RTEL1_BOVIN
ID RTEL1_BOVIN Reviewed; 1216 AA.
AC A4K436; A4K3A3; A4K434; A4K435; A5J092;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 {ECO:0000255|HAMAP-Rule:MF_03065};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4 AND 5),
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17338827; DOI=10.1186/1471-2199-8-18;
RA Du Z., Zhao D., Zhao Y., Wang S., Gao Y., Li N.;
RT "Identification and characterization of bovine regulator of telomere length
RT elongation helicase gene (RTEL): molecular cloning, expression
RT distribution, splice variants and DNA methylation profile.";
RL BMC Mol. Biol. 8:18-18(2007).
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=5;
CC Name=1; Synonyms=SV-3;
CC IsoId=A4K436-1; Sequence=Displayed;
CC Name=2; Synonyms=SV-2;
CC IsoId=A4K436-2; Sequence=VSP_036942, VSP_036944;
CC Name=3;
CC IsoId=A4K436-3; Sequence=VSP_036944;
CC Name=4;
CC IsoId=A4K436-4; Sequence=VSP_036943;
CC Name=5; Synonyms=SV-1;
CC IsoId=A4K436-5; Sequence=VSP_036941;
CC -!- TISSUE SPECIFICITY: Highly expressed in adult testis, liver and ovary.
CC {ECO:0000269|PubMed:17338827}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the blastocyst stage.
CC {ECO:0000269|PubMed:17338827}.
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}.
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DR EMBL; DQ323152; ABC54575.1; -; Genomic_DNA.
DR EMBL; DQ323153; ABC54576.1; -; mRNA.
DR EMBL; DQ420360; ABD78306.1; -; mRNA.
DR EMBL; DQ420361; ABD78307.1; -; mRNA.
DR EMBL; DQ420362; ABD78308.1; -; mRNA.
DR EMBL; DQ420363; ABD78309.1; -; mRNA.
DR RefSeq; NP_001091044.1; NM_001097575.1. [A4K436-3]
DR AlphaFoldDB; A4K436; -.
DR SMR; A4K436; -.
DR STRING; 9913.ENSBTAP00000051019; -.
DR PaxDb; A4K436; -.
DR PRIDE; A4K436; -.
DR GeneID; 505721; -.
DR KEGG; bta:505721; -.
DR CTD; 51750; -.
DR eggNOG; KOG1132; Eukaryota.
DR InParanoid; A4K436; -.
DR OrthoDB; 186062at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; 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:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
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:0000723; P:telomere maintenance; 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; 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..1216
FT /note="Regulator of telomere elongation helicase 1"
FT /id="PRO_0000370609"
FT DOMAIN 7..295
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT REGION 978..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 150..166
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOTIF 249..252
FT /note="DEAH box"
FT MOTIF 874..880
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT MOTIF 1172..1179
FT /note="PIP-box"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 144
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 162
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 171
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT BINDING 206
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT VAR_SEQ 1063..1216
FT /note="VSAYLADVRRTLGAAGYSQLLTALTTYKQDDDFEKVVAVVAALTTEKPEDLP
FT LLQRFGMFVRPHHKQRFRQMCVDLSGPGTQAPGPQEGGPAMPSDPVCEAPSPGPRKTQS
FT KISSFLRCQACWRQHLQVSRKCPGCCAATRKQTLAQVFWPEPQ -> GSACSCGHTTSS
FT ASDRCVWT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17338827"
FT /id="VSP_036941"
FT VAR_SEQ 1063..1091
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17338827"
FT /id="VSP_036942"
FT VAR_SEQ 1119..1216
FT /note="FGMFVRPHHKQRFRQMCVDLSGPGTQAPGPQEGGPAMPSDPVCEAPSPGPRK
FT TQSKISSFLRCQACWRQHLQVSRKCPGCCAATRKQTLAQVFWPEPQ -> CLE (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:17338827"
FT /id="VSP_036943"
FT VAR_SEQ 1177
FT /note="S -> SFLMQRTAEDTGAPGSPLSFPRGQAQLEWAGVACAGCRAEDVVFFKC
FT PSCD (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:17338827"
FT /id="VSP_036944"
SQ SEQUENCE 1216 AA; 134448 MW; EFBE167EAE46F720 CRC64;
MPKITLKGVT VDFPFQPYKC QEEYMSKVLE CLQEKVNGIL ESPTGTGKTL CLLCSTLAWR
EHLRDAVSAR RIAERASGEL FPDRTLASWG NAIPEGDVPA CYTDIPKIIY ASRTHSQLTQ
VISELRNTSY RPRVCVLGSR EQLCIHPEVK KQESNHMQVH LCRRKVASRS CHFYNNVEEK
SLEQELATPI LDIEDLVRSG TKHKLCPYYL SRNLKQQADI IFMPYNYLLD AKSRRAHGID
LKGTVVIFDE AHNVEKMCEE AASFDLTPHD VASELDVIDR VLEERTKVAQ QAELHPEFSA
DSARSGLNLE PEDLAKLKMI LLRLEGAIDA VELPGDNSGV TKPGSYIFEL FAEAQITFQT
KGCILDSLDQ LIQHLAGRAG LFTNTAGLQK LVDIIQIVFS VDSAEGDPGP MVGLASQSYK
VHIHLDAGHR RTAQRSDVWN TTAARKPGKV LSYWCFSPGH SMRELVRQGV RTLILTSGTL
APMASFSLEM QIPFPVCLEN PHVINQHQIW VGVIPKGPDG AQLSSAFDRR FSDECLSSLG
KVLSNISRVV PHGLLVFFPS YPVMEKSLEF WRARDFTRKL EVRKPLFVEP RSKGGFSEVM
EAFYARVAAP ESSGAIFLAV CRGKASEGLD FADVNGRGVI VTGLPYPPRM DPRVLLKMQF
LDEMKAQSGA GGQFLSGHDW YRQQASRAVN QAIGRVIRHR HDYGAVFLCD HRFAHADTRA
QLPSWVRPHV KVYDSFGHVI RDVAQFFRVA QKTMPEPAPR AAAPSLGEGG GIVSVSVSPG
PLPTRKAMSL DVHVPSLRQR HTGSPVTKDT EGSLCVEYEQ EPVRAQRRPA GLLAALGHNE
QLAEGPGDEA LPVEEACGCP TLLGPREKRP AEEQRGRRRK VRLVGSSEVP AASTDTGRAK
LFMVAVKQAL SQASFDTFTQ ALRDYKSSDD LEALVARLSP LFAEDPKKHS LLQGFYQFVR
PHHKQQFEEV CLQLTGQGCS SPHKHGHPQR QGAQLALDSS GRKESDPKLT VSQGATRQLD
PCEQLNQGRP HLASGPFPAG DLNCSLHKGS RAPGAEKQHP STVSAYLADV RRTLGAAGYS
QLLTALTTYK QDDDFEKVVA VVAALTTEKP EDLPLLQRFG MFVRPHHKQR FRQMCVDLSG
PGTQAPGPQE GGPAMPSDPV CEAPSPGPRK TQSKISSFLR CQACWRQHLQ VSRKCPGCCA
ATRKQTLAQV FWPEPQ
