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 19-MAR-2014, entry version 62. DE RecName: Full=Regulator of telomere elongation helicase 1; DE EC=3.6.4.12; GN Name=Rtel1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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 RT project: 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. CC Acts as an anti-recombinase to counteract toxic recombination and CC limit crossover during meiosis. Regulates meiotic recombination CC and crossover homeostasis by physically dissociating strand CC invasion events and thereby promotes noncrossover repair by CC meiotic synthesis dependent strand annealing (SDSA) as well as CC disassembly of D loop recombination intermediates. Also CC disassembles T loops and prevents telomere fragility by CC counteracting telomeric G4-DNA structures, which together ensure CC the dynamics and stability of the telomere (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBUNIT: Interacts with TERF1. Interacts (via PIP-box) with PCNA; CC the interaction is direct and essential for suppressing telomere CC fragility. Interacts with MMS19; the interaction mediates the CC association of RTEL1 with the cytosolic iron-sulfur protein CC assembly (CIA) complex (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Colocalizes CC with PCNA within the replication foci in S-phase cells (By CC similarity). 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 Note=No experimental confirmation available; CC -!- DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates the CC interaction with PCNA and localization to replication foci (By CC similarity). CC -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SEQUENCE CAUTION: CC Sequence=EDL88727.1; Type=Erroneous gene model prediction; 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. DR UniGene; Rn.98315; -. DR STRING; 10116.ENSRNOP00000051909; -. 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; COG1199; -. DR GeneTree; ENSGT00530000063199; -. DR HOGENOM; HOG000007558; -. DR KO; K11136; -. DR OMA; VLKMQFL; -. DR OrthoDB; EOG7N8ZTR; -. DR NextBio; 679364; -. DR Genevestigator; Q5RJZ1; -. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB. DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB. DR HAMAP; MF_03065; RTEL1; 1. DR InterPro; IPR006555; ATP-dep_Helicase_C. DR InterPro; IPR010614; DEAD_2. DR InterPro; IPR013020; DNA_helicase_DNA-repair_Rad3. DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3. DR InterPro; IPR006554; Helicase-like_DEXD_c2. DR InterPro; IPR006935; Helicase/UvrB_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF06733; DEAD_2; 1. DR Pfam; PF13307; Helicase_C_2; 1. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00488; DEXDc2; 1. DR SMART; SM00491; HELICc2; 1. DR SUPFAM; SSF52540; SSF52540; 8. 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; Complete proteome; KW DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase; Iron; KW Iron-sulfur; Metal-binding; Nucleotide-binding; Nucleus; KW Reference proteome. FT CHAIN 1 1274 Regulator of telomere elongation helicase FT 1. FT /FTId=PRO_0000370613. FT DOMAIN 7 296 Helicase ATP-binding. FT NP_BIND 42 49 ATP (By similarity). FT MOTIF 151 167 Nuclear localization signal (Potential). FT MOTIF 250 253 DEAH box. FT MOTIF 871 877 Nuclear localization signal (Potential). FT METAL 145 145 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 163 163 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 172 172 Iron-sulfur (4Fe-4S) (By similarity). FT METAL 207 207 Iron-sulfur (4Fe-4S) (By similarity). FT VAR_SEQ 995 998 SKQG -> R (in isoform 2). FT /FTId=VSP_036956. FT VAR_SEQ 1112 1139 RFGMFIRRHHKPRFVQTCADLMGLPTIG -> S (in FT isoform 2). FT /FTId=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 //