ID   PARG1_ARATH             Reviewed;         548 AA.
AC   Q9SKB3; Q56W82; Q94ET7;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Poly(ADP-ribose) glycohydrolase 1;
DE            EC=3.2.1.143 {ECO:0000250|UniProtKB:Q867X0};
GN   Name=PARG1; Synonyms=TEJ; OrderedLocusNames=At2g31870; ORFNames=F20M17.9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLY-262, AND FUNCTION.
RC   STRAIN=cv. C24;
RX   PubMed=12110167; DOI=10.1016/s1534-5807(02)00200-9;
RA   Panda S., Poirier G.G., Kay S.A.;
RT   "tej defines a role for poly(ADP-ribosyl)ation in establishing period
RT   length of the arabidopsis circadian oscillator.";
RL   Dev. Cell 3:51-61(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Poly(ADP-ribose) synthesized after DNA damage is only present
CC       transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase
CC       (By similarity). Involved in establishing period length of the
CC       circadian oscillator. May regulate post-translational poly(ADP-
CC       ribosyl)ation of an oscillator component. {ECO:0000250,
CC       ECO:0000269|PubMed:12110167}.
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:0000250|UniProtKB:Q867X0};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9SKB3-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the poly(ADP-ribose) glycohydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; AF394690; AAK72256.1; -; mRNA.
DR   EMBL; AC006533; AAD32285.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08597.1; -; Genomic_DNA.
DR   EMBL; AK222165; BAD95273.1; -; mRNA.
DR   PIR; B84726; B84726.
DR   RefSeq; NP_565730.1; NM_128745.3. [Q9SKB3-1]
DR   AlphaFoldDB; Q9SKB3; -.
DR   SMR; Q9SKB3; -.
DR   BioGRID; 3092; 4.
DR   STRING; 3702.AT2G31870.1; -.
DR   PaxDb; Q9SKB3; -.
DR   PRIDE; Q9SKB3; -.
DR   EnsemblPlants; AT2G31870.1; AT2G31870.1; AT2G31870. [Q9SKB3-1]
DR   GeneID; 817745; -.
DR   Gramene; AT2G31870.1; AT2G31870.1; AT2G31870. [Q9SKB3-1]
DR   KEGG; ath:AT2G31870; -.
DR   Araport; AT2G31870; -.
DR   TAIR; locus:2045243; AT2G31870.
DR   eggNOG; KOG2064; Eukaryota.
DR   InParanoid; Q9SKB3; -.
DR   OrthoDB; 730627at2759; -.
DR   PhylomeDB; Q9SKB3; -.
DR   BRENDA; 3.2.1.143; 399.
DR   PRO; PR:Q9SKB3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SKB3; baseline and differential.
DR   Genevisible; Q9SKB3; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IDA:TAIR.
DR   GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0009225; P:nucleotide-sugar metabolic process; IBA:GO_Central.
DR   GO; GO:0006282; P:regulation of DNA repair; IMP:TAIR.
DR   GO; GO:0031056; P:regulation of histone modification; IBA:GO_Central.
DR   GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0090332; P:stomatal closure; IMP:TAIR.
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   Alternative splicing; Biological rhythms; Hydrolase; Reference proteome.
FT   CHAIN           1..548
FT                   /note="Poly(ADP-ribose) glycohydrolase 1"
FT                   /id="PRO_0000288791"
FT   MUTAGEN         262
FT                   /note="G->E: In tej; loss of function."
FT                   /evidence="ECO:0000269|PubMed:12110167"
FT   CONFLICT        170
FT                   /note="V -> I (in Ref. 4; BAD95273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408
FT                   /note="Missing (in Ref. 4; BAD95273)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   548 AA;  62170 MW;  F1A79FDA157C3329 CRC64;
     MENREDLNSI LPYLPLVIRS SSLYWPPRVV EALKAMSEGP SHSQVDSGEV LRQAIFDMRR
     SLSFSTLEPS ASNGYAFLFD ELIDEKESKR WFDEIIPALA SLLLQFPSLL EVHFQNADNI
     VSGIKTGLRL LNSQQAGIVF LSQELIGALL ACSFFCLFPD DNRGAKHLPV INFDHLFASL
     YISYSQSQES KIRCIMHYFE RFCSCVPIGI VSFERKITAA PDADFWSKSD VSLCAFKVHS
     FGLIEDQPDN ALEVDFANKY LGGGSLSRGC VQEEIRFMIN PELIAGMLFL PRMDDNEAIE
     IVGAERFSCY TGYASSFRFA GEYIDKKAMD PFKRRRTRIV AIDALCTPKM RHFKDICLLR
     EINKALCGFL NCSKAWEHQN IFMDEGDNEI QLVRNGRDSG LLRTETTASH RTPLNDVEMN
     REKPANNLIR DFYVEGVDNE DHEDDGVATG NWGCGVFGGD PELKATIQWL AASQTRRPFI
     SYYTFGVEAL RNLDQVTKWI LSHKWTVGDL WNMMLEYSAQ RLYKQTSVGF FSWLLPSLAT
     TNKAIQPP