RECQ5_RAT
ID RECQ5_RAT Reviewed; 973 AA.
AC D4ACP5;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=RecQ protein-like 5;
GN Name=Recql5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489 AND SER-492, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Interacts with
CC WRN; this interaction stimulates WRN helicase activity on DNA fork
CC duplexes. Interacts with MUS1; this interaction promotes MUS81-
CC dependent mitotic DNA synthesis. {ECO:0000250|UniProtKB:O94762}.
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; AABR06066170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473948; EDM06625.1; -; Genomic_DNA.
DR RefSeq; NP_001099323.1; NM_001105853.1.
DR AlphaFoldDB; D4ACP5; -.
DR SMR; D4ACP5; -.
DR STRING; 10116.ENSRNOP00000007246; -.
DR iPTMnet; D4ACP5; -.
DR PhosphoSitePlus; D4ACP5; -.
DR PaxDb; D4ACP5; -.
DR PeptideAtlas; D4ACP5; -.
DR PRIDE; D4ACP5; -.
DR Ensembl; ENSRNOT00000007246; ENSRNOP00000007246; ENSRNOG00000005107.
DR GeneID; 287834; -.
DR KEGG; rno:287834; -.
DR CTD; 9400; -.
DR RGD; 1310823; Recql5.
DR eggNOG; KOG0352; Eukaryota.
DR GeneTree; ENSGT00940000157800; -.
DR HOGENOM; CLU_001103_4_1_1; -.
DR InParanoid; D4ACP5; -.
DR OMA; QNITRFF; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; D4ACP5; -.
DR TreeFam; TF317614; -.
DR PRO; PR:D4ACP5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000005107; Expressed in thymus and 19 other tissues.
DR Genevisible; D4ACP5; RN.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISO:RGD.
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: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; ISO:RGD.
DR GO; GO:1901655; P:cellular response to ketone; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
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..973
FT /note="ATP-dependent DNA helicase Q5"
FT /id="PRO_0000423435"
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 518..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..726
FT /note="Interaction with RAD51"
FT /evidence="ECO:0000250"
FT REGION 679..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 157..160
FT /note="DEAH box"
FT COMPBIAS 729..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..882
FT /note="Polar 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:0007744|PubMed:22673903"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 527
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VID5"
FT MOD_RES 728
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:O94762"
SQ SEQUENCE 973 AA; 107222 MW; 9E1E4F02D7811A3A CRC64;
MSARPFSTPF DRERRVRSTL KKVFGFDSFK TPLQESAIMA VVKGDKDVFV CMPTGAGKSL
CYQLPAVLAK GITIVVSPLI ALIQDQVDHL LALKVQVSSL NSKLSVQERK ELLSDLERDK
PRTKLLYITP EMAASASFQP TLNSLLSRNL LSYLVVDEAH CVSQWGHDFR PDYLRLGALR
SRLAHAPCVA LTATATPQVQ EDVFAALHLK QPVASFKTPC FRANLFYDVQ FKELIPDVYG
NLRDFCLKAL GQKADNGSSS GCGIVYCRTR EACEQLAIEL SSRGVNAKAY HAGLKASERT
QVQNEWMEEK VPVIVATISF GMGVDKANVR FVAHWNIAKS MAGYYQESGR AGRDGKPSWC
RLYYSRNDRD QVSFLIRKEL AKLQEKRGNK PSDKATLLAF DALVTFCEEV GCRHAAIAKY
FGDAPPACAK GCDCCQSPAA IRKKLDALEH SSSWGKTCIG PSQGDGFDPE LYEGGRRGYG
GFSRYDEGSG GSGDEGRDEA HKREWNLFYQ RQMSLRKGKE AKPEEFTPPG EDCPLRDASS
RKIPKLTVKA REHCLRLLEE ALNSNHQAAG STHGADLQAK AVELEHETFR SAKMVNLYKA
SVLKKVAEIH KASKDGQLYD MESSTKSCGA IAELLEPSDY DIPPTSHLYS LKPKRVGAGF
SKGPCPFQTA TELLGKSQTE KLAPEAALES EQEPSGWVCD PQDGDRSKPC LGYQEEAPGS
RTNCGDPSPE KRTKGSSQGS AKARASKRQQ LLATAARKDS QSITRFLRQR TECPPPAASV
PSSEDASPCG DVPGKCTEEV GAQGHLVAVF QTECPRERLS TCSLEDQSLP KGQPSPLKET
QAEKRPRPQQ ESQEKRAQKR LRPSTNSSAL ASDPSTENRV AREPCQLSAP GISLKEAADI
VVRYLTPFYK EGRFISKDLF KGFARHLSHL LAQKLSPGRS VKEEAQSLIK QFFHNRARCE
SEADWHGLCG PQR
