ID CHD1L_HUMAN Reviewed; 897 AA. AC Q86WJ1; A5YM64; B4DDE1; B5MDZ7; Q53EZ3; Q5VXX7; Q6DD94; Q6PK83; Q86XH3; AC Q96HF7; Q96SP3; Q9BVJ1; Q9NVV8; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 12-SEP-2018, sequence version 3. DT 27-MAR-2024, entry version 172. DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1-like {ECO:0000305}; DE EC=3.6.4.- {ECO:0000269|PubMed:29220652, ECO:0000269|PubMed:29220653, ECO:0000269|PubMed:34486521}; DE AltName: Full=Amplified in liver cancer protein 1 {ECO:0000303|PubMed:18023026}; GN Name=CHD1L {ECO:0000303|PubMed:34210977, ECO:0000312|HGNC:HGNC:1916}; GN Synonyms=ALC1 {ECO:0000303|PubMed:18023026}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=18023026; DOI=10.1002/hep.22072; RA Ma N.-F., Hu L., Fung J.-M., Xie D., Zheng B.-J., Chen L., Tang D.-J., RA Fu L., Wu Z., Chen M., Fang Y., Guan X.-Y.; RT "Isolation and characterization of a novel oncogene, amplified in liver RT cancer 1, within a commonly amplified region at 1q21 in hepatocellular RT carcinoma."; RL Hepatology 47:503-510(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5), AND VARIANT RP CYS-743. RC TISSUE=Neuron; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-350. RC TISSUE=Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-885. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 2-897 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE RP MRNA] OF 15-897 (ISOFORM 2), AND VARIANTS PRO-25 AND CYS-743. RC TISSUE=Brain, Eye, Prostate, and Skin; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-798. RC TISSUE=Hepatocyte; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-891, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN MACRO, ADP-RIBOSE-BINDING, RP INTERACTION WITH PARP1, AND MUTAGENESIS OF LYS-77 AND ASP-723. RX PubMed=19661379; DOI=10.1126/science.1177321; RA Ahel D., Horejsi Z., Wiechens N., Polo S.E., Garcia-Wilson E., Ahel I., RA Flynn H., Skehel M., West S.C., Jackson S.P., Owen-Hughes T., Boulton S.J.; RT "Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin RT remodeling enzyme ALC1."; RL Science 325:1240-1243(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607; SER-618; SER-628 AND RP SER-636, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-9, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP INTERACTION WITH CIAO1. RX PubMed=23891004; DOI=10.1016/j.cmet.2013.06.015; RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B., RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.; RT "Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and RT maturation of different subsets of cytosolic-nuclear iron-sulfur RT proteins."; RL Cell Metab. 18:187-198(2013). RN [15] RP ERRATUM OF PUBMED:23891004. RX PubMed=29320706; DOI=10.1016/j.cmet.2017.12.009; RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B., RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.; RT "Human CIA2A-FAM96A and CIA2B-FAM96B Integrate Iron Homeostasis and RT Maturation of Different Subsets of Cytosolic-Nuclear Iron-Sulfur RT Proteins."; RL Cell Metab. 27:263-263(2018). RN [16] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DOMAIN MACRO, RP ADP-RIBOSE-BINDING, VARIANTS GLN-857 AND TRP-860, CHARACTERIZATION OF RP VARIANTS GLN-857 AND TRP-860, AND MUTAGENESIS OF ARG-857. RX PubMed=29220652; DOI=10.1016/j.molcel.2017.10.017; RA Lehmann L.C., Hewitt G., Aibara S., Leitner A., Marklund E., Maslen S.L., RA Maturi V., Chen Y., van der Spoel D., Skehel J.M., Moustakas A., RA Boulton S.J., Deindl S.; RT "Mechanistic insights into autoinhibition of the oncogenic chromatin RT remodeler ALC1."; RL Mol. Cell 68:847-847(2017). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PARP1, DOMAIN MACRO, RP ADP-RIBOSE-BINDING, MUTAGENESIS OF GLU-175; 307-LYS-LYS-308; RP 319-ARG-LYS-320; 332-GLU--GLU-337; ARG-398; LYS-407; SER-420; ARG-422; RP 653-LYS--ARG-656; GLY-750 AND ARG-842, VARIANTS HIS-842; GLN-857 AND RP TRP-860, AND CHARACTERIZATION OF VARIANTS HIS-842; GLN-857 AND TRP-860. RX PubMed=29220653; DOI=10.1016/j.molcel.2017.11.019; RA Singh H.R., Nardozza A.P., Moeller I.R., Knobloch G., Kistemaker H.A.V., RA Hassler M., Harrer N., Blessing C., Eustermann S., Kotthoff C., Huet S., RA Mueller-Planitz F., Filippov D.V., Timinszky G., Rand K.D., Ladurner A.G.; RT "A Poly-ADP-Ribose trigger releases the auto-inhibition of a chromatin RT remodeling oncogene."; RL Mol. Cell 68:860-871(2017). RN [18] RP FUNCTION, AND MUTAGENESIS OF GLU-175. RX PubMed=33275888; DOI=10.1016/j.molcel.2020.10.009; RA Blessing C., Mandemaker I.K., Gonzalez-Leal C., Preisser J., Schomburg A., RA Ladurner A.G.; RT "The oncogenic helicase ALC1 regulates PARP inhibitor potency by trapping RT PARP2 at DNA breaks."; RL Mol. Cell 80:862-875(2020). RN [19] RP FUNCTION, ACTIVITY REGULATION, AND DOMAIN. RX PubMed=34874266; DOI=10.7554/elife.71502; RA Mohapatra J., Tashiro K., Beckner R.L., Sierra J., Kilgore J.A., RA Williams N.S., Liszczak G.; RT "Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin RT remodeling."; RL Elife 10:0-0(2021). RN [20] RP FUNCTION. RX PubMed=34465625; DOI=10.1073/pnas.2107277118; RA Ooi S.K., Sato S., Tomomori-Sato C., Zhang Y., Wen Z., Banks C.A.S., RA Washburn M.P., Unruh J.R., Florens L., Conaway R.C., Conaway J.W.; RT "Multiple roles for PARP1 in ALC1-dependent nucleosome remodeling."; RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021). RN [21] {ECO:0007744|PDB:6ZHX, ECO:0007744|PDB:6ZHY} RP STRUCTURE BY ELECTRON MICROSCOPY (2.50 ANGSTROMS) OF 604-639 IN COMPLEX RP WITH NUCLEOSOME CORE COMPLEX, FUNCTION, ACTIVITY REGULATION, INTERACTION RP WITH NUCLEOSOMES, AND MUTAGENESIS OF 611-ARG-SER-612. RX PubMed=33357431; DOI=10.1016/j.celrep.2020.108529; RA Lehmann L.C., Bacic L., Hewitt G., Brackmann K., Sabantsev A., Gaullier G., RA Pytharopoulou S., Degliesposti G., Okkenhaug H., Tan S., Costa A., RA Skehel J.M., Boulton S.J., Deindl S.; RT "Mechanistic insights into regulation of the ALC1 remodeler by the RT nucleosome acidic patch."; RL Cell Rep. 33:108529-108529(2020). RN [22] {ECO:0007744|PDB:7ENN, ECO:0007744|PDB:7EPU} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH RP NUCLEOSOME CORE COMPLEX, FUNCTION, INTERACTION WITH NUCLEOSOMES, RP MUTAGENESIS OF ASP-381; ARG-457; ARG-611 AND ARG-614, VARIANT CYS-852, AND RP CHARACTERIZATION OF VARIANT CYS-852. RX PubMed=34210977; DOI=10.1038/s41467-021-24320-4; RA Wang L., Chen K., Chen Z.; RT "Structural basis of ALC1/CHD1L autoinhibition and the mechanism of RT activation by the nucleosome."; RL Nat. Commun. 12:4057-4057(2021). RN [23] {ECO:0007744|PDB:7OTQ} RP STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS) OF 16-879 IN COMPLEX WITH RP NUCLEOSOME CORE COMPLEX, FUNCTION, ACTIVITY REGULATION, INTERACTION WITH RP NUCLEOSOMES, DOMAIN, AND MUTAGENESIS OF 611-ARG-SER-612. RX PubMed=34486521; DOI=10.7554/elife.71420; RA Bacic L., Gaullier G., Sabantsev A., Lehmann L.C., Brackmann K., RA Dimakou D., Halic M., Hewitt G., Boulton S.J., Deindl S.; RT "Structure and dynamics of the chromatin remodeler ALC1 bound to a RT PARylated nucleosome."; RL Elife 10:0-0(2021). CC -!- FUNCTION: ATP-dependent chromatin remodeler that mediates chromatin- CC remodeling following DNA damage (PubMed:19661379, PubMed:29220652, CC PubMed:29220653, PubMed:33357431, PubMed:34486521, PubMed:34874266, CC PubMed:34210977). Recruited to DNA damage sites through interaction CC with poly-ADP-ribose: specifically recognizes and binds histones that CC are poly-ADP-ribosylated on serine residues in response to DNA damage CC (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:34874266, CC PubMed:34486521). Poly-ADP-ribose-binding activates the ATP-dependent CC chromatin remodeler activity, thereby regulating chromatin during DNA CC repair (PubMed:19661379, PubMed:29220652, PubMed:29220653, CC PubMed:34874266, PubMed:34486521). Catalyzes nucleosome sliding away CC from DNA breaks in an ATP-dependent manner (PubMed:19661379, CC PubMed:29220652, PubMed:29220653). Chromatin remodeling activity CC promotes PARP2 removal from chromatin (PubMed:33275888). CC {ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:29220652, CC ECO:0000269|PubMed:29220653, ECO:0000269|PubMed:33275888, CC ECO:0000269|PubMed:33357431, ECO:0000269|PubMed:34210977, CC ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}. 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:0000269|PubMed:29220652, ECO:0000269|PubMed:29220653, CC ECO:0000269|PubMed:34486521}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; CC Evidence={ECO:0000269|PubMed:29220652, ECO:0000269|PubMed:29220653, CC ECO:0000269|PubMed:34486521}; CC -!- ACTIVITY REGULATION: Adopts an inactive conformation in absence of DNA CC damage (PubMed:33357431, PubMed:34486521, PubMed:34874266). Binding to CC poly-ADP-ribosylated histones activates the ATP-dependent chromatin CC remodeler activity (PubMed:34486521, PubMed:34874266). CC {ECO:0000269|PubMed:33357431, ECO:0000269|PubMed:34486521, CC ECO:0000269|PubMed:34874266}. CC -!- SUBUNIT: Interacts with nucleosomes; interacts with the acidic patch of CC histones (PubMed:34486521, PubMed:33357431, PubMed:34210977). Interacts CC (via macro domain) with PARP1; interacts only when PARP1 is poly-ADP- CC ribosylated (PARylated) (PubMed:19661379, PubMed:29220653). Interacts CC with CIAO1 (PubMed:23891004). {ECO:0000269|PubMed:19661379, CC ECO:0000269|PubMed:23891004, ECO:0000269|PubMed:29220653, CC ECO:0000269|PubMed:33357431, ECO:0000269|PubMed:34210977, CC ECO:0000269|PubMed:34486521}. CC -!- INTERACTION: CC Q86WJ1-1; P09874: PARP1; NbExp=3; IntAct=EBI-15797018, EBI-355676; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19661379}. Chromosome CC {ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:29220652, CC ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}. CC Note=Localizes at sites of DNA damage; recruited by histones H2B and H3 CC poly-ADP-ribosylated on 'Ser-6' and 'Ser-10', respectively (H2BS6ADPr CC and H3S10ADPr) by PARP1 or PARP2. {ECO:0000269|PubMed:34486521, CC ECO:0000269|PubMed:34874266}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q86WJ1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86WJ1-2; Sequence=VSP_033342; CC Name=3; CC IsoId=Q86WJ1-3; Sequence=VSP_033341; CC Name=4; CC IsoId=Q86WJ1-4; Sequence=VSP_033340; CC Name=5; CC IsoId=Q86WJ1-5; Sequence=VSP_055675; CC -!- TISSUE SPECIFICITY: Frequently overexpressed in hepatomacellular CC carcinomas. {ECO:0000269|PubMed:18023026}. CC -!- DOMAIN: The macro domain mediates non-covalent poly(ADP-ribose)-binding CC and recruitment to DNA damage sites (PubMed:19661379, PubMed:29220652, CC PubMed:29220653). Mediates auto-inhibition of ATPase activity by CC interacting with the N-terminal ATPase module, encompassing the CC helicase ATP-binding domain and helicase C-terminal domain CC (PubMed:29220652, PubMed:29220653). Binding to poly-ADP-ribosylated CC histones upon DNA damage releases the auto-inhibition by the macro CC domain and trigger ATPase activity (PubMed:34486521, PubMed:34874266). CC Does not bind monomeric ADP-ribose and mono-ADP-ribose fails to release CC the auto-inhibition of the ATPase module by the macro domain CC (PubMed:29220653). {ECO:0000269|PubMed:19661379, CC ECO:0000269|PubMed:29220652, ECO:0000269|PubMed:29220653, CC ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}. CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB55248.1; Type=Frameshift; Evidence={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; AF537213; AAO49505.1; -; mRNA. DR EMBL; AK001342; BAA91637.1; -; mRNA. DR EMBL; AK027631; BAB55248.1; ALT_FRAME; mRNA. DR EMBL; AK293157; BAG56702.1; -; mRNA. DR EMBL; EF560738; ABQ59048.1; -; mRNA. DR EMBL; AC242426; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL356378; CAH72650.1; -; Genomic_DNA. DR EMBL; BC001171; AAH01171.1; -; mRNA. DR EMBL; BC005038; AAH05038.1; -; mRNA. DR EMBL; BC008649; AAH08649.1; -; mRNA. DR EMBL; BC043501; AAH43501.1; -; mRNA. DR EMBL; BC077717; AAH77717.1; -; mRNA. DR EMBL; AK223496; BAD97216.1; -; mRNA. DR CCDS; CCDS58021.1; -. [Q86WJ1-3] DR CCDS; CCDS927.1; -. [Q86WJ1-1] DR RefSeq; NP_001243266.1; NM_001256337.2. [Q86WJ1-5] DR RefSeq; NP_001243267.1; NM_001256338.2. [Q86WJ1-3] DR RefSeq; NP_001335382.1; NM_001348453.1. [Q86WJ1-4] DR RefSeq; NP_001335385.1; NM_001348456.1. [Q86WJ1-5] DR RefSeq; NP_001335386.1; NM_001348457.1. [Q86WJ1-5] DR RefSeq; NP_001335387.1; NM_001348458.1. [Q86WJ1-5] DR RefSeq; NP_001335388.1; NM_001348459.1. [Q86WJ1-5] DR RefSeq; NP_001335389.1; NM_001348460.1. [Q86WJ1-5] DR RefSeq; NP_001335390.1; NM_001348461.1. [Q86WJ1-5] DR RefSeq; NP_001335391.1; NM_001348462.1. [Q86WJ1-5] DR RefSeq; NP_001335392.1; NM_001348463.1. [Q86WJ1-5] DR RefSeq; NP_001335393.1; NM_001348464.1. [Q86WJ1-5] DR RefSeq; NP_001335394.1; NM_001348465.1. [Q86WJ1-5] DR RefSeq; NP_001335395.1; NM_001348466.1. [Q86WJ1-5] DR RefSeq; NP_004275.4; NM_004284.5. [Q86WJ1-1] DR RefSeq; NP_078844.2; NM_024568.3. [Q86WJ1-4] DR PDB; 6ZHX; EM; 2.50 A; K/L=604-639. DR PDB; 6ZHY; EM; 3.00 A; K=604-639. DR PDB; 7ENN; EM; 2.80 A; K=1-897. DR PDB; 7EPU; X-ray; 3.50 A; B=1-880. DR PDB; 7OTQ; EM; 4.80 A; K=16-879. DR PDB; 8B0A; EM; 3.00 A; K=16-879. DR PDBsum; 6ZHX; -. DR PDBsum; 6ZHY; -. DR PDBsum; 7ENN; -. DR PDBsum; 7EPU; -. DR PDBsum; 7OTQ; -. DR PDBsum; 8B0A; -. DR AlphaFoldDB; Q86WJ1; -. DR EMDB; EMD-11220; -. DR EMDB; EMD-11221; -. DR EMDB; EMD-13065; -. DR EMDB; EMD-13070; -. DR EMDB; EMD-15777; -. DR EMDB; EMD-31217; -. DR SMR; Q86WJ1; -. DR BioGRID; 114929; 105. DR DIP; DIP-48933N; -. DR IntAct; Q86WJ1; 49. DR MINT; Q86WJ1; -. DR STRING; 9606.ENSP00000358262; -. DR GlyCosmos; Q86WJ1; 1 site, 1 glycan. DR GlyGen; Q86WJ1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q86WJ1; -. DR PhosphoSitePlus; Q86WJ1; -. DR BioMuta; CHD1L; -. DR DMDM; 311033359; -. DR EPD; Q86WJ1; -. DR jPOST; Q86WJ1; -. DR MassIVE; Q86WJ1; -. DR MaxQB; Q86WJ1; -. DR PaxDb; 9606-ENSP00000358262; -. DR PeptideAtlas; Q86WJ1; -. DR ProteomicsDB; 6203; -. DR ProteomicsDB; 70174; -. [Q86WJ1-1] DR ProteomicsDB; 70175; -. [Q86WJ1-2] DR ProteomicsDB; 70176; -. [Q86WJ1-3] DR ProteomicsDB; 70177; -. [Q86WJ1-4] DR Pumba; Q86WJ1; -. DR ABCD; Q86WJ1; 1 sequenced antibody. DR Antibodypedia; 20241; 236 antibodies from 30 providers. DR DNASU; 9557; -. DR Ensembl; ENST00000369258.8; ENSP00000358262.4; ENSG00000131778.20. [Q86WJ1-1] DR Ensembl; ENST00000369259.4; ENSP00000358263.3; ENSG00000131778.20. [Q86WJ1-3] DR GeneID; 9557; -. DR KEGG; hsa:9557; -. DR MANE-Select; ENST00000369258.8; ENSP00000358262.4; NM_004284.6; NP_004275.4. DR UCSC; uc001epm.6; human. [Q86WJ1-1] DR AGR; HGNC:1916; -. DR DisGeNET; 9557; -. DR GeneCards; CHD1L; -. DR HGNC; HGNC:1916; CHD1L. DR HPA; ENSG00000131778; Low tissue specificity. DR MIM; 613039; gene. DR neXtProt; NX_Q86WJ1; -. DR OpenTargets; ENSG00000131778; -. DR PharmGKB; PA26452; -. DR VEuPathDB; HostDB:ENSG00000131778; -. DR eggNOG; KOG0385; Eukaryota. DR GeneTree; ENSGT00940000159402; -. DR InParanoid; Q86WJ1; -. DR OMA; FIVHCVD; -. DR OrthoDB; 5482994at2759; -. DR PhylomeDB; Q86WJ1; -. DR TreeFam; TF333326; -. DR PathwayCommons; Q86WJ1; -. DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER. DR Reactome; R-HSA-5696400; Dual Incision in GG-NER. DR SignaLink; Q86WJ1; -. DR BioGRID-ORCS; 9557; 15 hits in 1172 CRISPR screens. DR ChiTaRS; CHD1L; human. DR GeneWiki; CHD1L; -. DR GenomeRNAi; 9557; -. DR Pharos; Q86WJ1; Tbio. DR PRO; PR:Q86WJ1; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q86WJ1; Protein. DR Bgee; ENSG00000131778; Expressed in primordial germ cell in gonad and 160 other cell types or tissues. DR ExpressionAtlas; Q86WJ1; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0090734; C:site of DNA damage; IDA:UniProt. DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB. DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:UniProtKB. DR GO; GO:0003678; F:DNA helicase activity; TAS:UniProtKB. DR GO; GO:0140566; F:histone reader activity; IDA:UniProtKB. DR GO; GO:0031491; F:nucleosome binding; IDA:UniProtKB. DR GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB. DR GO; GO:0160004; F:poly-ADP-D-ribose modification-dependent protein binding; IDA:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB. DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; IDA:UniProt. 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; IPR002464; DNA/RNA_helicase_DEAH_CS. 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; PS00690; DEAH_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51154; MACRO; 1. DR Genevisible; Q86WJ1; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Chromosome; Coiled coil; KW DNA damage; DNA repair; Hydrolase; Methylation; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..897 FT /note="Chromodomain-helicase-DNA-binding protein 1-like" FT /id="PRO_0000332141" FT DOMAIN 58..223 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 351..513 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT DOMAIN 704..897 FT /note="Macro" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490" FT REGION 601..635 FT /note="Regulatory linker segment (RLS)" FT /evidence="ECO:0000269|PubMed:33357431" FT REGION 615..673 FT /note="Required for ATPase activity" FT /evidence="ECO:0000269|PubMed:29220653" FT REGION 628..654 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 687..711 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 638..675 FT /evidence="ECO:0000255" FT MOTIF 174..177 FT /note="DEAH box" FT COMPBIAS 631..654 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 691..708 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 71..78 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 9 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 540 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 607 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 618 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 628 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 636 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 891 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..281 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055675" FT VAR_SEQ 1..113 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_033340" FT VAR_SEQ 43..246 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_033341" FT VAR_SEQ 331..424 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_033342" FT VARIANT 25 FT /note="R -> P (in dbSNP:rs11588753)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_042954" FT VARIANT 350 FT /note="H -> Q (in dbSNP:rs17356233)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_042955" FT VARIANT 649 FT /note="E -> A (in dbSNP:rs13374920)" FT /id="VAR_042956" FT VARIANT 743 FT /note="S -> C (in dbSNP:rs2275249)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334" FT /id="VAR_042957" FT VARIANT 842 FT /note="R -> H (found in patients with cancer; loss of FT auto-inhibition, leading to constitutive ATP-dependent FT chromatin remodeler activity; dbSNP:rs782473109)" FT /evidence="ECO:0000269|PubMed:29220653" FT /id="VAR_086613" FT VARIANT 852 FT /note="W -> C (found in patients with cancer; loss of FT auto-inhibition, leading to constitutive ATP-dependent FT chromatin remodeler activity; dbSNP:rs1553974573)" FT /evidence="ECO:0000269|PubMed:34210977" FT /id="VAR_086614" FT VARIANT 857 FT /note="R -> Q (found in patients with cancer; loss of FT auto-inhibition, leading to constitutive ATP-dependent FT chromatin remodeler activity; dbSNP:rs1180954265)" FT /evidence="ECO:0000269|PubMed:29220652, FT ECO:0000269|PubMed:29220653" FT /id="VAR_086615" FT VARIANT 860 FT /note="R -> W (found in patients with cancer; loss of FT auto-inhibition, leading to constitutive ATP-dependent FT chromatin remodeler activity; dbSNP:rs139712616)" FT /evidence="ECO:0000269|PubMed:29220652, FT ECO:0000269|PubMed:29220653" FT /id="VAR_086616" FT VARIANT 885 FT /note="S -> A (in dbSNP:rs4950394)" FT /evidence="ECO:0000269|PubMed:16710414" FT /id="VAR_042958" FT MUTAGEN 77 FT /note="K->R: Abolishes ATPase activity." FT /evidence="ECO:0000269|PubMed:19661379" FT MUTAGEN 175 FT /note="E->Q: Abrogates chromatin remodeling activity. FT Prevents PARP2 removal from chromatin." FT /evidence="ECO:0000269|PubMed:29220653, FT ECO:0000269|PubMed:33275888" FT MUTAGEN 307..308 FT /note="KK->EE: Reduces interaction of the macro domain with FT the N-terminal ATPase module; when associated with E-398 FT and E-750." FT /evidence="ECO:0000269|PubMed:29220653" FT MUTAGEN 319..320 FT /note="RK->EE: Reduces interaction of the macro domain with FT the N-terminal ATPase module; when associated with E-407; FT E-422 and E-750." FT /evidence="ECO:0000269|PubMed:29220653" FT MUTAGEN 332..337 FT /note="EPEPFE->APAPAA: Reduces interaction of the macro FT domain with the N-terminal ATPase module; when associated FT with E-750." FT /evidence="ECO:0000269|PubMed:29220653" FT MUTAGEN 381 FT /note="D->A: Decreased interaction with nucleosomes." FT /evidence="ECO:0000269|PubMed:34210977" FT MUTAGEN 398 FT /note="R->E: Reduces interaction of the macro domain with FT the N-terminal ATPase module; when associated with E-307, FT E-308 and E-750." FT /evidence="ECO:0000269|PubMed:29220653" FT MUTAGEN 407 FT /note="K->E: Reduces interaction of the macro domain with FT the N-terminal ATPase module; when associated with E-319, FT E-320, E-422 and E-750." FT /evidence="ECO:0000269|PubMed:29220653" FT MUTAGEN 420 FT /note="S->A: Does not reduce interaction of the macro FT domain with the N-terminal ATPase module; when associated FT with E-750." FT /evidence="ECO:0000269|PubMed:29220653" FT MUTAGEN 422 FT /note="R->E: Reduces interaction of the macro domain with FT the N-terminal ATPase module; when associated with E-319, FT E-320, E-407 and E-750." FT /evidence="ECO:0000269|PubMed:29220653" FT MUTAGEN 457 FT /note="R->H: Abolished ATP-dependent chromatin remodeler FT activity." FT /evidence="ECO:0000269|PubMed:34210977" FT MUTAGEN 611..612 FT /note="RS->AA: Strongly reduced interaction with the acidic FT patch of histones." FT /evidence="ECO:0000269|PubMed:33357431, FT ECO:0000269|PubMed:34486521" FT MUTAGEN 611 FT /note="R->E: Reduced interaction with histones." FT /evidence="ECO:0000269|PubMed:34210977" FT MUTAGEN 614 FT /note="R->E: Reduced interaction with histones." FT /evidence="ECO:0000269|PubMed:34210977" FT MUTAGEN 653..656 FT /note="KRRR->AAAA: Does not reduce interaction of the macro FT domain with the N-terminal ATPase module; when associated FT with E-750." FT /evidence="ECO:0000269|PubMed:29220653" FT MUTAGEN 723 FT /note="D->A: Strongly reduces poly(ADP-ribose)-binding but FT not ATPase activity." FT /evidence="ECO:0000269|PubMed:19661379" FT MUTAGEN 750 FT /note="G->E: Disrupts interaction with PARP1. Abolishes the FT release from auto-inhibition through macro domain binding FT to the N-terminal ATPase module. Reduces interaction of the FT macro domain with the N-terminal ATPase module; when FT associated with E-307, E-308 and E-398; E-319, E-320, E-407 FT and E-422." FT /evidence="ECO:0000269|PubMed:29220653" FT MUTAGEN 857 FT /note="R->E: Loss of auto-inhibition, leading to FT constitutive ATP-dependent chromatin remodeler activity." FT /evidence="ECO:0000269|PubMed:29220652" FT CONFLICT 192 FT /note="E -> EVFE (in Ref. 3; ABQ59048)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="M -> T (in Ref. 2; BAG56702)" FT /evidence="ECO:0000305" FT CONFLICT 379 FT /note="L -> P (in Ref. 2; BAB55248)" FT /evidence="ECO:0000305" FT CONFLICT 447 FT /note="N -> D (in Ref. 6; BAD97216)" FT /evidence="ECO:0000305" FT CONFLICT 597 FT /note="N -> S (in Ref. 6; BAD97216)" FT /evidence="ECO:0000305" FT CONFLICT 674 FT /note="M -> V (in Ref. 2; BAA91637)" FT /evidence="ECO:0000305" FT TURN 21..24 FT /evidence="ECO:0007829|PDB:7EPU" FT HELIX 33..39 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 48..63 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 77..90 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 98..102 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 107..117 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 130..137 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 147..152 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 153..158 FT /evidence="ECO:0007829|PDB:7ENN" FT TURN 159..161 FT /evidence="ECO:0007829|PDB:7EPU" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 169..175 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 185..191 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 196..201 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:7EPU" FT HELIX 210..220 FT /evidence="ECO:0007829|PDB:7ENN" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 227..229 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 230..236 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 244..253 FT /evidence="ECO:0007829|PDB:7ENN" FT TURN 254..257 FT /evidence="ECO:0007829|PDB:7ENN" FT TURN 263..266 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 276..280 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 284..295 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 301..306 FT /evidence="ECO:0007829|PDB:7EPU" FT HELIX 314..323 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 325..327 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 329..331 FT /evidence="ECO:0007829|PDB:7ENN" FT TURN 341..345 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 347..362 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 366..371 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 373..386 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 390..393 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 395..397 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 400..411 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 416..420 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 421..424 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 425..427 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 435..439 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 445..453 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 464..471 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 475..487 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 490..497 FT /evidence="ECO:0007829|PDB:7ENN" FT TURN 517..519 FT /evidence="ECO:0007829|PDB:7ENN" FT TURN 523..526 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 537..544 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 549..552 FT /evidence="ECO:0007829|PDB:7ENN" FT STRAND 569..573 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 587..598 FT /evidence="ECO:0007829|PDB:7ENN" FT TURN 614..616 FT /evidence="ECO:0007829|PDB:7ENN" FT HELIX 641..666 FT /evidence="ECO:0007829|PDB:7EPU" FT STRAND 718..722 FT /evidence="ECO:0007829|PDB:7EPU" FT STRAND 734..736 FT /evidence="ECO:0007829|PDB:7EPU" FT STRAND 738..740 FT /evidence="ECO:0007829|PDB:7EPU" FT HELIX 750..757 FT /evidence="ECO:0007829|PDB:7EPU" FT TURN 758..760 FT /evidence="ECO:0007829|PDB:7EPU" FT HELIX 761..771 FT /evidence="ECO:0007829|PDB:7EPU" FT STRAND 800..802 FT /evidence="ECO:0007829|PDB:7EPU" FT HELIX 808..810 FT /evidence="ECO:0007829|PDB:7EPU" FT HELIX 818..834 FT /evidence="ECO:0007829|PDB:7EPU" FT STRAND 837..840 FT /evidence="ECO:0007829|PDB:7EPU" FT STRAND 845..847 FT /evidence="ECO:0007829|PDB:7EPU" FT HELIX 849..862 FT /evidence="ECO:0007829|PDB:7EPU" FT TURN 863..867 FT /evidence="ECO:0007829|PDB:7EPU" FT STRAND 870..874 FT /evidence="ECO:0007829|PDB:7EPU" SQ SEQUENCE 897 AA; 101000 MW; 226A1F8A44A8F9FE CRC64; MERAGATSRG GQAPGFLLRL HTEGRAEAAR VQEQDLRQWG LTGIHLRSYQ LEGVNWLAQR FHCQNGCILG DEMGLGKTCQ TIALFIYLAG RLNDEGPFLI LCPLSVLSNW KEEMQRFAPG LSCVTYAGDK EERACLQQDL KQESRFHVLL TTYEICLKDA SFLKSFPWSV LVVDEAHRLK NQSSLLHKTL SEFSVVFSLL LTGTPIQNSL QELYSLLSFV EPDLFSKEEV GDFIQRYQDI EKESESASEL HKLLQPFLLR RVKAEVATEL PKKTEVVIYH GMSALQKKYY KAILMKDLDA FENETAKKVK LQNILSQLRK CVDHPYLFDG VEPEPFEVGD HLTEASGKLH LLDKLLAFLY SGGHRVLLFS QMTQMLDILQ DYMDYRGYSY ERVDGSVRGE ERHLAIKNFG QQPIFVFLLS TRAGGVGMNL TAADTVIFVD SDFNPQNDLQ AAARAHRIGQ NKSVKVIRLI GRDTVEEIVY RKAASKLQLT NMIIEGGHFT LGAQKPAADA DLQLSEILKF GLDKLLASEG STMDEIDLES ILGETKDGQW VSDALPAAEG GSRDQEEGKN HMYLFEGKDY SKEPSKEDRK SFEQLVNLQK TLLEKASQEG RSLRNKGSVL IPGLVEGSTK RKRVLSPEEL EDRQKKRQEA AAKRRRLIEE KKRQKEEAEH KKKMAWWESN NYQSFCLPSE ESEPEDLENG EESSAELDYQ DPDATSLKYV SGDVTHPQAG AEDALIVHCV DDSGHWGRGG LFTALEKRSA EPRKIYELAG KMKDLSLGGV LLFPVDDKES RNKGQDLLAL IVAQHRDRSN VLSGIKMAAL EEGLKKIFLA AKKKKASVHL PRIGHATKGF NWYGTERLIR KHLAARGIPT YIYYFPRSKS AVLHSQSSSS SSRQLVP //