RTEL1_RAT
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 03-AUG-2022, entry version 110.
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};
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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; Q5RJZ1; -.
DR PRIDE; Q5RJZ1; -.
DR Ensembl; ENSRNOT00000055030; ENSRNOP00000051909; ENSRNOG00000027513. [Q5RJZ1-1]
DR GeneID; 362288; -.
DR KEGG; rno:362288; -.
DR UCSC; RGD:1306721; rat. [Q5RJZ1-1]
DR CTD; 51750; -.
DR RGD; 1306721; Rtel1.
DR eggNOG; KOG1132; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR InParanoid; Q5RJZ1; -.
DR OMA; WRANGHT; -.
DR OrthoDB; 186062at2759; -.
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 tissues.
DR ExpressionAtlas; Q5RJZ1; baseline and differential.
DR Genevisible; Q5RJZ1; RN.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
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: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:0000732; P:strand displacement; 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 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; 2.
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 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
