PARG1_CAEEL
ID PARG1_CAEEL Reviewed; 781 AA.
AC Q867X0; Q19637;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Poly(ADP-ribose) glycohydrolase 1 {ECO:0000312|WormBase:F20C5.1a};
DE EC=3.2.1.143 {ECO:0000269|PubMed:17188026};
DE AltName: Full=Poly ADP-ribose metabolism enzyme 3;
GN Name=parg-1 {ECO:0000312|WormBase:F20C5.1a};
GN Synonyms=pme-3 {ECO:0000312|WormBase:F20C5.1a};
GN ORFNames=F20C5.1 {ECO:0000312|WormBase:F20C5.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:AAO26316.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-536; GLU-554; GLU-555 AND
RP TYR-594.
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] {ECO:0000312|EMBL:CAD89735.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAD89735.1};
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: Nucleus {ECO:0000269|PubMed:17188026}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F20C5.1a}; Synonyms=long
CC {ECO:0000303|PubMed:17188026};
CC IsoId=Q867X0-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F20C5.1b}; Synonyms=short
CC {ECO:0000303|PubMed:17188026};
CC IsoId=Q867X0-2; Sequence=VSP_051616, VSP_051617;
CC -!- TISSUE SPECIFICITY: Expressed in head and tail neurons. Also detected
CC in the central nerve cord and motor 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; AY185493; AAO26316.1; -; mRNA.
DR EMBL; AY185494; AAO26317.1; -; mRNA.
DR EMBL; Z68161; CAA92299.2; -; Genomic_DNA.
DR EMBL; Z68161; CAD89735.1; -; Genomic_DNA.
DR PIR; T21138; T21138.
DR RefSeq; NP_001023135.1; NM_001027964.3. [Q867X0-1]
DR RefSeq; NP_001023136.1; NM_001027965.2. [Q867X0-2]
DR AlphaFoldDB; Q867X0; -.
DR SMR; Q867X0; -.
DR STRING; 6239.F20C5.1f; -.
DR EPD; Q867X0; -.
DR PaxDb; Q867X0; -.
DR PRIDE; Q867X0; -.
DR EnsemblMetazoa; F20C5.1a.1; F20C5.1a.1; WBGene00004051. [Q867X0-1]
DR EnsemblMetazoa; F20C5.1b.1; F20C5.1b.1; WBGene00004051. [Q867X0-2]
DR GeneID; 177683; -.
DR UCSC; F20C5.1a; c. elegans. [Q867X0-1]
DR CTD; 177683; -.
DR WormBase; F20C5.1a; CE33775; WBGene00004051; parg-1. [Q867X0-1]
DR WormBase; F20C5.1b; CE32867; WBGene00004051; parg-1. [Q867X0-2]
DR eggNOG; KOG2064; Eukaryota.
DR InParanoid; Q867X0; -.
DR BRENDA; 3.2.1.143; 1045.
DR Reactome; R-CEL-110362; POLB-Dependent Long Patch Base Excision Repair.
DR PRO; PR:Q867X0; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004051; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q867X0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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; ISS:UniProtKB.
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 Alternative splicing; DNA damage; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..781
FT /note="Poly(ADP-ribose) glycohydrolase 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000066605"
FT REGION 28..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 162
FT /note="Q -> QLSQ (in isoform b)"
FT /evidence="ECO:0000303|PubMed:17188026"
FT /id="VSP_051616"
FT VAR_SEQ 217..236
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:17188026"
FT /id="VSP_051617"
FT MUTAGEN 536
FT /note="D->N: No poly(ADP-ribose) glycohydrolase activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:17188026"
FT MUTAGEN 554
FT /note="E->N: Reduced poly(ADP-ribose) glycohydrolase
FT activity in vitro."
FT /evidence="ECO:0000269|PubMed:17188026"
FT MUTAGEN 555
FT /note="E->N: No poly(ADP-ribose) glycohydrolase activity in
FT vitro."
FT /evidence="ECO:0000269|PubMed:17188026"
FT MUTAGEN 594
FT /note="Y->A: Reduced poly(ADP-ribose) glycohydrolase
FT activity in vitro."
FT /evidence="ECO:0000269|PubMed:17188026"
SQ SEQUENCE 781 AA; 89274 MW; 30447D06605CED0A CRC64;
MSKKFIELGD PVTQDEKDYE DYVGVGFAHQ VPTMKRRKLT EHGNTTESKE DPEEPKSRDV
FVSSQSSDES QEDSAENPEI AKEVSENCEN LTETLKISNI ESLDNVTERS EHTLDNHKST
EPMEEDVNNK SNIDVAINSD EDDELVLEEN NKEMRDGEQV QQDLFADDQE LIEYPGIMKD
TTTQLDITDS EVETAQKMEM IEETEADSTF VGEDSKNQRQ SGTTSDEVDA DSQINLATKT
VRTSSSSFLS TVSTCEAPAK GRARMYQKEL EKHVIAFTEG NLTLQPDLNK VDPDRNYRYC
TIPNFPASQG KLREDNRYGP KIVLPQRWRE FDSRGRRRDS YFYFKRKLDG YLKCYKTTGY
FMFVGLLHNM WEFDPDITYK LPALEMYYKE MSELVGREEV LEKFARVARI AKTAEDILPE
RIYRLVGDVE SATLSHKQCA ALVARMFFAR PDSPFSFCRI LSSDKSICVE KLKFLFTYFD
KMSMDPPDGA VSFRLTKMDK DTFNEEWKDK KLRSLPEVEF FDEMLIEDTA LCTQVDFANE
HLGGGVLNHG SVQEEIRFLM CPEMMVGMLL CEKMKQLEAI SIVGAYVFSS YTGYGHTLKW
AELQPNHSRQ NTNEFRDRFG RLRVETIAID AILFKGSKLD CQTEQLNKAN IIREMKKASI
GFMSQGPKFT NIPIVTGWWG CGAFNGDKPL KFIIQVIAAG VADRPLHFCS FGEPELAAKC
KKIIERMKQK DVTLGMLFSM INNTGLPHKH FEFYVFDRIS TYLSSSEDVE SSKSSPSVSR
A
