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   27-MAR-2024, entry version 189.
DE   RecName: Full=ATP-dependent DNA helicase Q1 {ECO:0000250|UniProtKB:P46063};
DE            EC=5.6.2.4 {ECO:0000250|UniProtKB:P46063};
DE   AltName: Full=DNA 3'-5' helicase Q1 {ECO:0000305};
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 plays a role in DNA damage repair and
CC       genome stability (By similarity). Exhibits a magnesium- and ATP-
CC       dependent DNA-helicase activity that unwinds single- and double-
CC       stranded DNA in a 3'-5' direction (By similarity). Plays a role in
CC       restoring regressed replication forks (By similarity). Required to
CC       restart stalled replication forks induced by abortive topoisomerase 1
CC       and 2 lesions (By similarity). May play a role in the repair of DNA
CC       that is damaged by ultraviolet light or other mutagens (By similarity).
CC       {ECO:0000250|UniProtKB:P46063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={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;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P46063};
CC       Note=Binds 1 Zn(2+) per monomer. {ECO:0000250|UniProtKB:P46063};
CC   -!- SUBUNIT: May form homodimers or higher order oligomers (By similarity).
CC       Interacts with EXO1. Interacts with MLH1. Interacts with PARP1 (By
CC       similarity). {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.
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; 10090-ENSMUSP00000107434; -.
DR   ProteomicsDB; 255173; -. [Q9Z129-1]
DR   ProteomicsDB; 255174; -. [Q9Z129-2]
DR   Pumba; Q9Z129; -.
DR   Antibodypedia; 4055; 118 antibodies from 21 providers.
DR   DNASU; 19691; -.
DR   Ensembl; ENSMUST00000032370.13; ENSMUSP00000032370.7; ENSMUSG00000030243.17. [Q9Z129-2]
DR   Ensembl; ENSMUST00000111803.9; ENSMUSP00000107434.3; ENSMUSG00000030243.17. [Q9Z129-1]
DR   GeneID; 19691; -.
DR   KEGG; mmu:19691; -.
DR   UCSC; uc009epf.2; mouse. [Q9Z129-1]
DR   AGR; MGI:103021; -.
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; 5474026at2759; -.
DR   PhylomeDB; Q9Z129; -.
DR   TreeFam; TF323555; -.
DR   BioGRID-ORCS; 19691; 3 hits in 116 CRISPR screens.
DR   PRO; PR:Q9Z129; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9Z129; Protein.
DR   Bgee; ENSMUSG00000030243; Expressed in spermatid and 245 other cell types or tissues.
DR   ExpressionAtlas; Q9Z129; baseline and differential.
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:0005634; C:nucleus; ISS:UniProtKB.
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:0036121; F:double-stranded DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0009378; F:four-way junction helicase activity; 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   GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR   CDD; cd18015; DEXHc_RecQ1; 1.
DR   CDD; cd18794; SF2_C_RecQ; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF72; ATP-DEPENDENT DNA HELICASE Q1; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   Genevisible; Q9Z129; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Direct protein sequencing;
KW   DNA-binding; Helicase; Hydrolase; Isomerase; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc.
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   BINDING         453
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P46063"
FT   BINDING         471
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P46063"
FT   BINDING         475
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P46063"
FT   BINDING         478
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P46063"
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
//