RTEL1_MUSSP
ID RTEL1_MUSSP Reviewed; 1203 AA.
AC Q6H1L8; Q6H0K8; Q6H1L4; Q6H1L5; Q6H1L6; Q6H1L7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Rtel;
OS Mus spretus (Western Mediterranean mouse) (Algerian mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10096;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
RC 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).
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=6;
CC Name=1;
CC IsoId=Q6H1L8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6H1L8-2; Sequence=VSP_036953;
CC Name=3;
CC IsoId=Q6H1L8-3; Sequence=VSP_036953, VSP_036955;
CC Name=4;
CC IsoId=Q6H1L8-4; Sequence=VSP_036951;
CC Name=5;
CC IsoId=Q6H1L8-5; Sequence=VSP_036954;
CC Name=6;
CC IsoId=Q6H1L8-6; Sequence=VSP_036952;
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; AY481613; AAR27228.1; -; mRNA.
DR EMBL; AY481614; AAR27229.1; -; mRNA.
DR EMBL; AY481615; AAR27230.1; -; mRNA.
DR EMBL; AY481616; AAR27231.1; -; mRNA.
DR EMBL; AY481617; AAR27232.1; -; mRNA.
DR EMBL; AY530632; AAS98192.1; -; mRNA.
DR AlphaFoldDB; Q6H1L8; -.
DR SMR; Q6H1L8; -.
DR MGI; MGI:2139369; Rtel1.
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.
FT CHAIN 1..1203
FT /note="Regulator of telomere elongation helicase 1"
FT /id="PRO_0000370611"
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 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 981..1019
FT /note="GKSELESKLTLSEGVDRQLDPGQHLNHGQPHLSAHPTSK -> AHFSKP
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15210109"
FT /id="VSP_036951"
FT VAR_SEQ 981..1019
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15210109"
FT /id="VSP_036952"
FT VAR_SEQ 1019
FT /note="K -> KAHFSKP (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15210109"
FT /id="VSP_036953"
FT VAR_SEQ 1021..1095
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15210109"
FT /id="VSP_036954"
FT VAR_SEQ 1149..1203
FT /note="GPSMSKKPEKTQSKISSFFRQRPDESVRSDDTTPKPMQLPPRLPHELMKPHR
FT SKQ -> AIFRALDVQET (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15210109"
FT /id="VSP_036955"
SQ SEQUENCE 1203 AA; 133666 MW; 175D99E6E20882FA CRC64;
MPRVVLNGVT VDFPFQPYPC QQEYMTKVLE CLQKKVNGIL ESPTGTGKTL CLLCSTLAWQ
QHLRDAISSL KIAERVQGEL FASRTLSSWG SAAAASGDSI ECYTDIPKII YASRTHSQPT
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 EKQIPFPVCL ENPHIIDKNQ LWVGIVPRGP DGVQLSSAYD KRFSEECLSS
LGKALSNIAR VVPHGLLVFF PSYPVMEKSL EFWQVQGLAR KVEALKPLFV EPRNKGSFSE
VIDAYYQQVA SPASNGATFL AVCRGKASEG LDFSDMNGRG VIVTGLPYPP RMDPRVVLKM
QFLDEMRGRS GVGGQCLSGQ EWYQQQASRA VNQAIGRVIR HRHDYGAIFL CDHRFAYADA
RAQLPSWVRP YLKVYDNFGH AIRDVAQFLR VAQKTMPLPV PQAVTSSVSE GEIALKDATL
SSYSLSTRKA ISLDVHVPSL RQKSIGLPAA GDPESSLCGE YEQQTFSAQQ RPMGLLAALE
YNEQKAGASE EQALGSSTPS LRFEKRLSTE QKGGRKKVRL VNHPEEPMAG TQAGRAKMFM
VAVKQALSQA NFDTFTQALQ HYKSSDDFEA LVASLTCLFA EDPKKHTLLK GFYQFVRPHH
KQQFEDICFQ LTGQRCGYQP GKSELESKLT LSEGVDRQLD PGQHLNHGQP HLSAHPTSKG
HTSHCTKVGC AVEKPGQPAV SDYLSDVHKA LGSASCNQLT AALRAYKQDD DLDKVVAVVA
ALTTAKPEHL PLLQRFGMFV RRHHKPQFLQ TCADLMGLPT TGKDLELEGP RDESPTVPPE
LTHEDLKPGP SMSKKPEKTQ SKISSFFRQR PDESVRSDDT TPKPMQLPPR LPHELMKPHR
SKQ
