PARP2_CAEEL
ID PARP2_CAEEL Reviewed; 538 AA.
AC Q09525;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Poly [ADP-ribose] polymerase 2 {ECO:0000250|UniProtKB:Q9UGN5};
DE EC=2.4.2.30 {ECO:0000269|PubMed:12145714, ECO:0000269|PubMed:15923155};
DE AltName: Full=Poly ADP-ribose metabolism enzyme 2 {ECO:0000305};
DE AltName: Full=Protein poly-ADP-ribosyltransferase parp-2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
GN Name=parp-2 {ECO:0000312|WormBase:E02H1.4};
GN Synonyms=pme-2 {ECO:0000303|PubMed:12145714, ECO:0000312|WormBase:E02H1.4};
GN ORFNames=E02H1.4 {ECO:0000312|WormBase:E02H1.4};
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], CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12145714; DOI=10.1042/bj20020669;
RA Gagnon S.N., Hengartner M.O., Desnoyers S.;
RT "The genes pme-1 and pme-2 encode two poly(ADP-ribose) polymerases in
RT Caenorhabditis elegans.";
RL Biochem. J. 368:263-271(2002).
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=15923155; DOI=10.1016/j.dnarep.2005.04.015;
RA Dequen F., Gagnon S.N., Desnoyers S.;
RT "Ionizing radiations in Caenorhabditis elegans induce poly(ADP-
RT ribosyl)ation, a conserved DNA-damage response essential for survival.";
RL DNA Repair 4:814-825(2005).
CC -!- FUNCTION: Poly[ADP-ribose] polymerase modifies various nuclear proteins
CC by poly(ADP-ribosyl)ation, a post-translational modification
CC synthesized after DNA damage that appears as an obligatory step in a
CC detection/signaling pathway leading to the reparation of DNA strand
CC breaks and programmed cell death. {ECO:0000269|PubMed:15923155}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000269|PubMed:12145714, ECO:0000269|PubMed:15923155};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by N-(6-oxo-5,6-dihydrophenanthridin-2-
CC yl)-N,N-dimethylacetamide HCl (PJ34), 1,5-dihydroxyisoquinoline (DHQ)
CC and 3-aminobenzamide (3AB). {ECO:0000269|PubMed:15923155}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- DEVELOPMENTAL STAGE: Predominantly expressed at early embryonic stages
CC and later in L4 and adult stages. {ECO:0000269|PubMed:12145714}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {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; AF500111; AAM27196.1; -; mRNA.
DR EMBL; BX284602; CAA87379.1; -; Genomic_DNA.
DR PIR; T20414; T20414.
DR RefSeq; NP_001022057.1; NM_001026886.3.
DR AlphaFoldDB; Q09525; -.
DR SMR; Q09525; -.
DR BioGRID; 533285; 3.
DR IntAct; Q09525; 1.
DR MINT; Q09525; -.
DR STRING; 6239.E02H1.4; -.
DR EPD; Q09525; -.
DR PaxDb; Q09525; -.
DR PeptideAtlas; Q09525; -.
DR PRIDE; Q09525; -.
DR EnsemblMetazoa; E02H1.4.1; E02H1.4.1; WBGene00004050.
DR EnsemblMetazoa; E02H1.4.2; E02H1.4.2; WBGene00004050.
DR GeneID; 3565967; -.
DR KEGG; cel:CELE_E02H1.4; -.
DR UCSC; E02H1.4; c. elegans.
DR CTD; 3565967; -.
DR WormBase; E02H1.4; CE01539; WBGene00004050; parp-2.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000158452; -.
DR HOGENOM; CLU_004841_1_0_1; -.
DR InParanoid; Q09525; -.
DR OMA; SANYCCP; -.
DR OrthoDB; 909382at2759; -.
DR PhylomeDB; Q09525; -.
DR PRO; PR:Q09525; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004050; Expressed in embryo and 4 other tissues.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:WormBase.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:WormBase.
DR Gene3D; 1.20.142.10; -; 1.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR InterPro; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Glycosyltransferase; NAD; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Transferase.
FT CHAIN 1..538
FT /note="Poly [ADP-ribose] polymerase 2"
FT /id="PRO_0000211336"
FT DOMAIN 1..94
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 148..285
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 309..535
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 104..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 538 AA; 61268 MW; 3144E25465FC7341 CRC64;
MSIINDENGR GYKVHLCKTN IAQNNNKFYD MELLDEGGDF IVKLINGRIG YRGVTQLKDF
DDLDRAKKFF ESKFYEKTHL HWEERDDEPV PNKYAVVELA TNARQTEKEV KKEEPEPEPK
VDEKNTRGRK KRGIVKEKKE IKKEEEPVEE VNEKLKELMK CICDEDVHLG LLKQLKFNEA
FGRPIDCLSL AQLTTGYEIL SKIEESIGGK SARRSTRGRP RVADRVLAVK SDGPSLHDIN
KYYSLIPHSF GFCVPPKIDS HAKIQAEREL LDALKGSIEA SLELKDLKKT ASSKDIYQRL
YERLPCHLEP VSEEIAGKIG DCLAMRGPTH CYKLSLIDAF ELKDPNEIPT EAPVEVQEVP
KKRGRKSTKT AAPTVPPPTT KRLLWHGTRV TNVFSILMNG LQFPVGDRCG LMFGNGVYFA
NVPTKSANYC CPEASKRVFM LLCEVETANP LVLYESEIDA DEKMEKAKKT SVYAAGKHTP
RDTVEINGIP AFKSNLETIE EETRLLYDEY VMFNKEHFKI KYVVEVKVDR LTAKEMMA
