ID CHD1L_MOUSE Reviewed; 900 AA.
AC Q9CXF7; Q3TMX1; Q6P5C0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1-like;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:Q86WJ1};
GN Name=Chd1l;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, 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).
CC -!- FUNCTION: ATP-dependent chromatin remodeler that mediates chromatin-
CC remodeling following DNA damage. Recruited to DNA damage sites through
CC interaction with poly-ADP-ribose: specifically recognizes and binds
CC histones that are poly-ADP-ribosylated on serine residues in response
CC to DNA damage. Poly-ADP-ribose-binding activates the ATP-dependent
CC chromatin remodeler activity, thereby regulating chromatin during DNA
CC repair. Catalyzes nucleosome sliding away from DNA breaks in an ATP-
CC dependent manner. Chromatin remodeling activity promotes PARP2 removal
CC from chromatin. {ECO:0000250|UniProtKB:Q86WJ1}.
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:Q86WJ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q86WJ1};
CC -!- ACTIVITY REGULATION: Adopts an inactive conformation in absence of DNA
CC damage. Binding to poly-ADP-ribosylated histones activates the ATP-
CC dependent chromatin remodeler activity. {ECO:0000250|UniProtKB:Q86WJ1}.
CC -!- SUBUNIT: Interacts with nucleosomes; interacts with the acidic patch of
CC histones. Interacts (via macro domain) with PARP1; interacts only when
CC PARP1 is poly-ADP-ribosylated (PARylated). Interacts with CIAO1.
CC {ECO:0000250|UniProtKB:Q86WJ1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86WJ1}.
CC Chromosome {ECO:0000250|UniProtKB:Q86WJ1}. Note=Localizes at sites of
CC DNA damage; recruited by histones H2B and H3 poly-ADP-ribosylated on
CC 'Ser-6' and 'Ser-10', respectively (H2BS6ADPr and H3S10ADPr) by PARP1
CC or PARP2. {ECO:0000250|UniProtKB:Q86WJ1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CXF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CXF7-2; Sequence=VSP_033343;
CC -!- DOMAIN: The macro domain mediates non-covalent poly(ADP-ribose)-binding
CC and recruitment to DNA damage sites. Mediates auto-inhibition of ATPase
CC activity by interacting with the N-terminal ATPase module, encompassing
CC the helicase ATP-binding domain and helicase C-terminal domain. Binding
CC to poly-ADP-ribosylated histones upon DNA damage releases the auto-
CC inhibition by the macro domain and trigger ATPase activity. Does not
CC bind monomeric ADP-ribose and mono-ADP-ribose fails to release the
CC auto-inhibition of the ATPase module by the macro domain.
CC {ECO:0000250|UniProtKB:Q86WJ1}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AK014473; BAB29376.1; -; mRNA.
DR EMBL; AK165656; BAE38319.1; -; mRNA.
DR EMBL; BC052385; AAH52385.1; -; mRNA.
DR EMBL; BC057567; AAH57567.1; -; mRNA.
DR EMBL; BC062966; AAH62966.1; -; mRNA.
DR CCDS; CCDS38561.1; -. [Q9CXF7-1]
DR RefSeq; NP_080815.1; NM_026539.2. [Q9CXF7-1]
DR AlphaFoldDB; Q9CXF7; -.
DR SMR; Q9CXF7; -.
DR BioGRID; 212634; 1.
DR DIP; DIP-58953N; -.
DR IntAct; Q9CXF7; 1.
DR STRING; 10090.ENSMUSP00000029730; -.
DR iPTMnet; Q9CXF7; -.
DR PhosphoSitePlus; Q9CXF7; -.
DR SwissPalm; Q9CXF7; -.
DR EPD; Q9CXF7; -.
DR jPOST; Q9CXF7; -.
DR MaxQB; Q9CXF7; -.
DR PaxDb; 10090-ENSMUSP00000029730; -.
DR PeptideAtlas; Q9CXF7; -.
DR ProteomicsDB; 283825; -. [Q9CXF7-1]
DR ProteomicsDB; 283826; -. [Q9CXF7-2]
DR Pumba; Q9CXF7; -.
DR Antibodypedia; 20241; 236 antibodies from 30 providers.
DR DNASU; 68058; -.
DR Ensembl; ENSMUST00000029730.5; ENSMUSP00000029730.5; ENSMUSG00000028089.6. [Q9CXF7-1]
DR GeneID; 68058; -.
DR KEGG; mmu:68058; -.
DR UCSC; uc008qow.1; mouse. [Q9CXF7-1]
DR UCSC; uc008qox.1; mouse. [Q9CXF7-2]
DR AGR; MGI:1915308; -.
DR CTD; 9557; -.
DR MGI; MGI:1915308; Chd1l.
DR VEuPathDB; HostDB:ENSMUSG00000028089; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000159402; -.
DR HOGENOM; CLU_000315_17_9_1; -.
DR InParanoid; Q9CXF7; -.
DR OMA; FIVHCVD; -.
DR OrthoDB; 5482994at2759; -.
DR PhylomeDB; Q9CXF7; -.
DR TreeFam; TF333326; -.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR BioGRID-ORCS; 68058; 7 hits in 116 CRISPR screens.
DR ChiTaRS; Chd1l; mouse.
DR PRO; PR:Q9CXF7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CXF7; Protein.
DR Bgee; ENSMUSG00000028089; Expressed in saccule of membranous labyrinth and 239 other cell types or tissues.
DR Genevisible; Q9CXF7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0090734; C:site of DNA damage; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0140566; F:histone reader activity; ISS:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB.
DR GO; GO:0160004; F:poly-ADP-D-ribose modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISO:MGI.
DR CDD; cd18006; DEXHc_CHD1L; 1.
DR CDD; cd03331; Macro_Poa1p-like_SNF2; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR031053; ALC1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR47157; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1-LIKE; 1.
DR PANTHER; PTHR47157:SF1; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1-LIKE; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52949; Macro domain-like; 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 PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromosome; Coiled coil; DNA damage;
KW DNA repair; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..900
FT /note="Chromodomain-helicase-DNA-binding protein 1-like"
FT /id="PRO_0000332142"
FT DOMAIN 52..217
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 345..507
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 709..900
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT REGION 546..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..640
FT /note="Regulatory linker segment (RLS)"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT REGION 620..678
FT /note="Required for ATPase activity"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT REGION 641..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..680
FT /evidence="ECO:0000255"
FT MOTIF 168..171
FT /note="DEAH box"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT VAR_SEQ 877..900
FT /note="IYYFPRSKARHSQPASSSSAPLVP -> MYPSVV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033343"
FT CONFLICT 300
FT /note="A -> S (in Ref. 2; AAH62966/AAH57567)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="G -> GG (in Ref. 1; BAE38319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 900 AA; 101438 MW; 89FEE484E71BBE09 CRC64;
MASGLPRFLQ ALPAEHGPEP LRTRVQEPDL QQWGLTGIRL RSYQLEGVNW LVQCFHCQNG
CILGDEMGLG KTCQTIALLI YLVGRLNDEG PFLVLCPLSV LSNWKEEMER FAPGLSCVTY
TGDKEERARL QQDLRQESGF HVLLTTYEIC LKDASFLKSF SWSVLAVDEA HRLKNQSSLL
HRTLSEFSAV FRLLLTGTPI QNSLRELYSL LCVVEPDLFC REQVEDFVQR YQDIEKESKS
ASELHRLLQP FLLRRVKAQV ATELPKKTEV VVYHGMSALQ KKYYKAILMK DLDAFENETA
KKVKLQNILT QLRKCVDHPY LFDGVEPEPF EVGEHLIEAS GKLHLLDRLL AFLYSGGHRV
LLFSQMTHML DILQDYMDYR GYSYERVDGS VRGEERHLAI KNFGNQPIFV FLLSTRAGGV
GMNLTAADTV IFVDSDFNPQ NDLQAAARAH RIGQNKSVKV IRLIGRDTVE EIVYRKAASK
LQLTNMVIEG GHFTPGAQKP SAEADFQLSE ILKFGLDKLL SSEGSSMEDI DLKSILGETK
DGQWTPDALP AAAAAGGGSL EPEEGSELES RSYENHMYLF EGRDYSKEPS KEDRKSFEQL
VNLQKTLLEK TSHGGRTLRN KGSVLIPGLA EGPIKRKKIL SPEELEDRRK KRQEAAAKRK
RLMEEKRKEK EEAEHRKKMA WWESNGYQSF CLSSEDSELE DLEGGDESSA ELAYEDLDST
SINYVSGDVT HPQAGEEDAV IVHCVDDSGR WGRGGLFTAL EVRSAEPRKI YELAGKMEDL
SLGDVLLFPI DDKESRDKGQ DLLALVVAQH RDRTNVLSGI KMAALEEGLK KIFLAAKKKK
ASVHLPRIGH ATKGFNWYGT ERLIRKHLAT RGIPTYIYYF PRSKARHSQP ASSSSAPLVP
//
