PARP1_CAEEL
ID PARP1_CAEEL Reviewed; 945 AA.
AC Q9N4H4; Q8MZU4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Poly [ADP-ribose] polymerase 1 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.30 {ECO:0000255|PROSITE-ProRule:PRU00397, ECO:0000269|PubMed:12145714, ECO:0000269|PubMed:15923155};
DE AltName: Full=Poly ADP-ribose metabolism enzyme 1;
DE AltName: Full=Protein poly-ADP-ribosyltransferase parp-1 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
GN Name=parp-1 {ECO:0000312|WormBase:Y71F9AL.18};
GN Synonyms=pme-1 {ECO:0000303|PubMed:12145714,
GN ECO:0000312|WormBase:Y71F9AL.18};
GN ORFNames=Y71F9AL.18 {ECO:0000312|WormBase:Y71F9AL.18};
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.
RX PubMed=12600937; DOI=10.1101/gad.1060703;
RA Pothof J., van Haaften G., Thijssen K., Kamath R.S., Fraser A.G.,
RA Ahringer J., Plasterk R.H.A., Tijsterman M.;
RT "Identification of genes that protect the C. elegans genome against
RT mutations by genome-wide RNAi.";
RL Genes Dev. 17:443-448(2003).
RN [4]
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 (PubMed:15923155). Involved in
CC protection of the genome against mutations (PubMed:12600937).
CC {ECO:0000269|PubMed:12600937, 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:0000255|PROSITE-ProRule:PRU00397}.
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}.
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DR EMBL; AF499444; AAM27195.1; -; mRNA.
DR EMBL; BX284601; CCD73512.1; -; Genomic_DNA.
DR RefSeq; NP_491072.1; NM_058671.7.
DR AlphaFoldDB; Q9N4H4; -.
DR SMR; Q9N4H4; -.
DR BioGRID; 57311; 5.
DR STRING; 6239.Y71F9AL.18; -.
DR EPD; Q9N4H4; -.
DR PaxDb; Q9N4H4; -.
DR PeptideAtlas; Q9N4H4; -.
DR PRIDE; Q9N4H4; -.
DR EnsemblMetazoa; Y71F9AL.18a.1; Y71F9AL.18a.1; WBGene00004049.
DR EnsemblMetazoa; Y71F9AL.18a.2; Y71F9AL.18a.2; WBGene00004049.
DR GeneID; 266823; -.
DR KEGG; cel:CELE_Y71F9AL.18; -.
DR UCSC; Y71F9AL.18.1; c. elegans.
DR CTD; 266823; -.
DR WormBase; Y71F9AL.18; CE25556; WBGene00004049; parp-1.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000156058; -.
DR HOGENOM; CLU_004841_0_1_1; -.
DR InParanoid; Q9N4H4; -.
DR OMA; THNEYVI; -.
DR OrthoDB; 909382at2759; -.
DR PhylomeDB; Q9N4H4; -.
DR Reactome; R-CEL-110362; POLB-Dependent Long Patch Base Excision Repair.
DR Reactome; R-CEL-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-CEL-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-CEL-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-CEL-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-CEL-5696400; Dual Incision in GG-NER.
DR PRO; PR:Q9N4H4; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004049; Expressed in adult organism and 3 other tissues.
DR ExpressionAtlas; Q9N4H4; baseline and differential.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
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 Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.30.1740.10; -; 2.
DR InterPro; IPR012982; PADR1.
DR InterPro; IPR038650; PADR1_dom_sf.
DR InterPro; IPR008288; PARP.
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 InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR Pfam; PF08063; PADR1; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR Pfam; PF00645; zf-PARP; 1.
DR PIRSF; PIRSF000489; NAD_ADPRT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 2.
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; PS00347; PARP_ZN_FINGER_1; 1.
DR PROSITE; PS50064; PARP_ZN_FINGER_2; 1.
DR PROSITE; PS51977; WGR; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA-binding; Glycosyltransferase; Metal-binding;
KW NAD; Nucleotidyltransferase; Nucleus; Reference proteome; Repeat;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..945
FT /note="Poly [ADP-ribose] polymerase 1"
FT /id="PRO_0000211335"
FT DOMAIN 464..563
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 586..704
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 717..945
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ZN_FING 10..96
FT /note="PARP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT ZN_FING 117..183
FT /note="PARP-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT REGION 195..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 152..153
FT /note="FK -> LN (in Ref. 1; AAM27195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 945 AA; 108007 MW; 1D0A62C954BC6AD9 CRC64;
MIHSNEPLPY AIEYAKSGRS NCKTCKKNIA LDQLRMSMNR PSTFFDGNMD SWFHYNCFWI
KMIRGRDDIN ISSIRGVDWL RWEDQEKLRQ EIQHFKTASP PTLTPLCSTT TVILSTIKTE
KSLSNRGKCG KCGQNFERGE IKAHNKGKAN HFKCFLQEFD KISGTVEDIP GWADYEENFK
IKAVGEYVEA LAAKRRSTEP ATPASASPTP PEAETPVLSA EGSPESSNKR PASSEIIEID
GEGNPDENDF AKKRRMKKEA RLMEVQKKRM KKQSDLLWEY RQIFERMPYT DKISILRENE
QDIPEGHDPT AQVIERLVDN ALFGCPIICQ TCSNGKIVYN SSCRTYVCTG YATEYSKCTY
ESKNPIRTPF EVSHRLTEKH KLQDIVFNQM SERLYIGEED GESVVKIDKR KSKGGTRGEQ
FIYAAEAFDS TNNVPIKVGD LTSTNTHIIK KGTVVDAKFA LADRCHVFKN EIDGSLYQAT
LSFTDLTQNK NSYYKIQLLK DDQRENYYVF RSWGRVGTEV GGNKHESYSN SNEAILKFQD
VFHEKTKNDW IYRKHFRKMP GMFSYVETDY SEFAQITDTE ITPGSKTLLP KSVKEVVMSI
FDVENMKSAL KSFEMDVNKM PLGRLSHNQI NLAFEVLNDI SDLLVKLPID ASRILDFSNK
FYTIIPHNFG MRVPEPIDSF HKIKEKNNML NALLDIKFAY DQISGGDVPA STSLGIDPVD
INYQKLKCIM EPLQQGCDDW NMIHQYLKNT HGATHDLKVE LIDILKLNRD NESSKFKRHI
GNRRLLWHGS GKMNFAGILG QGLRIAPPEA PVSGYMFGKG VYFADMFSKS FFYCRANAKE
EAYLLLCDVA LGNVQQLMAS KNVSRQTLPA GFQSVQGLGR QCPREIGSYN HPDGYTIPLG
LTYMQLQGKQ DVDYHLLYNE FIVYDVDQIQ LKYLVRVKMH HARHL
