PARG_HUMAN
ID PARG_HUMAN Reviewed; 976 AA.
AC Q86W56; A5YBK3; B2RC24; B4DIU5; B4DYR4; I6RUV3; Q6E4P6; Q6E4P7; Q7Z742;
AC Q9Y4W7;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Poly(ADP-ribose) glycohydrolase {ECO:0000303|PubMed:14527731};
DE EC=3.2.1.143 {ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:23481255};
GN Name=PARG {ECO:0000303|PubMed:14527731, ECO:0000312|HGNC:HGNC:8605};
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.
RC TISSUE=Skin;
RX PubMed=14527731; DOI=10.1016/s0378-1119(03)00738-8;
RA Meyer R.G., Meyer-Ficca M.L., Jacobson E.L., Jacobson M.K.;
RT "Human poly(ADP-ribose) glycohydrolase (PARG) gene and the common promoter
RT sequence it shares with inner mitochondrial membrane translocase 23
RT (TIM23).";
RL Gene 314:181-190(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), MUTAGENESIS OF LYS-12;
RP ARG-13; ARG-36 AND ARG-37, SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION
RP SIGNAL.
RC TISSUE=Skin;
RX PubMed=15212953; DOI=10.1016/j.yexcr.2004.03.050;
RA Meyer-Ficca M.L., Meyer R.G., Coyle D.L., Jacobson E.L., Jacobson M.K.;
RT "Human poly(ADP-ribose) glycohydrolase is expressed in alternative splice
RT variants yielding isoforms that localize to different cell compartments.";
RL Exp. Cell Res. 297:521-532(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10449915; DOI=10.1159/000015310;
RA Ame J.-C., Apiou F., Jacobson E.L., Jacobson M.K.;
RT "Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to human
RT chromosome 10q11.23 and mouse chromosome 14B by in situ hybridization.";
RL Cytogenet. Cell Genet. 85:269-270(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=17509564; DOI=10.1016/j.yexcr.2007.03.043;
RA Meyer R.G., Meyer-Ficca M.L., Whatcott C.J., Jacobson E.L., Jacobson M.K.;
RT "Two small enzyme isoforms mediate mammalian mitochondrial poly(ADP-ribose)
RT glycohydrolase (PARG) activity.";
RL Exp. Cell Res. 313:2920-2936(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING (ISOFORMS 4
RP AND 5), ABSENCE OF CATALYTIC ACTIVITY (ISOFORMS 4 AND 5), AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Peripheral blood monocyte;
RX PubMed=22433848; DOI=10.1074/jbc.m112.349183;
RA Niere M., Mashimo M., Agledal L., Dolle C., Kasamatsu A., Kato J., Moss J.,
RA Ziegler M.;
RT "ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG)
RT isoforms, is responsible for degradation of mitochondrial matrix-associated
RT poly(ADP-ribose).";
RL J. Biol. Chem. 287:16088-16102(2012).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain cortex, Hippocampus, and Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, and Testis;
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 [8]
RP FUNCTION.
RX PubMed=15450800; DOI=10.1016/j.ab.2004.04.032;
RA Putt K.S., Hergenrother P.J.;
RT "A nonradiometric, high-throughput assay for poly(ADP-ribose)
RT glycohydrolase (PARG): application to inhibitor identification and
RT evaluation.";
RL Anal. Biochem. 333:256-264(2004).
RN [9]
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
RX PubMed=16460818; DOI=10.1016/j.bbamcr.2005.11.015;
RA Haince J.F., Ouellet M.E., McDonald D., Hendzel M.J., Poirier G.G.;
RT "Dynamic relocation of poly(ADP-ribose) glycohydrolase isoforms during
RT radiation-induced DNA damage.";
RL Biochim. Biophys. Acta 1763:226-237(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133; SER-137; SER-197 AND
RP THR-199, AND IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION AT SER-197; THR-199 AND SER-298.
RX PubMed=19105632; DOI=10.1021/pr800810n;
RA Gagne J.P., Moreel X., Gagne P., Labelle Y., Droit A., Chevalier-Pare M.,
RA Bourassa S., McDonald D., Hendzel M.J., Prigent C., Poirier G.G.;
RT "Proteomic investigation of phosphorylation sites in poly(ADP-ribose)
RT polymerase-1 and poly(ADP-ribose) glycohydrolase.";
RL J. Proteome Res. 8:1014-1029(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND THR-199, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY 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 [15]
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 [16]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASN-740;
RP GLU-755; GLU-756; ALA-874 AND PHE-875.
RX PubMed=21892188; DOI=10.1038/nature10404;
RA Slade D., Dunstan M.S., Barkauskaite E., Weston R., Lafite P., Dixon N.,
RA Ahel M., Leys D., Ahel I.;
RT "The structure and catalytic mechanism of a poly(ADP-ribose)
RT glycohydrolase.";
RL Nature 477:616-620(2011).
RN [17]
RP SUBCELLULAR LOCATION (ISOFORM 1), AND INTERACTION WITH PCNA.
RX PubMed=21398629; DOI=10.1093/nar/gkr099;
RA Mortusewicz O., Fouquerel E., Ame J.C., Leonhardt H., Schreiber V.;
RT "PARG is recruited to DNA damage sites through poly(ADP-ribose)- and PCNA-
RT dependent mechanisms.";
RL Nucleic Acids Res. 39:5045-5056(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP FUNCTION.
RX PubMed=23102699; DOI=10.1016/j.molcel.2012.09.021;
RA Le May N., Iltis I., Ame J.C., Zhovmer A., Biard D., Egly J.M.,
RA Schreiber V., Coin F.;
RT "Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-mediated
RT gene expression.";
RL Mol. Cell 48:785-798(2012).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23481255; DOI=10.1038/emboj.2013.51;
RA Sharifi R., Morra R., Appel C.D., Tallis M., Chioza B., Jankevicius G.,
RA Simpson M.A., Matic I., Ozkan E., Golia B., Schellenberg M.J., Weston R.,
RA Williams J.G., Rossi M.N., Galehdari H., Krahn J., Wan A., Trembath R.C.,
RA Crosby A.H., Ahel D., Hay R., Ladurner A.G., Timinszky G., Williams R.S.,
RA Ahel I.;
RT "Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in
RT neurodegenerative disease.";
RL EMBO J. 32:1225-1237(2013).
RN [22]
RP FUNCTION.
RX PubMed=23474714; DOI=10.1038/nsmb.2521;
RA Rosenthal F., Feijs K.L., Frugier E., Bonalli M., Forst A.H., Imhof R.,
RA Winkler H.C., Fischer D., Caflisch A., Hassa P.O., Luescher B.,
RA Hottiger M.O.;
RT "Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases.";
RL Nat. Struct. Mol. Biol. 20:502-507(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-68; SER-133; SER-137;
RP THR-139; SER-286; SER-291; SER-302; SER-316 AND SER-448, AND IDENTIFICATION
RP 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-264, AND
RP IDENTIFICATION BY 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 [25]
RP FUNCTION.
RX PubMed=24906880; DOI=10.1093/nar/gku505;
RA Illuzzi G., Fouquerel E., Ame J.C., Noll A., Rehmet K., Nasheuer H.P.,
RA Dantzer F., Schreiber V.;
RT "PARG is dispensable for recovery from transient replicative stress but
RT required to prevent detrimental accumulation of poly(ADP-ribose) upon
RT prolonged replicative stress.";
RL Nucleic Acids Res. 42:7776-7792(2014).
RN [26]
RP FUNCTION, AND INTERACTION WITH NUDT5.
RX PubMed=27257257; DOI=10.1126/science.aad9335;
RA Wright R.H., Lioutas A., Le Dily F., Soronellas D., Pohl A., Bonet J.,
RA Nacht A.S., Samino S., Font-Mateu J., Vicent G.P., Wierer M., Trabado M.A.,
RA Schelhorn C., Carolis C., Macias M.J., Yanes O., Oliva B., Beato M.;
RT "ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for
RT chromatin remodeling.";
RL Science 352:1221-1225(2016).
RN [27]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33186521; DOI=10.1016/j.cell.2020.09.055;
RA Bonfiglio J.J., Leidecker O., Dauben H., Longarini E.J., Colby T.,
RA San Segundo-Acosta P., Perez K.A., Matic I.;
RT "An HPF1/PARP1-based chemical biology strategy for exploring ADP-
RT ribosylation.";
RL Cell 183:1086-1102(2020).
RN [28]
RP FUNCTION.
RX PubMed=34019811; DOI=10.1016/j.molcel.2021.04.028;
RA Prokhorova E., Agnew T., Wondisford A.R., Tellier M., Kaminski N.,
RA Beijer D., Holder J., Groslambert J., Suskiewicz M.J., Zhu K., Reber J.M.,
RA Krassnig S.C., Palazzo L., Murphy S., Nielsen M.L., Mangerich A., Ahel D.,
RA Baets J., O'Sullivan R.J., Ahel I.;
RT "Unrestrained poly-ADP-ribosylation provides insights into chromatin
RT regulation and human disease.";
RL Mol. Cell 81:2640-2655.e8(2021).
RN [29]
RP FUNCTION, AND MUTAGENESIS OF GLU-756.
RX PubMed=34321462; DOI=10.1038/s41467-021-24723-3;
RA Rack J.G.M., Liu Q., Zorzini V., Voorneveld J., Ariza A.,
RA Honarmand Ebrahimi K., Reber J.M., Krassnig S.C., Ahel D.,
RA van der Marel G.A., Mangerich A., McCullagh J.S.O., Filippov D.V., Ahel I.;
RT "Mechanistic insights into the three steps of poly(ADP-ribosylation)
RT reversal.";
RL Nat. Commun. 12:4581-4581(2021).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 448-976 ALONE AND IN COMPLEX WITH
RP INHIBITORS, ACTIVE SITE, AND SUBSTRATE-BINDING SITES.
RX PubMed=23251397; DOI=10.1371/journal.pone.0050889;
RA Tucker J.A., Bennett N., Brassington C., Durant S.T., Hassall G.,
RA Holdgate G., McAlister M., Nissink J.W., Truman C., Watson M.;
RT "Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain
RT confirm catalytic mechanism and explain inhibition by ADP-HPD
RT derivatives.";
RL PLoS ONE 7:E50889-E50889(2012).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 448-976 IN COMPLEX WITH
RP SUBSTRATE.
RX PubMed=30472116; DOI=10.1016/j.chembiol.2018.11.001;
RA Rack J.G.M., Ariza A., Drown B.S., Henfrey C., Bartlett E., Shirai T.,
RA Hergenrother P.J., Ahel I.;
RT "(ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate
RT Recognition and Inhibition.";
RL Cell Chem. Biol. 0:0-0(2018).
CC -!- FUNCTION: Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-
CC ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-
CC ribose) (PubMed:15450800, PubMed:21892188, PubMed:23102699,
CC PubMed:23474714, PubMed:33186521, PubMed:34321462, PubMed:34019811).
CC PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-
CC ribose) of different length as well as ADP-ribose monomers
CC (PubMed:23102699, PubMed:23481255). It is however unable to cleave the
CC ester bond between the terminal ADP-ribose and ADP-ribosylated
CC residues, leaving proteins that are mono-ADP-ribosylated
CC (PubMed:21892188, PubMed:23474714, PubMed:33186521). Poly(ADP-ribose)
CC is synthesized after DNA damage is only present transiently and is
CC rapidly degraded by PARG (PubMed:23102699, PubMed:34019811). Required
CC to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged
CC replicative stress, while it is not required for recovery from
CC transient replicative stress (PubMed:24906880). Responsible for the
CC prevalence of mono-ADP-ribosylated proteins in cells, thanks to its
CC ability to degrade poly(ADP-ribose) without cleaving the terminal
CC protein-ribose bond (PubMed:33186521). Required for retinoid acid-
CC dependent gene transactivation, probably by removing poly(ADP-ribose)
CC from histone demethylase KDM4D, allowing chromatin derepression at RAR-
CC dependent gene promoters (PubMed:23102699). Involved in the synthesis
CC of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5
CC (PubMed:27257257). Nuclear ATP generation is required for extensive
CC chromatin remodeling events that are energy-consuming
CC (PubMed:27257257). {ECO:0000269|PubMed:15450800,
CC ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:23102699,
CC ECO:0000269|PubMed:23474714, ECO:0000269|PubMed:23481255,
CC ECO:0000269|PubMed:24906880, ECO:0000269|PubMed:27257257,
CC ECO:0000269|PubMed:33186521, ECO:0000269|PubMed:34019811,
CC ECO:0000269|PubMed:34321462}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-
CC alpha-D-ribose](n-1) + ADP-D-ribose; Xref=Rhea:RHEA:52216, Rhea:RHEA-
CC COMP:16922, Rhea:RHEA-COMP:16923, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:142512; EC=3.2.1.143;
CC Evidence={ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:23481255,
CC ECO:0000269|PubMed:33186521};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52217;
CC Evidence={ECO:0000269|PubMed:21892188, ECO:0000269|PubMed:23481255,
CC ECO:0000269|PubMed:33186521};
CC -!- SUBUNIT: Interacts with PCNA (PubMed:21398629). Interacts with NUDT5
CC (PubMed:27257257). {ECO:0000269|PubMed:21398629,
CC ECO:0000269|PubMed:27257257}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000269|PubMed:16460818, ECO:0000269|PubMed:21398629}.
CC Note=Colocalizes with PCNA at replication foci (PubMed:21398629).
CC Relocalizes to the cytoplasm in response to DNA damage
CC (PubMed:16460818). {ECO:0000269|PubMed:16460818,
CC ECO:0000269|PubMed:21398629}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:15212953, ECO:0000269|PubMed:16460818}.
CC Note=Translocates to the nucleus in response to DNA damage.
CC {ECO:0000269|PubMed:16460818}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:15212953}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
CC {ECO:0000269|PubMed:22433848}. Mitochondrion
CC {ECO:0000269|PubMed:22433848}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion matrix
CC {ECO:0000269|PubMed:17509564}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=hPARG111;
CC IsoId=Q86W56-1; Sequence=Displayed;
CC Name=2; Synonyms=hPARG102;
CC IsoId=Q86W56-2; Sequence=VSP_011769;
CC Name=3; Synonyms=hPARG99;
CC IsoId=Q86W56-3; Sequence=VSP_011770;
CC Name=4; Synonyms=hPARG60;
CC IsoId=Q86W56-4; Sequence=VSP_044675, VSP_044676, VSP_044677;
CC Name=5; Synonyms=hPARG55;
CC IsoId=Q86W56-5; Sequence=VSP_044674, VSP_044677;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:14527731}.
CC -!- DOMAIN: The PIP-box mediates interaction with PCNA and localization to
CC replication foci. {ECO:0000269|PubMed:21398629}.
CC -!- MISCELLANEOUS: [Isoform 4]: Catalytically inactive. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Catalytically inactive. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the poly(ADP-ribose) glycohydrolase family.
CC {ECO:0000305}.
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DR EMBL; AY258587; AAP83314.1; -; mRNA.
DR EMBL; AY575848; AAT66421.1; -; mRNA.
DR EMBL; AY575849; AAT66422.1; -; mRNA.
DR EMBL; AF005043; AAB61614.1; -; mRNA.
DR EMBL; EF382674; ABR10027.1; -; mRNA.
DR EMBL; JQ890226; AFM56043.1; -; mRNA.
DR EMBL; AK295786; BAG58607.1; -; mRNA.
DR EMBL; AK302560; BAG63826.1; -; mRNA.
DR EMBL; AK314909; BAG37421.1; -; mRNA.
DR EMBL; BC050560; AAH50560.1; -; mRNA.
DR EMBL; BC052966; AAH52966.1; -; mRNA.
DR CCDS; CCDS73130.1; -. [Q86W56-1]
DR RefSeq; NP_001289706.1; NM_001302777.1.
DR RefSeq; NP_001290415.1; NM_001303486.1. [Q86W56-2]
DR RefSeq; NP_001290416.1; NM_001303487.1. [Q86W56-3]
DR RefSeq; NP_001311310.1; NM_001324381.1. [Q86W56-2]
DR RefSeq; NP_003622.2; NM_003631.3. [Q86W56-1]
DR PDB; 4A0D; X-ray; 1.75 A; A=448-976.
DR PDB; 4B1G; X-ray; 1.83 A; A=448-976.
DR PDB; 4B1H; X-ray; 2.00 A; A=448-976.
DR PDB; 4B1I; X-ray; 2.14 A; A=448-976.
DR PDB; 4B1J; X-ray; 2.08 A; A=448-976.
DR PDB; 5A7R; X-ray; 1.95 A; A=448-976.
DR PDB; 5LHB; X-ray; 2.23 A; A=448-976.
DR PDB; 6HH6; X-ray; 1.85 A; A=448-976.
DR PDB; 6HMK; X-ray; 2.06 A; A=448-976.
DR PDB; 6HML; X-ray; 2.25 A; A=448-976.
DR PDB; 6HMM; X-ray; 1.90 A; A=448-976.
DR PDB; 6HMN; X-ray; 2.87 A; A=448-976.
DR PDB; 6O9X; X-ray; 1.70 A; A=448-976.
DR PDB; 6O9Y; X-ray; 2.00 A; A=448-976.
DR PDB; 6OA0; X-ray; 2.00 A; A=448-976.
DR PDB; 6OA1; X-ray; 1.80 A; A=448-976.
DR PDB; 6OA3; X-ray; 1.90 A; A=448-976.
DR PDB; 6OAK; X-ray; 1.70 A; A=448-976.
DR PDB; 6OAL; X-ray; 1.60 A; A=448-976.
DR PDB; 7KFP; X-ray; 1.90 A; A=448-976.
DR PDB; 7KG0; X-ray; 1.66 A; A=448-976.
DR PDB; 7KG1; X-ray; 1.65 A; A=448-976.
DR PDB; 7KG6; X-ray; 1.96 A; A=448-976.
DR PDB; 7KG7; X-ray; 1.85 A; A=448-976.
DR PDB; 7KG8; X-ray; 1.43 A; A=448-976.
DR PDBsum; 4A0D; -.
DR PDBsum; 4B1G; -.
DR PDBsum; 4B1H; -.
DR PDBsum; 4B1I; -.
DR PDBsum; 4B1J; -.
DR PDBsum; 5A7R; -.
DR PDBsum; 5LHB; -.
DR PDBsum; 6HH6; -.
DR PDBsum; 6HMK; -.
DR PDBsum; 6HML; -.
DR PDBsum; 6HMM; -.
DR PDBsum; 6HMN; -.
DR PDBsum; 6O9X; -.
DR PDBsum; 6O9Y; -.
DR PDBsum; 6OA0; -.
DR PDBsum; 6OA1; -.
DR PDBsum; 6OA3; -.
DR PDBsum; 6OAK; -.
DR PDBsum; 6OAL; -.
DR PDBsum; 7KFP; -.
DR PDBsum; 7KG0; -.
DR PDBsum; 7KG1; -.
DR PDBsum; 7KG6; -.
DR PDBsum; 7KG7; -.
DR PDBsum; 7KG8; -.
DR AlphaFoldDB; Q86W56; -.
DR SMR; Q86W56; -.
DR BioGRID; 114077; 13.
DR IntAct; Q86W56; 4.
DR MINT; Q86W56; -.
DR STRING; 9606.ENSP00000384408; -.
DR BindingDB; Q86W56; -.
DR ChEMBL; CHEMBL1795143; -.
DR GlyGen; Q86W56; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86W56; -.
DR PhosphoSitePlus; Q86W56; -.
DR BioMuta; PARG; -.
DR DMDM; 56417893; -.
DR EPD; Q86W56; -.
DR jPOST; Q86W56; -.
DR MassIVE; Q86W56; -.
DR MaxQB; Q86W56; -.
DR PaxDb; Q86W56; -.
DR PeptideAtlas; Q86W56; -.
DR PRIDE; Q86W56; -.
DR ProteomicsDB; 70121; -. [Q86W56-1]
DR ProteomicsDB; 70122; -. [Q86W56-2]
DR ProteomicsDB; 70123; -. [Q86W56-3]
DR Antibodypedia; 44981; 240 antibodies from 27 providers.
DR DNASU; 670; -.
DR Ensembl; ENST00000402038.7; ENSP00000384408.3; ENSG00000227345.9. [Q86W56-1]
DR Ensembl; ENST00000616448.2; ENSP00000484285.1; ENSG00000227345.9. [Q86W56-1]
DR GeneID; 670; -.
DR GeneID; 8505; -.
DR KEGG; hsa:8505; -.
DR MANE-Select; ENST00000616448.2; ENSP00000484285.1; NM_003631.5; NP_003622.2.
DR UCSC; uc057tfe.1; human. [Q86W56-1]
DR CTD; 670; -.
DR CTD; 8505; -.
DR DisGeNET; 670; -.
DR DisGeNET; 8505; -.
DR GeneCards; PARG; -.
DR HGNC; HGNC:8605; PARG.
DR HPA; ENSG00000227345; Low tissue specificity.
DR MIM; 603501; gene.
DR neXtProt; NX_Q86W56; -.
DR OpenTargets; ENSG00000227345; -.
DR PharmGKB; PA32940; -.
DR VEuPathDB; HostDB:ENSG00000227345; -.
DR eggNOG; KOG2064; Eukaryota.
DR GeneTree; ENSGT00390000003652; -.
DR HOGENOM; CLU_015146_0_0_1; -.
DR InParanoid; Q86W56; -.
DR OMA; GCDACVS; -.
DR OrthoDB; 730627at2759; -.
DR PhylomeDB; Q86W56; -.
DR TreeFam; TF323527; -.
DR BRENDA; 3.2.1.143; 2681.
DR PathwayCommons; Q86W56; -.
DR Reactome; R-HSA-110362; POLB-Dependent Long Patch Base Excision Repair.
DR SignaLink; Q86W56; -.
DR BioGRID-ORCS; 670; 8 hits in 1082 CRISPR screens.
DR BioGRID-ORCS; 8505; 41 hits in 236 CRISPR screens.
DR ChiTaRS; PARG; human.
DR GeneWiki; PARG; -.
DR Pharos; Q86W56; Tchem.
DR PRO; PR:Q86W56; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q86W56; protein.
DR Bgee; ENSG00000227345; Expressed in calcaneal tendon and 169 other tissues.
DR ExpressionAtlas; Q86W56; baseline and differential.
DR Genevisible; Q86W56; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IDA:UniProtKB.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; IDA:UniProtKB.
DR GO; GO:0006287; P:base-excision repair, gap-filling; TAS:Reactome.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IBA:GO_Central.
DR GO; GO:0006282; P:regulation of DNA repair; IBA:GO_Central.
DR GO; GO:0031056; P:regulation of histone modification; IBA:GO_Central.
DR InterPro; IPR046372; PARG_cat.
DR InterPro; IPR007724; Poly_GlycHdrlase.
DR PANTHER; PTHR12837; PTHR12837; 1.
DR Pfam; PF05028; PARG_cat; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA damage;
KW Hydrolase; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..976
FT /note="Poly(ADP-ribose) glycohydrolase"
FT /id="PRO_0000066602"
FT REGION 1..456
FT /note="A-domain"
FT /evidence="ECO:0000269|PubMed:23251397"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..795
FT /note="Catalytic"
FT /evidence="ECO:0000269|PubMed:23251397"
FT MOTIF 10..16
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:15212953"
FT MOTIF 76..83
FT /note="PIP-box (PCNA interacting peptide)"
FT /evidence="ECO:0000269|PubMed:21398629"
FT COMPBIAS 191..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 737
FT /evidence="ECO:0000269|PubMed:23251397"
FT ACT_SITE 755
FT /evidence="ECO:0000269|PubMed:21892188,
FT ECO:0000269|PubMed:23251397"
FT ACT_SITE 756
FT /evidence="ECO:0000269|PubMed:21892188,
FT ECO:0000269|PubMed:23251397"
FT BINDING 726..727
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23251397,
FT ECO:0000269|PubMed:30472116"
FT BINDING 740
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23251397,
FT ECO:0000269|PubMed:30472116"
FT BINDING 754
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23251397,
FT ECO:0000269|PubMed:30472116"
FT BINDING 795
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9QYM2"
FT BINDING 869..874
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23251397,
FT ECO:0000269|PubMed:30472116"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105632,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"
FT MOD_RES 199
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19105632,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19105632"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 340
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88622"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..460
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17509564"
FT /id="VSP_044674"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15212953"
FT /id="VSP_011770"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15212953"
FT /id="VSP_011769"
FT VAR_SEQ 1..15
FT /note="MNAGPGCEPCTKRPR -> MVQAGAEKDAQSISL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:22433848"
FT /id="VSP_044675"
FT VAR_SEQ 16..423
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:22433848"
FT /id="VSP_044676"
FT VAR_SEQ 485..526
FT /note="RVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDE -> W (in
FT isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:17509564,
FT ECO:0000303|PubMed:22433848"
FT /id="VSP_044677"
FT MUTAGEN 12
FT /note="K->A: Abolishes nuclear targeting; when associated
FT with G-13."
FT /evidence="ECO:0000269|PubMed:15212953"
FT MUTAGEN 13
FT /note="R->G: Abolishes nuclear targeting; when associated
FT with A-12."
FT /evidence="ECO:0000269|PubMed:15212953"
FT MUTAGEN 36
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:15212953"
FT MUTAGEN 37
FT /note="R->G: No effect."
FT /evidence="ECO:0000269|PubMed:15212953"
FT MUTAGEN 740
FT /note="N->A: Reduced poly(ADP-ribose) glycohydrolase
FT activity."
FT /evidence="ECO:0000269|PubMed:21892188"
FT MUTAGEN 755
FT /note="E->A: Abolished poly(ADP-ribose) glycohydrolase
FT activity."
FT /evidence="ECO:0000269|PubMed:21892188"
FT MUTAGEN 756
FT /note="E->A: Abolished poly(ADP-ribose) glycohydrolase
FT activity."
FT /evidence="ECO:0000269|PubMed:21892188"
FT MUTAGEN 756
FT /note="E->N: Reduces hydrolase activity."
FT /evidence="ECO:0000269|PubMed:34321462"
FT MUTAGEN 874
FT /note="A->W: Reduced poly(ADP-ribose) glycohydrolase
FT activity."
FT /evidence="ECO:0000269|PubMed:21892188"
FT MUTAGEN 875
FT /note="F->A: Abolished poly(ADP-ribose) glycohydrolase
FT activity."
FT /evidence="ECO:0000269|PubMed:21892188"
FT CONFLICT 13..14
FT /note="RP -> AT (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="R -> Q (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="E -> V (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="P -> L (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="Q -> H (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="D -> H (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="E -> K (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="P -> S (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="T -> I (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="F -> L (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="R -> Q (in Ref. 5; AFM56043)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="I -> V (in Ref. 5; AFM56043)"
FT /evidence="ECO:0000305"
FT CONFLICT 814..815
FT /note="WQ -> CE (in Ref. 3; AAB61614)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="R -> H (in Ref. 7; AAH52966)"
FT /evidence="ECO:0000305"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:7KG8"
FT TURN 464..467
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 497..501
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:6O9X"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:6O9X"
FT HELIX 535..543
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 550..559
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:7KG8"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 571..579
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 583..591
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 593..602
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 604..607
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 621..626
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 627..638
FT /evidence="ECO:0007829|PDB:7KG8"
FT TURN 652..655
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 662..665
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 671..688
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 694..701
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 708..710
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 718..724
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 726..729
FT /evidence="ECO:0007829|PDB:7KG8"
FT TURN 730..732
FT /evidence="ECO:0007829|PDB:6OAL"
FT STRAND 733..739
FT /evidence="ECO:0007829|PDB:7KG8"
FT TURN 743..750
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 754..761
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 763..767
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 768..771
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 779..784
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 790..793
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 796..798
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 800..804
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 815..818
FT /evidence="ECO:0007829|PDB:6HH6"
FT STRAND 820..825
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 832..836
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 838..852
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 859..861
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 865..868
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 873..875
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 879..892
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 897..900
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 905..920
FT /evidence="ECO:0007829|PDB:7KG8"
FT HELIX 925..939
FT /evidence="ECO:0007829|PDB:7KG8"
FT TURN 940..942
FT /evidence="ECO:0007829|PDB:7KG8"
FT STRAND 945..947
FT /evidence="ECO:0007829|PDB:7KG1"
FT HELIX 952..961
FT /evidence="ECO:0007829|PDB:7KG8"
FT MOD_RES Q86W56-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 976 AA; 111110 MW; D6646353C6D0180E CRC64;
MNAGPGCEPC TKRPRWGAAT TSPAASDARS FPSRQRRVLD PKDAHVQFRV PPSSPACVPG
RAGQHRGSAT SLVFKQKTIT SWMDTKGIKT AESESLDSKE NNNTRIESMM SSVQKDNFYQ
HNVEKLENVS QLSLDKSPTE KSTQYLNQHQ TAAMCKWQNE GKHTEQLLES EPQTVTLVPE
QFSNANIDRS PQNDDHSDTD SEENRDNQQF LTTVKLANAK QTTEDEQARE AKSHQKCSKS
CDPGEDCASC QQDEIDVVPE SPLSDVGSED VGTGPKNDNK LTRQESCLGN SPPFEKESEP
ESPMDVDNSK NSCQDSEADE ETSPGFDEQE DGSSSQTANK PSRFQARDAD IEFRKRYSTK
GGEVRLHFQF EGGESRTGMN DLNAKLPGNI SSLNVECRNS KQHGKKDSKI TDHFMRLPKA
EDRRKEQWET KHQRTERKIP KYVPPHLSPD KKWLGTPIEE MRRMPRCGIR LPLLRPSANH
TVTIRVDLLR AGEVPKPFPT HYKDLWDNKH VKMPCSEQNL YPVEDENGER TAGSRWELIQ
TALLNKFTRP QNLKDAILKY NVAYSKKWDF TALIDFWDKV LEEAEAQHLY QSILPDMVKI
ALCLPNICTQ PIPLLKQKMN HSITMSQEQI ASLLANAFFC TFPRRNAKMK SEYSSYPDIN
FNRLFEGRSS RKPEKLKTLF CYFRRVTEKK PTGLVTFTRQ SLEDFPEWER CEKPLTRLHV
TYEGTIEENG QGMLQVDFAN RFVGGGVTSA GLVQEEIRFL INPELIISRL FTEVLDHNEC
LIITGTEQYS EYTGYAETYR WSRSHEDGSE RDDWQRRCTE IVAIDALHFR RYLDQFVPEK
MRRELNKAYC GFLRPGVSSE NLSAVATGNW GCGAFGGDAR LKALIQILAA AAAERDVVYF
TFGDSELMRD IYSMHIFLTE RKLTVGDVYK LLLRYYNEEC RNCSTPGPDI KLYPFIYHAV
ESCAETADHS GQRTGT
