ID HELQ_MOUSE Reviewed; 1069 AA.
AC Q2VPA6; Q2VPA7; Q640L4; Q8BWI5; Q8R4K9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 24-JAN-2024, entry version 134.
DE RecName: Full=Helicase POLQ-like {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q8TDG4};
DE AltName: Full=Mus308-like helicase {ECO:0000303|PubMed:11751861};
DE AltName: Full=POLQ-like helicase {ECO:0000303|PubMed:11751861};
GN Name=Helq {ECO:0000303|PubMed:24005329};
GN Synonyms=Hel308 {ECO:0000303|PubMed:11751861};
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 [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 3-1069 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-749 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [MRNA] OF 298-1069 (ISOFORM 3).
RC STRAIN=BALB/cJ;
RX PubMed=11751861; DOI=10.1074/jbc.m110271200;
RA Marini F., Wood R.D.;
RT "A human DNA helicase homologous to the DNA cross-link sensitivity protein
RT Mus308.";
RL J. Biol. Chem. 277:8716-8723(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and 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).
RN [5]
RP FUNCTION, INTERACTION WITH RAD51C, AND DISRUPTION PHENOTYPE.
RX PubMed=24005329; DOI=10.1038/nature12565;
RA Adelman C.A., Lolo R.L., Birkbak N.J., Murina O., Matsuzaki K., Horejsi Z.,
RA Parmar K., Borel V., Skehel J.M., Stamp G., D'Andrea A., Sartori A.A.,
RA Swanton C., Boulton S.J.;
RT "HELQ promotes RAD51 paralogue-dependent repair to avert germ cell loss and
RT tumorigenesis.";
RL Nature 502:381-384(2013).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24005041; DOI=10.1093/nar/gkt676;
RA Luebben S.W., Kawabata T., Akre M.K., Lee W.L., Johnson C.S.,
RA O'Sullivan M.G., Shima N.;
RT "Helq acts in parallel to Fancc to suppress replication-associated genome
RT instability.";
RL Nucleic Acids Res. 41:10283-10297(2013).
CC -!- FUNCTION: Single-stranded 3'-5' DNA helicase that plays a key role in
CC homology-driven double-strand break (DSB) repair (PubMed:24005329,
CC PubMed:24005041). Involved in different DSB repair mechanisms that are
CC guided by annealing of extensive stretches of complementary bases at
CC break ends, such as microhomology-mediated end-joining (MMEJ), single-
CC strand annealing (SSA) or synthesis-dependent strand annealing (SDSA)
CC (By similarity). Possesses both DNA unwinding and annealing activities
CC (By similarity). Forms a complex with RAD51, stimulating HELQ DNA
CC helicase activity and ability to unwing DNA (By similarity).
CC Efficiently unwinds substrates containing 3' overhangs or a D-loop (By
CC similarity). In contrast, interaction with the replication protein A
CC (RPA/RP-A) complex inhibits DNA unwinding by HELQ but strongly
CC stimulates DNA strand annealing (By similarity). Triggers displacement
CC of RPA from single-stranded DNA to facilitate annealing of
CC complementary sequences (By similarity). {ECO:0000250|UniProtKB:Q8TDG4,
CC ECO:0000269|PubMed:24005041, ECO:0000269|PubMed:24005329}.
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:Q8TDG4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q8TDG4};
CC -!- SUBUNIT: Hexamer (By similarity). Interacts with POLN (By similarity).
CC Interacts with RAD51B (By similarity). Interacts with RAD51C; promoting
CC association with the BCDX2 complex (PubMed:24005329). Interacts with
CC the replication protein A (RPA/RP-A) complex (By similarity). Interacts
CC with RAD51; stimulating HELQ DNA helicase activity and ability to
CC unwing DNA (By similarity). {ECO:0000250|UniProtKB:Q8TDG4,
CC ECO:0000269|PubMed:24005329}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TDG4}.
CC Chromosome {ECO:0000250|UniProtKB:Q8TDG4}. Note=Localizes to sites of
CC DNA damage; localizes to damaged replication forks.
CC {ECO:0000250|UniProtKB:Q8TDG4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2VPA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2VPA6-2; Sequence=VSP_032952;
CC Name=3;
CC IsoId=Q2VPA6-3; Sequence=VSP_032949, VSP_032950, VSP_032951;
CC -!- DISRUPTION PHENOTYPE: Mice display Fanconi anemia-like phenotypes,
CC characterized by subfertility, germ cell attrition, interstrand cross-
CC links (ICLs) sensitivity and cancer susceptibility.
CC {ECO:0000269|PubMed:24005041, ECO:0000269|PubMed:24005329}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC082601; AAH82601.1; -; mRNA.
DR EMBL; BC109169; AAI09170.1; -; mRNA.
DR EMBL; BC109170; AAI09171.2; -; mRNA.
DR EMBL; AK052427; BAC34984.1; -; mRNA.
DR EMBL; AF436846; AAL85275.1; -; mRNA.
DR CCDS; CCDS39184.1; -. [Q2VPA6-1]
DR RefSeq; NP_001074576.1; NM_001081107.1. [Q2VPA6-1]
DR AlphaFoldDB; Q2VPA6; -.
DR SMR; Q2VPA6; -.
DR BioGRID; 228629; 5.
DR STRING; 10090.ENSMUSP00000041599; -.
DR iPTMnet; Q2VPA6; -.
DR PhosphoSitePlus; Q2VPA6; -.
DR EPD; Q2VPA6; -.
DR MaxQB; Q2VPA6; -.
DR PaxDb; 10090-ENSMUSP00000041599; -.
DR ProteomicsDB; 269731; -. [Q2VPA6-1]
DR ProteomicsDB; 269732; -. [Q2VPA6-2]
DR ProteomicsDB; 269733; -. [Q2VPA6-3]
DR Pumba; Q2VPA6; -.
DR Antibodypedia; 25213; 78 antibodies from 16 providers.
DR Ensembl; ENSMUST00000044684.14; ENSMUSP00000041599.8; ENSMUSG00000035266.17. [Q2VPA6-1]
DR GeneID; 191578; -.
DR KEGG; mmu:191578; -.
DR UCSC; uc008yhz.1; mouse. [Q2VPA6-1]
DR UCSC; uc012dzs.1; mouse. [Q2VPA6-2]
DR AGR; MGI:2176740; -.
DR CTD; 113510; -.
DR MGI; MGI:2176740; Helq.
DR VEuPathDB; HostDB:ENSMUSG00000035266; -.
DR eggNOG; KOG0950; Eukaryota.
DR GeneTree; ENSGT00940000157350; -.
DR HOGENOM; CLU_006553_1_0_1; -.
DR InParanoid; Q2VPA6; -.
DR OMA; AGIVKFC; -.
DR OrthoDB; 208079at2759; -.
DR PhylomeDB; Q2VPA6; -.
DR TreeFam; TF105018; -.
DR BioGRID-ORCS; 191578; 18 hits in 112 CRISPR screens.
DR ChiTaRS; Helq; mouse.
DR PRO; PR:Q2VPA6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q2VPA6; Protein.
DR Bgee; ENSMUSG00000035266; Expressed in animal zygote and 165 other cell types or tissues.
DR ExpressionAtlas; Q2VPA6; baseline and differential.
DR Genevisible; Q2VPA6; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0017117; C:single-stranded DNA-dependent ATP-dependent DNA helicase complex; ISO:MGI.
DR GO; GO:0090734; C:site of DNA damage; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISO:MGI.
DR GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; ISS:UniProtKB.
DR GO; GO:0006259; P:DNA metabolic process; ISO:MGI.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
DR CDD; cd18026; DEXHc_POLQ-like; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.20; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR046931; HTH_61.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048960; POLQ-like_helical.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF12; HELICASE POLQ-LIKE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF20470; HTH_61; 1.
DR Pfam; PF21099; POLQ_helical; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromosome; DNA damage; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1069
FT /note="Helicase POLQ-like"
FT /id="PRO_0000329061"
FT DOMAIN 305..477
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 525..717
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 422..425
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 42..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 318..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 725..766
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11751861"
FT /id="VSP_032949"
FT VAR_SEQ 851..866
FT /note="FGQLSPTEQNVAALLG -> VTEQVSWAETSLDFVT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11751861"
FT /id="VSP_032950"
FT VAR_SEQ 867..1069
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11751861"
FT /id="VSP_032951"
FT VAR_SEQ 884..979
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032952"
FT CONFLICT 428
FT /note="G -> C (in Ref. 1; AAI09170)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="L -> Q (in Ref. 3; AAL85275)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="V -> A (in Ref. 3; AAL85275)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="A -> S (in Ref. 1; AAH82601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1069 AA; 119098 MW; 69E56935E9F65BCB CRC64;
MEDGCPRIRR RVSVRKRNRG NLENLRASPT PAELQPAEDT EDEAAAGSRR RKTGSPEHAQ
ENDSEEDMFG DYDSFTESSF LAHVDDLEQR YMQLPECGDR DADSGTKDLC SAGLKNNLRV
TTVINLTDPE TSEHGQKQSH LDVPAEPEPG SDLSFDVPSS QILYFENPQN SPEALGDPCT
KKTNGDPQKS SHEELVSSHT EQPEPNNDFS NVRAASESSR RKSLKDHLKS TMAGNARAQT
PAFPRSKHLR EALLSEEISV AKKAIESPSD DLGPFYSLPS KVRDLYVQLK GIKKLYDWQH
TCLTLRSVQE RKNLIYSLPT SGGKTLVAEI LMLQELLCRQ KDVLMILPYV AIVQEKISSL
SSFGIELGFF VEEYAGSKGR FPPIKRREKK SLYIATIEKA HSLVNALIET SRLSTLGLVV
VDELHMIGEG SRGAILEMTL AKVLYTSKTT QIIGMSATLN NVEDLQAFLK AEYYTSQFRP
VELKEFLKVN DTIYEVDSQA ADGMTFSRLL SYKYSEALKK MDPDRLVALV TEVIPNYSCL
VFCPSKKNCE NVAEMLCKFL SKDYLNHREK EKCEVIKSLR NIGNGKVCPV LKRTVPFGIA
YHHSGLTSEE RKLLEEAYST GVLCLLTCTS TLAAGVNLPA RRVILRAPYV ANTFLKRNQY
KQMVGRAGRA GIDTAGESIL LLQEKDKQQV LELISGPLET CCSHLVEEFT KGIQALFLSL
IGLKIAASLG DIYQFMSGTF FGVQQKILLK EKSLWEITVD ALEHLTEKGL LQKDSCGDNE
GLECHFRITK LGQASFKGAI DLAYCDTLYR DLKKGLEGLV LESLLHLIYL TTPYDLAAQS
EPDWMVYFKQ FGQLSPTEQN VAALLGVSES FIGKKAAGQA VRKKVDKNVV NRLYLSFVLY
SLLKETNVWS VSEKFNLPRG YIQNLLMGAA SFSSCVLHFC EELEEFWVYK ALLVELTKKL
TYCVKAELIP LMEVTGVLEG RAKQLYNAGY RSIMHLANAN PEVLVKTIDH LSRRQARQIV
SSAKMLLHEK AEALQGEAEE LLRLPADLPG LGGPSSERAG SHAGDVTLS
//
