RECQ4_MOUSE
ID RECQ4_MOUSE Reviewed; 1216 AA.
AC Q75NR7; Q76MT1; Q99PV9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ATP-dependent DNA helicase Q4;
DE EC=3.6.4.12;
DE AltName: Full=DNA helicase, RecQ-like type 4;
DE Short=RecQ4;
DE AltName: Full=RecQ protein-like 4;
GN Name=Recql4; Synonyms=Recq4;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [MRNA] OF 16-1115 (ISOFORM 2).
RX PubMed=11167012; DOI=10.1016/s0378-1119(00)00498-4;
RA Ohhata T., Araki R., Fukumura R., Kuroiwa A., Matsuda Y., Tatsumi K.,
RA Abe M.;
RT "Cloning, genomic structure and chromosomal localization of the gene
RT encoding mouse DNA helicase RecQ helicase protein-like 4.";
RL Gene 261:251-258(2000).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12915449; DOI=10.1093/hmg/ddg254;
RA Hoki Y., Araki R., Fujimori A., Ohhata T., Koseki H., Fukumura R.,
RA Nakamura M., Takahashi H., Noda Y., Kito S., Abe M.;
RT "Growth retardation and skin abnormalities of the Recql4-deficient mouse.";
RL Hum. Mol. Genet. 12:2293-2299(2003).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=12952869; DOI=10.1093/hmg/ddg306;
RA Siitonen H.A., Kopra O., Kaeaeriaeinen H., Haravuori H., Winter R.M.,
RA Saeaemaenen A.-M., Peltonen L., Kestilae M.;
RT "Molecular defect of RAPADILINO syndrome expands the phenotype spectrum of
RT RECQL diseases.";
RL Hum. Mol. Genet. 12:2837-2844(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15703196; DOI=10.1093/hmg/ddi075;
RA Mann M.B., Hodges C.A., Barnes E., Vogel H., Hassold T.J., Luo G.;
RT "Defective sister-chromatid cohesion, aneuploidy and cancer predisposition
RT in a mouse model of type II Rothmund-Thomson syndrome.";
RL Hum. Mol. Genet. 14:813-825(2005).
CC -!- FUNCTION: DNA-dependent ATPase (By similarity). May play a role in
CC development of the palate and the limbs. May modulate chromosome
CC segregation. {ECO:0000250, ECO:0000269|PubMed:12915449,
CC ECO:0000269|PubMed:15703196}.
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 -!- SUBUNIT: Interacts with UBR1 and UBR2. Interacts with MCM10; this
CC interaction regulates RECQL4 unwinding activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O94761}. Nucleus
CC {ECO:0000250|UniProtKB:O94761}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q75NR7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q75NR7-2; Sequence=VSP_015177;
CC -!- DEVELOPMENTAL STAGE: Not expressed at 12.5 dpc. Expressed at 15.5 dpc-
CC 18.5 dpc, with highest levels in chondrocytes of developing bone and
CC cartilage and immature proliferating enterocytes of intestine.
CC {ECO:0000269|PubMed:12952869}.
CC -!- DISRUPTION PHENOTYPE: Early embryonic lethality. Transgenic mice with
CC exon 13-deleted RECQL4 are severely growth-retarded and show high (95%)
CC perinatal lethality. They exhibit various skin, bone, intestine, tooth
CC and thymus abnormalities and premature aging features, but have normal
CC sensitivity to IR and UV irradiation. In contrast, transgenic mice
CC expressing a truncated form of RECQL4 exhibit mild perinatal lethality,
CC no growth defect, but show defects of the skin and skeleton, aneuploidy
CC and increased cancer susceptibility. {ECO:0000269|PubMed:12915449,
CC ECO:0000269|PubMed:15703196}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AB039882; BAD11131.1; -; mRNA.
DR EMBL; AB175741; BAD14289.1; -; mRNA.
DR EMBL; AB042529; BAB32696.1; -; Genomic_DNA.
DR CCDS; CCDS27588.1; -. [Q75NR7-1]
DR RefSeq; NP_478121.2; NM_058214.3.
DR AlphaFoldDB; Q75NR7; -.
DR SMR; Q75NR7; -.
DR BioGRID; 219759; 9.
DR IntAct; Q75NR7; 9.
DR STRING; 10090.ENSMUSP00000044363; -.
DR iPTMnet; Q75NR7; -.
DR PhosphoSitePlus; Q75NR7; -.
DR EPD; Q75NR7; -.
DR jPOST; Q75NR7; -.
DR MaxQB; Q75NR7; -.
DR PaxDb; Q75NR7; -.
DR PeptideAtlas; Q75NR7; -.
DR PRIDE; Q75NR7; -.
DR ProteomicsDB; 255278; -. [Q75NR7-1]
DR ProteomicsDB; 255279; -. [Q75NR7-2]
DR DNASU; 79456; -.
DR GeneID; 79456; -.
DR KEGG; mmu:79456; -.
DR UCSC; uc007wlv.2; mouse. [Q75NR7-2]
DR CTD; 9401; -.
DR MGI; MGI:1931028; Recql4.
DR eggNOG; KOG0351; Eukaryota.
DR InParanoid; Q75NR7; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; Q75NR7; -.
DR TreeFam; TF324150; -.
DR BRENDA; 3.6.4.12; 3474.
DR BioGRID-ORCS; 79456; 23 hits in 111 CRISPR screens.
DR ChiTaRS; Recql4; mouse.
DR PRO; PR:Q75NR7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q75NR7; protein.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000405; F:bubble DNA binding; 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:0032357; F:oxidized purine DNA binding; ISO:MGI.
DR GO; GO:0061821; F:telomeric D-loop binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; ISO:MGI.
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:0045875; P:negative regulation of sister chromatid cohesion; IMP:MGI.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0000723; P:telomere maintenance; ISO:MGI.
DR GO; GO:0061820; P:telomeric D-loop disassembly; ISO:MGI.
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; IPR021110; DNA_rep_checkpnt_protein.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF11719; Drc1-Sld2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1216
FT /note="ATP-dependent DNA helicase Q4"
FT /id="PRO_0000205054"
FT DOMAIN 506..684
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 705..872
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 393..410
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 72..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 627..630
FT /note="DEAH box"
FT COMPBIAS 83..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 519..526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94761"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94761"
FT VAR_SEQ 843
FT /note="Q -> QVGSPISPDQDRPRGSTIPRPLQPQLLSCLPVSCRPGPKCGSSVHMT
FT VPMQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11167012"
FT /id="VSP_015177"
FT CONFLICT 732..739
FT /note="ERIQNGWL -> RKDTERVA (in Ref. 1; BAD14289)"
FT /evidence="ECO:0000305"
FT CONFLICT 878
FT /note="S -> G (in Ref. 1; BAD11131)"
FT /evidence="ECO:0000305"
FT CONFLICT 929
FT /note="I -> T (in Ref. 1; BAD11131)"
FT /evidence="ECO:0000305"
FT CONFLICT 937
FT /note="E -> TK (in Ref. 1; BAD11131)"
FT /evidence="ECO:0000305"
FT CONFLICT 1111
FT /note="T -> D (in Ref. 1; BAD11131)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1216 AA; 135124 MW; 431D79E43BAEC2AF CRC64;
MERLATVRAR LQEWERAFAR LHGRRPAKGD VEAAPEETRA LYREYRNLKQ AVRQADDRHR
VLEQSLAEAA EEAQEPSCWG PHLSRAATQN TQSMPKQSLL SSVQDYGKRL KANLKNTTQT
GPTQSRKLQL QKRSLSTVPA PRPPGSKTES PCPDEADDAL PRVPEPRPRL GQLQQLRSSL
SRRLTSLDPG WLERCHNRVS DLLEVPGACG LDLSAEESQP QMSGKVNIAD PDIQSEVSVQ
SPEAIAQQPA QVLSQSPKSI NSKGRKRKWN EKGEDFAQDQ PSSGAGPLSE GARATVHGQD
PPGEPTQVNV PQPCNSSNQA RTEKAKGTTH LHASPRPASL DRGNYIRLNM KNKRFVRVGA
NRGRLLRKQV WKQKWKKKQA AFGGSGPRAT DKDTCFRCGQ FGHWASQCSQ PGPTLTVQEE
GDRDDKQPIS TLEEVAQRTG TASCHHSGEE TQPAAPELQV PHCPTPMSPL YPPGPLGQVA
ETPAEVFQAL ERLGYRAFRP GQERAIMRIL SGISTLLVLP TGAGKSLCYQ LPALLYAQRS
PCLTLVVSPL LSLMDDQVSD LPSCLKAACL HSGMTKKQRE SVLKKVRAAQ VHVLIVSPEA
LVGCGARGPG SLPQAAQLPP IAFACIDEVH CLSQWSHNFR PCYLRVCKVL REHMGVRCFL
GLTATATRST ARDVAQHLGI AGEFELSGSA NIPANLHLSV SMDRDSDQAL VTLLQGDRFR
TLDSVIIYCT RERIQNGWLA LLRTCLSMVG DSRPRGCGPE AIAEAYHAGM SSQERRRVQQ
AFMRGHLRMV VATVAFGMGL DRPDVRAVLH LGLPPSFESY VQAIGRAGRD GKPAHCHLFM
HPQGEDLWEL RRHAHADSTD FLAVKRLVQR VFPPCTCSQR PVSKSSPEEV KEHSGQQTYP
VLGQACLGHE RALPVQSTVQ ALDMTEEAIE TLLCYLELHP RHWLELLPWT YAQCHLHCLG
GSAQLQALAH RCPPLAACQA KWPPKDTSQG RSSLEFGVVE LADSMGWKLA SVRQALHQLK
WDPEPKKGAA QGTGVLVKFS ELAFHLHSRG DLTDEEKDQI CDFLYNRVQA REHKALAHLH
QMSKAFRSVA FPSCGPCLEQ SNEEHSNQVK TLVSYYFEEE EEEEETMTDT QGPKPGQTQL
QDWEDQIRRD VRQLLSLRPE ERFSGRAVAR IFHGIASPCY PAQVYGLDRR FWRKYLHLDF
HALMHLATEE LLLRGR
