RECQ5_MOUSE
ID RECQ5_MOUSE Reviewed; 982 AA.
AC Q8VID5; Q8BQD7; Q8C7T6; Q8VID3;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=ATP-dependent DNA helicase Q5;
DE EC=3.6.4.12;
DE AltName: Full=DNA helicase, RecQ-like type 5;
DE Short=RecQ5;
DE AltName: Full=RECQL5beta;
DE AltName: Full=RecQ protein-like 5;
GN Name=Recql5;
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], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
RP 412-982.
RC TISSUE=Fibroblast;
RX PubMed=11738818; DOI=10.1016/s0378-1119(01)00740-5;
RA Ohhata T., Araki R., Fukumura R., Kuroiwa A., Matsuda Y., Abe M.;
RT "Cloning, genomic structure and chromosomal localization of the gene
RT encoding mouse DNA helicase RECQL5beta.";
RL Gene 280:59-66(2001).
RN [2]
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 [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 234-982.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-527, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: DNA helicase that plays an important role in DNA replication,
CC transcription and repair. Binds to the RNA polymerase II subunit POLR2A
CC during transcription elongation and suppresses transcription-associated
CC genomic instability. Associates also with POLR1A and enforces the
CC stability of ribosomal DNA arrays. Plays an important role in mitotic
CC chromosome separation after cross-over events and cell cycle progress.
CC Mechanistically, removes RAD51 filaments protecting stalled replication
CC forks at common fragile sites and stimulates MUS81-EME1 endonuclease
CC leading to mitotic DNA synthesis. Required for efficient DNA repair,
CC including repair of inter-strand cross-links. Stimulates DNA
CC decatenation mediated by TOP2A. Prevents sister chromatid exchange and
CC homologous recombination. {ECO:0000250|UniProtKB:O94762}.
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:0000250|UniProtKB:O94762};
CC -!- SUBUNIT: Monomer. Interacts with TOP2A, TOP3A and TOP3B. Interacts with
CC RNA polymerase II subunit POLR2A. Identified in a complex with the RNA
CC polymerase II core bound to DNA. Interacts with RAD51 (By similarity).
CC Interacts with WRN; this interaction stimulates WRN helicase activity
CC on DNA fork duplexes (By similarity). Interacts with MUS1; this
CC interaction promotes MUS81-dependent mitotic DNA synthesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:O94762}. Note=Recruited to sites of DNA damage,
CC such as single-strand breaks and inter-strand cross-links, and at
CC stalled replication forks. {ECO:0000250|UniProtKB:O94762}.
CC -!- PTM: Phosphorylated by CDK1 at Ser-728; this phosphorylation is
CC required for RECQL5-mediated disruption of RAD51 filaments on stalled
CC replication forks. {ECO:0000250|UniProtKB:O94762}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AB060698; BAB79233.1; -; Genomic_DNA.
DR EMBL; AB059999; BAB79232.1; -; mRNA.
DR EMBL; AL645647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34531.1; -; Genomic_DNA.
DR EMBL; AK049269; BAC33647.1; -; mRNA.
DR EMBL; AK050965; BAC34479.1; -; mRNA.
DR CCDS; CCDS25650.1; -.
DR RefSeq; NP_569721.1; NM_130454.2.
DR AlphaFoldDB; Q8VID5; -.
DR SMR; Q8VID5; -.
DR STRING; 10090.ENSMUSP00000021097; -.
DR iPTMnet; Q8VID5; -.
DR PhosphoSitePlus; Q8VID5; -.
DR EPD; Q8VID5; -.
DR jPOST; Q8VID5; -.
DR MaxQB; Q8VID5; -.
DR PaxDb; Q8VID5; -.
DR PeptideAtlas; Q8VID5; -.
DR PRIDE; Q8VID5; -.
DR ProteomicsDB; 255280; -.
DR Antibodypedia; 19590; 180 antibodies from 26 providers.
DR DNASU; 170472; -.
DR Ensembl; ENSMUST00000021097; ENSMUSP00000021097; ENSMUSG00000020752.
DR GeneID; 170472; -.
DR KEGG; mmu:170472; -.
DR UCSC; uc007mix.2; mouse.
DR CTD; 9400; -.
DR MGI; MGI:2156841; Recql5.
DR VEuPathDB; HostDB:ENSMUSG00000020752; -.
DR eggNOG; KOG0352; Eukaryota.
DR GeneTree; ENSGT00940000157800; -.
DR HOGENOM; CLU_001103_4_1_1; -.
DR InParanoid; Q8VID5; -.
DR OMA; QNITRFF; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q8VID5; -.
DR TreeFam; TF317614; -.
DR BRENDA; 3.6.4.12; 3474.
DR BioGRID-ORCS; 170472; 10 hits in 107 CRISPR screens.
DR ChiTaRS; Recql5; mouse.
DR PRO; PR:Q8VID5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VID5; protein.
DR Bgee; ENSMUSG00000020752; Expressed in granulocyte and 139 other tissues.
DR ExpressionAtlas; Q8VID5; baseline and differential.
DR Genevisible; Q8VID5; MM.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISO:MGI.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0072757; P:cellular response to camptothecin; IMP:MGI.
DR GO; GO:1901655; P:cellular response to ketone; IMP:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IMP:MGI.
DR GO; GO:0071417; P:cellular response to organonitrogen compound; IMP:MGI.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0051304; P:chromosome separation; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IGI:MGI.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010716; RECQ5.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF06959; RecQ5; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA repair;
KW DNA replication; Helicase; Hydrolase; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..982
FT /note="ATP-dependent DNA helicase Q5"
FT /id="PRO_0000423434"
FT DOMAIN 39..213
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 241..398
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 491..621
FT /note="Interaction with POLR2A"
FT /evidence="ECO:0000250"
FT REGION 653..726
FT /note="Interaction with RAD51"
FT /evidence="ECO:0000250"
FT REGION 675..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 157..160
FT /note="DEAH box"
FT COMPBIAS 726..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4ACP5"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94762"
FT MOD_RES 527
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 728
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:O94762"
FT CONFLICT 419
FT /note="K -> R (in Ref. 4; BAC33647)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="S -> C (in Ref. 4; BAC34479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 982 AA; 108246 MW; D2D7D28448AAE0C2 CRC64;
MSARPFSTPF DRERRVRSTL KKVFGFDSFK TPLQESATMA VVKGAEDVFV CMPTGAGKSL
CYQLPALLAS GITIVVSPLI ALIQDQVDHL LALKVQVSSL NSKLSVQERK ELLSDLERDK
PRTKLLYITP EMAASASFQP TLNSLVSRNL LSYLVVDEAH CVSQWGHDFR PDYLRLGALR
SRLAHAPCVA LTATATPQVQ EDVFAALHLK QPVASFKTPC FRANLFYDVQ FKELIPDVYG
NLRDFCLKAL GQKAENGSSS GCGIVYCRTR EACEQLAIEL SSRGVNAKAY HAGLKASDRT
QVQNEWMEEK VPVIVATISF GMGVDKANVR FVAHWNIAKS MAGYYQESGR AGRDGKPSWC
RLYYSRNDRD QVSFLIRKEL AKLQEKRGNK PSDKATLLAF DALVTFCEEV GCRHAAIAKY
FGDAPPACAK GCDYCQNPAA ITKKLDALER SSSWSKTCIG PSQGNGFDPE LYEGGRRGYG
GFSRYDEGSG GSGDEGRDEA HKREWNLFYQ KQMSLRKGKE PKIEEFTPPD EDCPLREASS
RKIPKLTVKA REHCLRLLEE ALISNHQAAG STHGADLQAK AVELEHETFR NAKMVNLYKA
SVLKKVAEIH KASKDGQLYD MESGTKSCGA AAEFSEPSDY DIPPTSHVYS LKPKRVGAGF
SKGPCSFQTA TELLGKSHSQ KQAPEAMLEG GQEPPGWVCD LQDEDRSKPH PGYQEKALGS
SVNCGDPSPE KKTKGSSQGS AKARASKKQQ LLATAARKDS QNITRFLCQR TESPPLPASV
PRSEDASPSC GDVPGKCTQE VGAQGHLVAV FQTEGPRERP STCSLRDQSF PEGQPSPLKE
TQAEKRPRPQ QGNPERRAQK RLRPSTKSSI LAEAKDSTLA SDRSTENKVA QEPCQLSASG
TSLREAADIV VRHLTPFYKE GRFISKDLFK GFARHLSHLL AQQLSPGRSV KEEAQSLIKQ
FFHNRARCES EADWHSLRGP QR
