR CTD; 51750; -. DR RGD; 1306721; Rtel1. DR eggNOG; KOG1132; Eukaryota. DR GeneTree; ENSGT00950000182970; -. DR InParanoid; Q5RJZ1; -. DR OMA; EDPNTHS; -. DR OrthoDB; 124793at2759; -. DR PhylomeDB; Q5RJZ1; -. DR Reactome; R-RNO-171319; Telomere Extension By Telomerase. DR PRO; PR:Q5RJZ1; -. DR Proteomes; UP000002494; Chromosome 3. DR Proteomes; UP000234681; Chromosome 3. DR Bgee; ENSRNOG00000027513; Expressed in thymus and 19 other cell types or tissues. DR ExpressionAtlas; Q5RJZ1; baseline and differential. DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD. DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl. DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. 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: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; ISO:RGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0032508; P:DNA duplex unwinding; ISO:RGD. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR GO; GO:0000732; P:DNA strand displacement; ISO:RGD. DR GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; ISO:RGD. DR GO; GO:0045910; P:negative regulation of DNA recombination; ISO:RGD. DR GO; GO:1904430; P:negative regulation of t-circle formation; ISO:RGD. DR GO; GO:1904506; P:negative regulation of telomere maintenance in response to DNA damage; ISO:RGD. DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:RGD. DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:RGD. DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; ISO:RGD. DR GO; GO:1904535; P:positive regulation of telomeric loop disassembly; ISO:RGD. DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB. DR GO; GO:0031297; P:replication fork processing; ISO:RGD. DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB. DR GO; GO:0043247; P:telomere maintenance in response to DNA damage; ISO:RGD. DR GO; GO:0090657; P:telomeric loop disassembly; ISO:RGD. DR CDD; cd17970; DEAHc_FancJ; 1. DR CDD; cd13932; HN_RTEL1; 2. DR CDD; cd18788; SF2_C_XPD; 1. DR Gene3D; 1.20.1160.20; -; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR HAMAP; MF_03065; RTEL1; 1. DR InterPro; IPR006555; ATP-dep_Helicase_C. 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; IPR049909; HHD_RTEL1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010614; RAD3-like_helicase_DEAD. DR InterPro; IPR013020; Rad3/Chl1-like. DR InterPro; IPR030845; RTEL1. DR NCBIfam; TIGR00604; rad3; 1. DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1. DR PANTHER; PTHR11472:SF34; REGULATOR OF TELOMERE ELONGATION HELICASE 1; 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; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1. PE 2: Evidence at transcript level; KW 4Fe-4S; Alternative splicing; ATP-binding; DNA damage; DNA repair; KW DNA-binding; Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; KW Nucleotide-binding; Nucleus; Reference proteome. FT CHAIN 1..1274 FT /note="Regulator of telomere elongation helicase 1" FT /id="PRO_0000370613" FT DOMAIN 7..296 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065" FT REGION 982..1002 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1014..1038 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1143..1198 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 151..167 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065" FT MOTIF 250..253 FT /note="DEAH box" FT MOTIF 871..877 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065" FT COMPBIAS 982..997 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1170..1197 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 42..49 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065" FT BINDING 145 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065" FT BINDING 163 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065" FT BINDING 172 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065" FT BINDING 207 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065" FT VAR_SEQ 995..998 FT /note="SKQG -> R (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_036956" FT VAR_SEQ 1112..1139 FT /note="RFGMFIRRHHKPRFVQTCADLMGLPTIG -> S (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_036957" SQ SEQUENCE 1274 AA; 141779 MW; CF7D27F451824347 CRC64; MPRVVLNGVT VDFPFQPYPC QQEYMTKVLE CLQKKVNGIL ESPTGTGKTL CLLCTTLAWR EHLRDAVSSL KIAERVQGEL FASRTLSSWR SAADANGDSI DCYTDIPKII YASRTHSQLT QVIGELRNTS YRPKVCVLGS REQLCIHPEV KKQESNHMQI SLCRKKVASR SCHFYNNVEE KSLEQELATP ILDIEDLVKN GSKHKVCPYY LSRNLKQQAD IIFMPYNYLL DAKSRKAHNI DLKGTVVIFD EAHNVEKICE ESASFDLTPR DVASGLEVIN QVLEEQARVA QHGELQQEFI IDTSSSGLNM ELEDIAKLKM ILLHLEEAID AVQLPGDDRG VTKPGSYIFE LFAEAQITFQ TKGCILESLD QIIQHLTGRT GVFTNTAGLQ KLMDIIQIVF SVDPLEGSPG SQVGLGSSHF YKVHIHPETS HRRAAQRSDA WSTTASRKQG KVLSYWCFSP SHSMRELVQQ GVRTLILTSG TLAPLSSFAL EMQIPFPVCL ENPHIIDKNQ LWVGVIPRGP DGVQLSSAYD KRFSEECLSS LGKALGNIAR VVPHGLLVFF PSYPVMEKSL EFWQAQGMSK KVEALKPLFV EPRNKGSFSE VIDAYYQQVA SPGSNGATFL AVCRGKASEG LDFSDMNGRG VIVTGLPYPP RMDPRVILKM QFLDEMKGRS RVGGQCLSGQ EWYQQQASRA VNQAIGRVIR HRHDYGAIFL CDHRFAYADA RAHLPSWVRP YLKVYDNFGR VIRDVAQFFR VAQKAMPLPV PQAVTSSVSE GEAAVKEATL SSHSLSTRKA MSLDVHVPSL RRRPVGLPTA GDSESSVCVE YEQQTFSAQK RPMGLLAALE YNEQKAGASE EQALSSSTPS LRCEKRLSVE QRGGKKKVRL VNHPEEPVAG TQAGRAKMFM VAVKQALSQA NFDTFTQALQ HYKSSDDFEA LVASLTCLFA EDPKKHTLLK GFYQFVRPHH KQQFEDICFQ LTGQRCSYQP GNSLPFGEQA QSTASKQGRR ELESKLTLSE GADRQLDPGE HLNQGWPHLS THLTSKGDTS NCPKVGCVGE KPGQPAVNDY LSDVHKALGS ASCNQLTAAL RAYKQDDDLD KVLAVVAALT TAKPEHLSLL QRFGMFIRRH HKPRFVQTCA DLMGLPTIGK GLELPCPRDE STTVPSELTH EDMKPGPSTS KKPEKTQSKI SSFLRQRPDQ SARSDDTIMQ LPPRLPPEHT TSQWNFVCPA CATEDTVLFQ CPSCDFCRCR ACWQRQLQAS RLCPACGAVN RKQSIAQVIW PKPQ //