RECQ1_MOUSE
ID RECQ1_MOUSE Reviewed; 648 AA.
AC Q9Z129; Q3TPI5; Q9Z128;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=ATP-dependent DNA helicase Q1 {ECO:0000250|UniProtKB:P46063};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P46063};
DE AltName: Full=DNA-dependent ATPase Q1;
DE AltName: Full=RecQ protein-like 1;
GN Name=Recql; Synonyms=Recql1;
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], ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Spermatocyte, and Testis;
RX PubMed=9838113; DOI=10.1016/s0167-4781(98)00208-5;
RA Wang W.-S., Seki M., Yamaoka T., Seki T., Tada S., Katada T., Fujimoto H.,
RA Enomoto T.;
RT "Cloning of two isoforms of mouse DNA helicase Q1/RecQL cDNA; alpha form is
RT expressed ubiquitously and beta form specifically in the testis.";
RL Biochim. Biophys. Acta 1443:198-202(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC STRAIN=C57BL/6J; TISSUE=Bone, and Spinal ganglion;
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 [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 PROTEIN SEQUENCE OF 186-196 AND 502-509, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 may play a role in the repair of DNA that
CC is damaged by ultraviolet light or other mutagens. Exhibits a
CC magnesium-dependent ATP-dependent DNA-helicase activity that unwinds
CC single- and double-stranded DNA in a 3'-5' direction.
CC {ECO:0000250|UniProtKB:P46063}.
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:P46063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P46063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dATP + H2O = dADP + H(+) + phosphate; Xref=Rhea:RHEA:51908,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57667, ChEBI:CHEBI:61404;
CC Evidence={ECO:0000250|UniProtKB:P46063};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51909;
CC Evidence={ECO:0000250|UniProtKB:P46063};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P46063};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P46063};
CC -!- SUBUNIT: Interacts with EXO1. Interacts with MLH1.
CC {ECO:0000250|UniProtKB:P46063}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46063}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q9Z129-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9Z129-2; Sequence=VSP_005567;
CC -!- TISSUE SPECIFICITY: [Isoform Alpha]: Expressed in all tissues examined.
CC {ECO:0000269|PubMed:9838113}.
CC -!- TISSUE SPECIFICITY: [Isoform Beta]: Only expressed in spermatocytes.
CC Expression increases at pachytene (17 days old) and decreases after
CC completion of meiosis II (7 weeks old). {ECO:0000269|PubMed:9838113}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AB017104; BAA75085.1; -; mRNA.
DR EMBL; AB017105; BAA75086.1; -; mRNA.
DR EMBL; AK137589; BAE23422.1; -; mRNA.
DR EMBL; AK164344; BAE37751.1; -; mRNA.
DR EMBL; CH466572; EDL10638.1; -; Genomic_DNA.
DR CCDS; CCDS39695.1; -. [Q9Z129-1]
DR CCDS; CCDS57465.1; -. [Q9Z129-2]
DR RefSeq; NP_001191836.1; NM_001204907.1. [Q9Z129-2]
DR RefSeq; NP_075529.2; NM_023042.3. [Q9Z129-1]
DR RefSeq; XP_017176957.1; XM_017321468.1. [Q9Z129-1]
DR RefSeq; XP_017176958.1; XM_017321469.1.
DR AlphaFoldDB; Q9Z129; -.
DR SMR; Q9Z129; -.
DR BioGRID; 202847; 5.
DR STRING; 10090.ENSMUSP00000107434; -.
DR iPTMnet; Q9Z129; -.
DR PhosphoSitePlus; Q9Z129; -.
DR EPD; Q9Z129; -.
DR MaxQB; Q9Z129; -.
DR PaxDb; Q9Z129; -.
DR PRIDE; Q9Z129; -.
DR ProteomicsDB; 255173; -. [Q9Z129-1]
DR ProteomicsDB; 255174; -. [Q9Z129-2]
DR Antibodypedia; 4055; 96 antibodies from 21 providers.
DR DNASU; 19691; -.
DR Ensembl; ENSMUST00000032370; ENSMUSP00000032370; ENSMUSG00000030243. [Q9Z129-2]
DR Ensembl; ENSMUST00000111803; ENSMUSP00000107434; ENSMUSG00000030243. [Q9Z129-1]
DR GeneID; 19691; -.
DR KEGG; mmu:19691; -.
DR UCSC; uc009epf.2; mouse. [Q9Z129-1]
DR CTD; 5965; -.
DR MGI; MGI:103021; Recql.
DR VEuPathDB; HostDB:ENSMUSG00000030243; -.
DR eggNOG; KOG0353; Eukaryota.
DR GeneTree; ENSGT00940000157013; -.
DR HOGENOM; CLU_001103_12_5_1; -.
DR InParanoid; Q9Z129; -.
DR OMA; FKLSTMV; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q9Z129; -.
DR TreeFam; TF323555; -.
DR BioGRID-ORCS; 19691; 3 hits in 111 CRISPR screens.
DR PRO; PR:Q9Z129; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9Z129; protein.
DR Bgee; ENSMUSG00000030243; Expressed in spermatid and 242 other tissues.
DR ExpressionAtlas; Q9Z129; baseline and differential.
DR Genevisible; Q9Z129; MM.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:1990814; F:DNA/DNA annealing activity; ISO:MGI.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Direct protein sequencing;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..648
FT /note="ATP-dependent DNA helicase Q1"
FT /id="PRO_0000205050"
FT DOMAIN 100..275
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 299..451
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 601..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..222
FT /note="DEVH box"
FT COMPBIAS 614..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 514
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46063"
FT MOD_RES 522
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46063"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46063"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46063"
FT VAR_SEQ 622..648
FT /note="NSQKSKSRLQPSGSKNAGAKKRKLDDA -> SHAADTAANV (in
FT isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_005567"
FT CONFLICT 216
FT /note="A -> V (in Ref. 1; BAA75085/BAA75086)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="A -> T (in Ref. 1; BAA75085/BAA75086)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="A -> P (in Ref. 1; BAA75085/BAA75086)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="L -> P (in Ref. 1; BAA75085/BAA75086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 72484 MW; DF84B5E9097BF3F3 CRC64;
MASVSALTEE LESVASELHA IDIQIQELTE RRQELLQRKS VLTGKIKQYL EDSSAEASSD
LDTSPAAWNK EDFPWFGKVK DVLQNVFKLQ KFRPLQLETI NVTMARKDIF LVMPTGGGKS
LCYQLPALCS DGFTLVICPL ISLMEDQLMV LKQLGISATM LNASSSKEHV KWVHAEMVNK
NSQLKLIYVT PEKIAKSKMF MSRLEKAYEA GRLTGAAVDE VHCCSQWGHD FRPDYKALGI
LKRQFPNASL MGLTATATNH VLKDVQKILC VGKCLTFTAS FNRPNLFYEV RQKPSSAEDF
TEDIVKLING RYKGQSGIIY CFSQKDSEQI TISLQKLGIH AGTYHANMEP EDKTKVHTQW
SANELQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ ESGRAGRDDS RADCILYYGF
GDIFRISSMV VMENVGQQKL YEMVSYCQNV SKCRRVLIAQ HFDEVWNADA CNKMCDNCCK
DVSFEKKNVT QHCRDLIKIL KQAEGLNEKL TPLKLIDAWM GKGAAKLRVA GVVAPALPRE
DLERIVAHAL LQQYLKEDYS FTAYATISYL KVGPRACLLS NEAHAVTMQV KKSAQSSVRG
ALSEARQVEQ VDSKGEEQSS GNSQKSKSRL QPSGSKNAGA KKRKLDDA
