PARG2_CAEEL
ID PARG2_CAEEL Reviewed; 485 AA.
AC Q9N5L4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Poly(ADP-ribose) glycohydrolase 2 {ECO:0000312|WormBase:H23L24.5};
DE EC=3.2.1.143 {ECO:0000269|PubMed:17188026};
DE AltName: Full=Poly ADP-ribose metabolism enzyme 4;
GN Name=parg-2 {ECO:0000312|WormBase:H23L24.5};
GN Synonyms=pme-4 {ECO:0000312|WormBase:H23L24.5};
GN ORFNames=H23L24.5 {ECO:0000312|WormBase:H23L24.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-253; GLU-271; GLU-272 AND TYR-311.
RX PubMed=17188026; DOI=10.1016/j.dnarep.2006.10.027;
RA St-Laurent J.F., Gagnon S.N., Dequen F., Hardy I., Desnoyers S.;
RT "Altered DNA damage response in Caenorhabditis elegans with impaired
RT poly(ADP-ribose) glycohydrolases genes expression.";
RL DNA Repair 6:329-343(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Poly(ADP-ribose) synthesized after DNA damage is only present
CC transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase
CC (PubMed:17188026). Poly(ADP-ribose) metabolism may be required for
CC maintenance of the normal function of neuronal cells (By similarity).
CC {ECO:0000250|UniProtKB:Q86W56, ECO:0000269|PubMed:17188026}.
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:17188026};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17188026}.
CC -!- TISSUE SPECIFICITY: Expressed in head and tail neurons.
CC {ECO:0000269|PubMed:17188026}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages.
CC {ECO:0000269|PubMed:17188026}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in increased
CC sensitivity to gamma irradiation. {ECO:0000269|PubMed:17188026}.
CC -!- SIMILARITY: Belongs to the poly(ADP-ribose) glycohydrolase family.
CC {ECO:0000305}.
CC -!- CAUTION: Weak activity relative to mammalian poly(ADP-ribose)
CC glycohydrolase orthologs. {ECO:0000269|PubMed:17188026}.
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DR EMBL; AF548468; AAN40699.1; -; mRNA.
DR EMBL; FO081083; CCD68980.1; -; Genomic_DNA.
DR RefSeq; NP_501496.2; NM_069095.3.
DR AlphaFoldDB; Q9N5L4; -.
DR SMR; Q9N5L4; -.
DR BioGRID; 51485; 1.
DR STRING; 6239.H23L24.5; -.
DR EPD; Q9N5L4; -.
DR PaxDb; Q9N5L4; -.
DR PeptideAtlas; Q9N5L4; -.
DR EnsemblMetazoa; H23L24.5.1; H23L24.5.1; WBGene00004052.
DR GeneID; 186765; -.
DR KEGG; cel:CELE_H23L24.5; -.
DR UCSC; H23L24.5; c. elegans.
DR CTD; 186765; -.
DR WormBase; H23L24.5; CE32685; WBGene00004052; parg-2.
DR eggNOG; KOG2064; Eukaryota.
DR GeneTree; ENSGT00390000003652; -.
DR HOGENOM; CLU_013388_4_0_1; -.
DR InParanoid; Q9N5L4; -.
DR OMA; KDQWSFD; -.
DR OrthoDB; 730627at2759; -.
DR PhylomeDB; Q9N5L4; -.
DR BRENDA; 3.2.1.143; 1045.
DR PRO; PR:Q9N5L4; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004052; Expressed in material anatomical entity and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IDA:WormBase.
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; IEA:UniProtKB-KW.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IDA:WormBase.
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 GO; GO:0010332; P:response to gamma radiation; IMP:WormBase.
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 Cytoplasm; DNA damage; Hydrolase; Reference proteome.
FT CHAIN 1..485
FT /note="Poly(ADP-ribose) glycohydrolase 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000066606"
FT MUTAGEN 253
FT /note="D->N: Reduced poly(ADP-ribose) glycohydrolase
FT activity in vitro."
FT /evidence="ECO:0000269|PubMed:17188026"
FT MUTAGEN 271
FT /note="E->N: No poly(ADP-ribose) glycohydrolase activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:17188026"
FT MUTAGEN 272
FT /note="E->N: No poly(ADP-ribose) glycohydrolase activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:17188026"
FT MUTAGEN 311
FT /note="Y->A: Little poly(ADP-ribose) glycohydrolase
FT activity in vitro."
FT /evidence="ECO:0000269|PubMed:17188026"
SQ SEQUENCE 485 AA; 55574 MW; 86367DDBAB15081F CRC64;
MDHENLMKYL EEFRSIRFQP DFQKVDAERN VRYCEITDFP ISNISFELLE TGVSQQWRNC
DQNLFNEYLK TYKNGGYSQF EDLLFKIWGY SEEKERFDLP ALKSFYRKMS EIVGEDEVLE
KLARLVRITK SACEVLPEKI YRLVGDIESA TFSHIQCASL IAWMFFSDTP RLSFIIILQK
TTCVAVEKLK FLFTYFDKMS IDPPIGAVSF RKMRITHKQY LENWKLRETN LLPDVQVFDK
MSIEETALCT QIDFANKRLG GGVLKGGAVQ EEIRFMMCPE MMVAILLNDV TQDLEAISIV
GAYVFSSYTG YSNTLKWAKI TPKHSAQNNN SFRDQFGRLQ TETVAIDAVR NAGTPLECLL
NQLTTEKLTR EVRKAAIGFL SAGDGFSKIP VVSGWWGCGA FRGNKPLKFL IQVIACGISD
RPLQFCTFGD TELAKKCEEM MTLFRNNNVR TGQLFLIINS IGPPLNYSEQ YVFDAIRAKI
NSTKA
