PARP1_ONCMA
ID PARP1_ONCMA Reviewed; 135 AA.
AC Q08824;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Poly [ADP-ribose] polymerase 1;
DE Short=PARP-1;
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 1;
DE Short=ARTD1;
DE AltName: Full=DNA ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 1;
DE Short=ADPRT 1;
DE AltName: Full=Poly[ADP-ribose] synthase 1;
DE AltName: Full=Protein poly-ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
DE Flags: Fragment;
GN Name=parp1; Synonyms=adprt;
OS Oncorhynchus masou (Cherry salmon) (Masu salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8020;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8503897; DOI=10.1006/bbrc.1993.1598;
RA Ozawa Y., Uchida K., Uchida M., Ami Y., Kushida S., Okada N., Miwa M.;
RT "Isolation of cDNAs encoding the catalytic domain of poly(ADP-ribose)
RT polymerase from Xenopus laevis and cherry salmon using heterologous
RT oligonucleotide consensus sequences.";
RL Biochem. Biophys. Res. Commun. 193:119-125(1993).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-
CC ribosylation of proteins and plays a key role in DNA repair. Mediates
CC glutamate, aspartate, serine or tyrosine ADP-ribosylation of proteins:
CC the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor
CC carboxyl group of target residues and further ADP-ribosyl groups are
CC transferred to the 2'-position of the terminal adenosine moiety,
CC building up a polymer with an average chain length of 20-30 units.
CC Serine ADP-ribosylation of proteins constitutes the primary form of
CC ADP-ribosylation of proteins in response to DNA damage. Mainly mediates
CC glutamate and aspartate ADP-ribosylation of target proteins in absence
CC of HPF1. Following interaction with HPF1, catalyzes serine ADP-
CC ribosylation of target proteins; HPF1 conferring serine specificity by
CC completing the PARP1 active site. Also catalyzes tyrosine ADP-
CC ribosylation of target proteins following interaction with HPF1. PARP1
CC initiates the repair of DNA breaks: recognizes and binds DNA breaks
CC within chromatin and recruits HPF1, licensing serine ADP-ribosylation
CC of target proteins, such as histones, thereby promoting decompaction of
CC chromatin and the recruitment of repair factors leading to the
CC reparation of DNA strand breaks. In addition to proteins, also able to
CC ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break
CC termini containing terminal phosphates and a 2'-OH group in single- and
CC double-stranded DNA, respectively. {ECO:0000250|UniProtKB:P09874}.
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:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142556; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58233;
CC Evidence={ECO:0000250|UniProtKB:P09874};
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:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC Evidence={ECO:0000250|UniProtKB:P09874};
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:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:58236, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:15092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:46858, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142557; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58237;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09874}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:P09874}. Chromosome
CC {ECO:0000250|UniProtKB:P09874}. Note=Localizes to sites of DNA damage.
CC {ECO:0000250|UniProtKB:P09874}.
CC -!- DOMAIN: The N-terminal disordered region does not act as a key DNA-
CC binding domain. The WGR and PARP catalytic domains function together to
CC recruit PARP1 to sites of DNA breaks. The N-terminal disordered region
CC is only required for activation on specific types of DNA damage.
CC {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- DOMAIN: The WGR domain bridges two nucleosomes, with the broken DNA
CC aligned in a position suitable for ligation. The bridging induces
CC structural changes in PARP1 that signal the recognition of a DNA break
CC to the catalytic domain of PARP1, promoting HPF1 recruitment and
CC subsequent activation of PARP1, licensing serine ADP-ribosylation of
CC target proteins. {ECO:0000250|UniProtKB:Q9UGN5}.
CC -!- PTM: Poly-ADP-ribosylated on glutamate and aspartate residues by
CC autocatalysis. {ECO:0000250|UniProtKB:P09874}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; D13809; BAA02965.1; -; mRNA.
DR PIR; PN0494; PN0494.
DR AlphaFoldDB; Q08824; -.
DR SMR; Q08824; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
DR GO; GO:0030592; P:DNA ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0018424; P:peptidyl-glutamic acid poly-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0018312; P:peptidyl-serine ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; ISS:UniProtKB.
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 Pfam; PF00644; PARP; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Chromosome; DNA damage; DNA repair; DNA-binding;
KW Glycosyltransferase; Metal-binding; NAD; Nucleotidyltransferase; Nucleus;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN <1..>135
FT /note="Poly [ADP-ribose] polymerase 1"
FT /id="PRO_0000211323"
FT DOMAIN <1..21
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 30..>135
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ACT_SITE 135
FT /evidence="ECO:0000250"
FT BINDING 104..106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT NON_TER 1
FT NON_TER 135
SQ SEQUENCE 135 AA; 15411 MW; A60E8E98890E42DC CRC64;
QAKVEMLDNL LDIEVAYSLL KGGAEDNKKD PIDINYEKLK TKIEVVDKTT KEAEIILQYV
KNTHAATHNT YTLVVEEIFK IVREGEYQKY RPFQDLPNRQ LLWHGSRATN YAGILSQGLR
IAPPEAPVTG YMFGK
