RTEL1_MOUSE
ID RTEL1_MOUSE Reviewed; 1203 AA.
AC Q0VGM9; A2AU09; A2AU10; A2AU11; A2AU12; A2AU13; A2AU14; Q3UM40; Q5F0J8;
AC Q69ZS1; Q6H1L0; Q6H1L1; Q6H1L2; Q6H1L3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 124.
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; Synonyms=Kiaa1088, Rtel;
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 [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=15210109; DOI=10.1016/j.cell.2004.05.026;
RA Ding H., Schertzer M., Wu X., Gertsenstein M., Selig S., Kammori M.,
RA Pourvali R., Poon S., Vulto I., Chavez E., Tam P.P.L., Nagy A.,
RA Lansdorp P.M.;
RT "Regulation of murine telomere length by Rtel: an essential gene encoding a
RT helicase-like protein.";
RL Cell 117:873-886(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Egg;
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 [6]
RP IDENTIFICATION.
RX PubMed=9671732; DOI=10.1073/pnas.95.15.8648;
RA Zhu L., Hathcock K.S., Hande P., Lansdorp P.M., Seldin M.F., Hodes R.J.;
RT "Telomere length regulation in mice is linked to a novel chromosome
RT locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8648-8653(1998).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=18064678; DOI=10.1002/dvg.20359;
RA Wu X., Sandhu S., Ding H.;
RT "Establishment of conditional knockout alleles for the gene encoding the
RT regulator of telomere length (RTEL).";
RL Genesis 45:788-792(2007).
RN [8]
RP FUNCTION IN TELOMERE INTEGRITY MAINTENANCE.
RX PubMed=22579284; DOI=10.1016/j.cell.2012.03.030;
RA Vannier J.B., Pavicic-Kaltenbrunner V., Petalcorin M.I., Ding H.,
RA Boulton S.J.;
RT "RTEL1 dismantles T loops and counteracts telomeric G4-DNA to maintain
RT telomere integrity.";
RL Cell 149:795-806(2012).
RN [9]
RP FUNCTION.
RX PubMed=22593209; DOI=10.1091/mbc.e12-03-0179;
RA Uringa E.J., Lisaingo K., Pickett H.A., Brind'Amour J., Rohde J.H.,
RA Zelensky A., Essers J., Lansdorp P.M.;
RT "RTEL1 contributes to DNA replication and repair and telomere
RT maintenance.";
RL Mol. Biol. Cell 23:2782-2792(2012).
RN [10]
RP FUNCTION, INTERACTION WITH PCNA, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF LYS-48; GLN-1160; ILE-1163; PHE-1166 AND PHE-1167.
RX PubMed=24115439; DOI=10.1126/science.1241779;
RA Vannier J.B., Sandhu S., Petalcorin M.I., Wu X., Nabi Z., Ding H.,
RA Boulton S.J.;
RT "RTEL1 is a replisome-associated helicase that promotes telomere and
RT genome-wide replication.";
RL Science 342:239-242(2013).
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, ECO:0000269|PubMed:15210109,
CC ECO:0000269|PubMed:22579284, ECO:0000269|PubMed:22593209,
CC ECO:0000269|PubMed:24115439}.
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, ECO:0000269|PubMed:24115439}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065,
CC ECO:0000269|PubMed:15210109, ECO:0000269|PubMed:24115439}.
CC Note=Colocalizes with PCNA within the replication foci in S-phase
CC cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q0VGM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0VGM9-2; Sequence=VSP_036949;
CC Name=3;
CC IsoId=Q0VGM9-3; Sequence=VSP_036947;
CC Name=4;
CC IsoId=Q0VGM9-4; Sequence=VSP_036950;
CC Name=5;
CC IsoId=Q0VGM9-5; Sequence=VSP_036948;
CC Name=6;
CC IsoId=Q0VGM9-6; Sequence=VSP_036945, VSP_036946;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in spleen, thymus,
CC Peyer patches, kidney, and intestine. Not expressed in brain, heart,
CC lung, skeletal muscles, skin and white fat. In the adult gonad, it is
CC highly expressed in the testis, mainly in the spermatogonia and meiotic
CC spermatocytes. {ECO:0000269|PubMed:15210109}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed in 8.5 dpc and 9.5 dpc embryos
CC with a more restricted expression pattern at 13.5 dpc-15.5 dpc. In
CC general, expression in embryos coincides with areas of actively
CC proliferating cells.
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, ECO:0000269|PubMed:24115439}.
CC -!- DISRUPTION PHENOTYPE: Death between days 10 and 11.5 of gestation with
CC defects in the nervous system, heart, vasculature and extraembryonic
CC tissues. Effects are due to severe genome instability and stochastic
CC telomere loss in embryonic stem cells which display many chromosome
CC breaks and fusions upon differentiation in vitro.
CC {ECO:0000269|PubMed:15210109, ECO:0000269|PubMed:18064678}.
CC -!- MISCELLANEOUS: Able to elongate M.spretus telomeres in crosses between
CC M.musculus and M.spretus.
CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03065}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32375.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAM26418.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY481619; AAR27234.1; -; mRNA.
DR EMBL; AY481620; AAR27235.1; -; mRNA.
DR EMBL; AY481621; AAR27236.1; -; mRNA.
DR EMBL; AY481622; AAR27237.1; -; mRNA.
DR EMBL; AY481623; AAR27238.1; -; mRNA.
DR EMBL; AK173097; BAD32375.1; ALT_INIT; mRNA.
DR EMBL; AK145145; BAE26258.1; -; mRNA.
DR EMBL; AL928965; CAM26413.1; -; Genomic_DNA.
DR EMBL; AL928965; CAM26414.1; -; Genomic_DNA.
DR EMBL; AL928965; CAM26415.1; -; Genomic_DNA.
DR EMBL; AL928965; CAM26416.1; -; Genomic_DNA.
DR EMBL; AL928965; CAM26417.1; -; Genomic_DNA.
DR EMBL; AL928965; CAM26418.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC105578; AAI05579.1; -; mRNA.
DR EMBL; BC144977; AAI44978.1; -; mRNA.
DR EMBL; BC144978; AAI44979.1; -; mRNA.
DR EMBL; BC145658; AAI45659.1; -; mRNA.
DR CCDS; CCDS17208.1; -. [Q0VGM9-2]
DR CCDS; CCDS50849.1; -. [Q0VGM9-1]
DR CCDS; CCDS50850.1; -. [Q0VGM9-4]
DR CCDS; CCDS50851.1; -. [Q0VGM9-3]
DR CCDS; CCDS50852.1; -. [Q0VGM9-5]
DR RefSeq; NP_001001882.3; NM_001001882.3. [Q0VGM9-2]
DR RefSeq; NP_001160137.1; NM_001166665.1. [Q0VGM9-1]
DR RefSeq; NP_001160138.1; NM_001166666.1. [Q0VGM9-3]
DR RefSeq; NP_001160139.1; NM_001166667.1. [Q0VGM9-5]
DR RefSeq; NP_001160140.1; NM_001166668.1. [Q0VGM9-4]
DR AlphaFoldDB; Q0VGM9; -.
DR SMR; Q0VGM9; -.
DR STRING; 10090.ENSMUSP00000053120; -.
DR iPTMnet; Q0VGM9; -.
DR PhosphoSitePlus; Q0VGM9; -.
DR EPD; Q0VGM9; -.
DR jPOST; Q0VGM9; -.
DR MaxQB; Q0VGM9; -.
DR PaxDb; Q0VGM9; -.
DR PRIDE; Q0VGM9; -.
DR ProteomicsDB; 260945; -. [Q0VGM9-1]
DR ProteomicsDB; 260946; -. [Q0VGM9-2]
DR ProteomicsDB; 260947; -. [Q0VGM9-3]
DR ProteomicsDB; 260948; -. [Q0VGM9-4]
DR ProteomicsDB; 260949; -. [Q0VGM9-5]
DR ProteomicsDB; 260950; -. [Q0VGM9-6]
DR DNASU; 269400; -.
DR Ensembl; ENSMUST00000048608; ENSMUSP00000043563; ENSMUSG00000038685. [Q0VGM9-4]
DR Ensembl; ENSMUST00000054622; ENSMUSP00000053120; ENSMUSG00000038685. [Q0VGM9-2]
DR Ensembl; ENSMUST00000098971; ENSMUSP00000096571; ENSMUSG00000038685. [Q0VGM9-3]
DR Ensembl; ENSMUST00000108814; ENSMUSP00000104442; ENSMUSG00000038685. [Q0VGM9-1]
DR Ensembl; ENSMUST00000108815; ENSMUSP00000104443; ENSMUSG00000038685. [Q0VGM9-5]
DR GeneID; 269400; -.
DR KEGG; mmu:269400; -.
DR UCSC; uc008olu.2; mouse. [Q0VGM9-6]
DR UCSC; uc008olv.2; mouse. [Q0VGM9-2]
DR UCSC; uc008olw.2; mouse. [Q0VGM9-1]
DR UCSC; uc008olx.2; mouse. [Q0VGM9-3]
DR UCSC; uc012cmk.1; mouse. [Q0VGM9-5]
DR UCSC; uc012cml.1; mouse. [Q0VGM9-4]
DR CTD; 51750; -.
DR MGI; MGI:2139369; Rtel1.
DR VEuPathDB; HostDB:ENSMUSG00000038685; -.
DR eggNOG; KOG1132; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR HOGENOM; CLU_006515_4_0_1; -.
DR InParanoid; Q0VGM9; -.
DR OMA; WRANGHT; -.
DR OrthoDB; 186062at2759; -.
DR TreeFam; TF317291; -.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR BioGRID-ORCS; 269400; 34 hits in 112 CRISPR screens.
DR ChiTaRS; Rtel1; mouse.
DR PRO; PR:Q0VGM9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q0VGM9; protein.
DR Bgee; ENSMUSG00000038685; Expressed in spermatocyte and 233 other tissues.
DR ExpressionAtlas; Q0VGM9; baseline and differential.
DR Genevisible; Q0VGM9; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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; IDA:BHF-UCL.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
DR GO; GO:0004386; F:helicase activity; TAS:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:BHF-UCL.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; IDA:BHF-UCL.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IDA:BHF-UCL.
DR GO; GO:1904430; P:negative regulation of t-circle formation; IMP:BHF-UCL.
DR GO; GO:1904506; P:negative regulation of telomere maintenance in response to DNA damage; IMP:BHF-UCL.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IMP:BHF-UCL.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; ISO:MGI.
DR GO; GO:1904535; P:positive regulation of telomeric loop disassembly; IDA:BHF-UCL.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; IDA:BHF-UCL.
DR GO; GO:0000732; P:strand displacement; IDA:BHF-UCL.
DR GO; GO:0000723; P:telomere maintenance; IMP:MGI.
DR GO; GO:0043247; P:telomere maintenance in response to DNA damage; IMP:BHF-UCL.
DR GO; GO:0061820; P:telomeric D-loop disassembly; TAS:BHF-UCL.
DR GO; GO:0090657; P:telomeric loop disassembly; IDA:BHF-UCL.
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 1: Evidence at protein 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..1203
FT /note="Regulator of telomere elongation helicase 1"
FT /id="PRO_0000370610"
FT DOMAIN 7..296
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 998..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1203
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 MOTIF 1160..1167
FT /note="PIP-box"
FT COMPBIAS 1002..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1168
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 451..527
FT /note="KVLSYWCFSPSQSMRELVCQGVRTLILTSGTLAPLSSFALEMQIPFPVCLEN
FT PHIIDKNQLWVGIVPRGPDGVQLSS -> TNLHCRKLYLAQPLHNNNITSGVMPTESQR
FT QEALLSTQRHLLGQWQNPGSARPPLPDLGYIIINHYRHYYYYFVFSR (in isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036945"
FT VAR_SEQ 528..1203
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036946"
FT VAR_SEQ 981..1019
FT /note="GKRELESKLTLSEGVDRQLDPGQHLNQGQPHLSAHPTSK -> AHFSKP
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15210109"
FT /id="VSP_036947"
FT VAR_SEQ 981..1019
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15210109"
FT /id="VSP_036948"
FT VAR_SEQ 1019
FT /note="K -> KAHFSKP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15210109,
FT ECO:0000303|PubMed:15368895"
FT /id="VSP_036949"
FT VAR_SEQ 1021..1095
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15210109"
FT /id="VSP_036950"
FT MUTAGEN 48
FT /note="K->R: Abolishes G4-DNA unwinding activity."
FT /evidence="ECO:0000269|PubMed:24115439"
FT MUTAGEN 1160
FT /note="Q->A: Abolishes interaction with PCNA."
FT /evidence="ECO:0000269|PubMed:24115439"
FT MUTAGEN 1163
FT /note="I->A: Abolishes interaction with PCNA."
FT /evidence="ECO:0000269|PubMed:24115439"
FT MUTAGEN 1166
FT /note="F->A: Abolishes interaction with PCNA."
FT /evidence="ECO:0000269|PubMed:24115439"
FT MUTAGEN 1167
FT /note="F->A: Abolishes interaction with PCNA."
FT /evidence="ECO:0000269|PubMed:24115439"
FT CONFLICT 180
FT /note="A -> T (in Ref. 4; AAI05579)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="G -> R (in Ref. 1; AAR27234/AAR27235/AAR27236/
FT AAR27237/AAR27238)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="F -> S (in Ref. 4; AAI05579)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="V -> A (in Ref. 4; AAI05579)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="G -> S (in Ref. 1; AAR27234/AAR27235/AAR27236/
FT AAR27237/AAR27238)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="F -> L (in Ref. 4; AAI05579)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="F -> S (in Ref. 4; AAI05579)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="H -> R (in Ref. 4; AAI05579)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1203 AA; 133767 MW; 670573FEF1E2D1B1 CRC64;
MPRVVLNGVT VDFPFQPYPC QQEYMTKVLE CLQKKVNGIL ESPTGTGKTL CLLCSTLAWQ
QHLRDAVSSL KIAERVQGEL FASRTLSSWG SAAAASGDSI ECYTDIPKII YASRTHSQLT
QVIRELRNTA YRPKVCVLGS REQLCIHPEV KKQESNHMQI SLCRKKVASR SCHFYNNVEA
KFLEQDLATP ILDIEDLVKN GSKQKMCPYY LSRNMKQQAD IIFMPYNYLL DAKSRKAHSI
DLKGTVVIFD EAHNVEKICE ESASFDLTPR DVASGLEIIN QVLEEQARVT QQGELQQEFI
VDTSSSGLNM ELEDIAKLKM ILLRLEEAID AVQLPGDDRG VTKPGSYIFE LFAEAQITFQ
TKGCILESLD QIIQHLAGRT GVFTNTAGLQ KLMDIIQIVF SVDPPEGSPG SLVGLGISHS
YKVHIHPETS HRRAAKRSDA WSTTASRKQG KVLSYWCFSP SQSMRELVCQ GVRTLILTSG
TLAPLSSFAL EMQIPFPVCL ENPHIIDKNQ LWVGIVPRGP DGVQLSSAYD KRFSEECLSS
LGKALSNIAR VVPHGLLVFF PSYPVMEKSL EFWQVQGLAR KVEALKPLFV EPRNKGSFSE
VIDAYYQQVA SPASNGATFL AVCRGKASEG LDFSDMNGRG VIVTGLPYPP RMDPRVVLKM
QFLDEMRGRS GVGGQCLSGQ EWYQQQASRA VNQAIGRVIR HRHDYGAIFL CDHRFAYADA
RAQLPSWVRP YLKVYDNFGH VIRDVAQFFR VAQKTMPLPV PQAVTSSVSE GEIALKDATL
SSYSLSTRKA MSLDVHVPSL RQKPIGLPAA GDSESSLCGE YEQQTFSAQQ RPMGLLAALE
YNEQKAGASE EQALGSSTPS LRCEKRLSTE QKGGRKKVRL VNHPEEPMAG TQAGRAKMFM
VAVKQALSQA NFDTFTQALQ HYKSSDDFEA LVASLTCLFA EDPKKHTLLK GFYQFVRPHH
KQQFEDICFQ LTGQRCGYQP GKRELESKLT LSEGVDRQLD PGQHLNQGQP HLSAHPTSKG
HTSHCTKVGC AVEKPGQPAV SDYLSDVHKA LGSASCNQLT AALRAYKQDD DLDKVVAVVA
ALTTAKPEHL PLLQRFGMFV RRHHKPQFLQ TCADLMGLPT TGKDLELEGP RDESPTVPPE
LTHEDLKPGP SMSKKPEKTQ SKISSFFRQR PDESVRSDDT TPKPMQLPPR LPHELMKPHR
SKQ
