ID   PARP1_RAT               Reviewed;        1014 AA.
AC   P27008; O35937;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 214.
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   Contains:
DE     RecName: Full=Poly [ADP-ribose] polymerase 1, processed C-terminus {ECO:0000250|UniProtKB:P09874};
DE     AltName: Full=Poly [ADP-ribose] polymerase 1, 89-kDa form {ECO:0000250|UniProtKB:P09874};
DE   Contains:
DE     RecName: Full=Poly [ADP-ribose] polymerase 1, processed N-terminus {ECO:0000250|UniProtKB:P09874};
DE     AltName: Full=Poly [ADP-ribose] polymerase 1, 24-kDa form {ECO:0000250|UniProtKB:P09874};
GN   Name=Parp1; Synonyms=Adprt;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Monocyte;
RX   PubMed=9385436; DOI=10.1080/15216549700204571;
RA   Beneke S., Meyer R., Buerkle A.;
RT   "Isolation of cDNA encoding full-length rat (Rattus norvegicus) poly (ADP-
RT   ribose) polymerase.";
RL   Biochem. Mol. Biol. Int. 43:755-761(1997).
RN   [2]
RP   SEQUENCE REVISION TO 812.
RA   Beneke S., Meyer R., Buerkle A.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RC   STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX   PubMed=1601134; DOI=10.1016/0014-5793(92)80457-r;
RA   Potvin F., Thibodeau J., Kirkland J.B., Dandenault B., Duchaine C.,
RA   Poirier G.G.;
RT   "Structural analysis of the putative regulatory region of the rat gene
RT   encoding poly(ADP-ribose) polymerase.";
RL   FEBS Lett. 302:269-273(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 515-1014.
RC   STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX   PubMed=2508731; DOI=10.1139/o89-097;
RA   Thibodeau J., Gradwohl G., Dumas C., Clairoux-Moreau S., Brunet G.;
RT   "Cloning of rodent cDNA coding the poly(ADP-ribose) polymerase catalytic
RT   domain and analysis of mRNA levels during the cell cycle.";
RL   Biochem. Cell Biol. 67:653-660(1989).
RN   [6]
RP   INTERACTION WITH NR4A3.
RX   PubMed=25625556; DOI=10.1111/bph.13091;
RA   Feng X.J., Gao H., Gao S., Li Z., Li H., Lu J., Wang J.J., Huang X.Y.,
RA   Liu M., Zou J., Ye J.T., Liu P.Q.;
RT   "The orphan receptor NOR1 participates in isoprenaline-induced cardiac
RT   hypertrophy by regulating PARP-1.";
RL   Br. J. Pharmacol. 172:2852-2863(2015).
RN   [7] {ECO:0007744|PDB:2LE0}
RP   STRUCTURE BY NMR OF 389-487.
RX   PubMed=21967661; DOI=10.1186/1472-6807-11-37;
RA   Loeffler P.A., Cuneo M.J., Mueller G.A., DeRose E.F., Gabel S.A.,
RA   London R.E.;
RT   "Structural studies of the PARP-1 BRCT domain.";
RL   BMC Struct. Biol. 11:37-37(2011).
CC   -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-
CC       ribosylation of proteins and plays a key role in DNA repair (By
CC       similarity). Mediates glutamate, aspartate, serine, histidine or
CC       tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of
CC       NAD(+) is transferred to the acceptor carboxyl group of target residues
CC       and further ADP-ribosyl groups are transferred to the 2'-position of
CC       the terminal adenosine moiety, building up a polymer with an average
CC       chain length of 20-30 units. Serine ADP-ribosylation of proteins
CC       constitutes the primary form of ADP-ribosylation of proteins in
CC       response to DNA damage (By similarity). Specificity for the different
CC       amino acids is conferred by interacting factors, such as HPF1 and
CC       NMNAT1 (By similarity). Following interaction with HPF1, catalyzes
CC       serine ADP-ribosylation of target proteins; HPF1 confers serine
CC       specificity by completing the PARP1 active site. Also catalyzes
CC       tyrosine ADP-ribosylation of target proteins following interaction with
CC       HPF1 (By similarity). Following interaction with NMNAT1, catalyzes
CC       glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1
CC       confers glutamate and aspartate specificity (By similarity). 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 (H2BS6ADPr and H3S10ADPr), thereby
CC       promoting decompaction of chromatin and the recruitment of repair
CC       factors leading to the reparation of DNA strand breaks. HPF1 initiates
CC       serine ADP-ribosylation but restricts the polymerase activity of PARP1
CC       in order to limit the length of poly-ADP-ribose chains. In addition to
CC       base excision repair (BER) pathway, also involved in double-strand
CC       breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage
CC       sites and promotes homologous recombination repair by mediating poly-
CC       ADP-ribosylation. Mediates the poly-ADP-ribosylation of a number of
CC       proteins, including itself, APLF, CHFR and NFAT5. In addition to
CC       proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation
CC       of DNA strand break termini containing terminal phosphates and a 2'-OH
CC       group in single- and double-stranded DNA, respectively. Required for
CC       PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-
CC       DTX3L-mediated ubiquitination promotes the rapid and specific
CC       recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage
CC       sites (By similarity). PARP1-mediated DNA repair in neurons plays a
CC       role in sleep: senses DNA damage in neurons and promotes sleep,
CC       facilitating efficient DNA repair. In addition to DNA repair, also
CC       involved in other processes, such as transcription regulation,
CC       programmed cell death, membrane repair, adipogenesis and innate
CC       immunity (By similarity). Acts as a repressor of transcription: binds
CC       to nucleosomes and modulates chromatin structure in a manner similar to
CC       histone H1, thereby altering RNA polymerase II. Acts both as a positive
CC       and negative regulator of transcription elongation, depending on the
CC       context. Acts as a positive regulator of transcription elongation by
CC       mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding
CC       activity of NELFE and relieving transcription pausing. Acts as a
CC       negative regulator of transcription elongation in response to DNA
CC       damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the
CC       phase separation activity of CCNT1 and subsequent activation of CDK9.
CC       Involved in replication fork progression following interaction with
CC       CARM1: mediates poly-ADP-ribosylation at replication forks, slowing
CC       fork progression (By similarity). Poly-ADP-ribose chains generated by
CC       PARP1 also play a role in poly-ADP-ribose-dependent cell death, a
CC       process named parthanatos. Also acts as a negative regulator of the
CC       cGAS-STING pathway. Acts by mediating poly-ADP-ribosylation of CGAS:
CC       PARP1 translocates into the cytosol following phosphorylation by PRKDC
CC       and catalyzes poly-ADP-ribosylation and inactivation of CGAS. Acts as a
CC       negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of
CC       histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1,
CC       inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby
CC       blocking expression of pro-adipogenetic genes (By similarity). Involved
CC       in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and
CC       NUDT5. Nuclear ATP generation is required for extensive chromatin
CC       remodeling events that are energy-consuming (By similarity).
CC       {ECO:0000250|UniProtKB:P09874, ECO:0000250|UniProtKB:P11103}.
CC   -!- FUNCTION: [Poly [ADP-ribose] polymerase 1, processed C-terminus]:
CC       Promotes AIFM1-mediated apoptosis. This form, which translocates into
CC       the cytoplasm following cleavage by caspase-3 (CASP3) and caspase-7
CC       (CASP7) in response to apoptosis, is auto-poly-ADP-ribosylated and
CC       serves as a poly-ADP-ribose carrier to induce AIFM1-mediated apoptosis.
CC       {ECO:0000250|UniProtKB:P09874}.
CC   -!- FUNCTION: [Poly [ADP-ribose] polymerase 1, processed N-terminus]: This
CC       cleavage form irreversibly binds to DNA breaks and interferes with DNA
CC       repair, promoting DNA damage-induced apoptosis.
CC       {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:P11103};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425;
CC         Evidence={ECO:0000250|UniProtKB:P11103};
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:P11103};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225;
CC         Evidence={ECO:0000250|UniProtKB:P11103};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + NAD(+) = H(+) + N(tele)-(ADP-D-
CC         ribosyl)-L-histidyl-[protein] + nicotinamide; Xref=Rhea:RHEA:72071,
CC         Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:18085, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29979, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:191398; Evidence={ECO:0000250|UniProtKB:P09874};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72072;
CC         Evidence={ECO:0000250|UniProtKB:P09874};
CC   -!- ACTIVITY REGULATION: ADP-ribosyltransferase activity is regulated via
CC       an allosteric activation mechanism. In absence of activation signal,
CC       PARP1 is autoinhibited by the PARP alpha-helical domain (also named HD
CC       region), which prevents effective NAD(+)-binding. Activity is highly
CC       stimulated by signals, such as DNA strand breaks. Binding to damaged
CC       DNA unfolds the PARP alpha-helical domain, relieving autoinhibition.
CC       Poly-ADP-ribosyltransferase activity is tightly regulated and PARP1 is
CC       removed from damaged chromatin following initial poly-ADP-ribosylation
CC       of chromatin to avoid prolonged residence (trapping) that has cytotoxic
CC       consequences. A number of factors (VCP/p97) or post-translational
CC       modifications (auto-poly-ADP-ribosylation or ubiquitination) promote
CC       PARP1 removal from chromatin. {ECO:0000250|UniProtKB:P09874}.
CC   -!- SUBUNIT: Homodimer; PARP-type zinc-fingers from separate PARP1
CC       molecules form a dimer module that specifically recognizes DNA strand
CC       breaks (By similarity). Heterodimer; heterodimerizes with PARP2 (By
CC       similarity). Interacts (via the PARP catalytic domain) with HPF1 (By
CC       similarity). Interacts with NMNAT1 (By similarity). Interacts with
CC       nucleosomes; with a preference for nucleosomes containing H2A.X.
CC       Interacts with APTX (By similarity). Component of a base excision
CC       repair (BER) complex, containing at least XRCC1, PARP1, PARP2, POLB and
CC       LRIG3 (By similarity). Interacts with SRY (By similarity). The SWAP
CC       complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2
CC       (By similarity). Interacts with PARP3; leading to activate PARP1 in
CC       absence of DNA. Interacts (when poly-ADP-ribosylated) with CHD1L (via
CC       macro domain). Interacts with the DNA polymerase alpha catalytic
CC       subunit POLA1; this interaction functions as part of the control of
CC       replication fork progression. Interacts with EEF1A1 and TXK (By
CC       similarity). Interacts with RNF4 (By similarity). Interacts with RNF146
CC       (By similarity). Interacts with ZNF423 (By similarity). Interacts with
CC       APLF (By similarity). Interacts with SNAI1 (via zinc fingers); the
CC       interaction requires SNAI1 to be poly-ADP-ribosylated and non-
CC       phosphorylated (active) by GSK3B (By similarity). Interacts (when poly-
CC       ADP-ribosylated) with PARP9 (By similarity). Interacts with NR4A3;
CC       activates PARP1 by improving acetylation of PARP1 and suppressing the
CC       interaction between PARP1 and SIRT1 (PubMed:25625556). Interacts (via
CC       catalytic domain) with PUM3; the interaction inhibits the poly-ADP-
CC       ribosylation activity of PARP1 and the degradation of PARP1 by CASP3
CC       following genotoxic stress. Interacts with ZNF365. Interacts with
CC       RRP1B. Interacts with TIMELESS; the interaction is direct. Interacts
CC       with CGAS; leading to impede the formation of the PARP1-TIMELESS
CC       complex. Interacts with KHDC3L, the interaction is increased following
CC       the formation of DNA double-strand breaks (By similarity). Interacts
CC       (when auto-poly-ADP-ribosylated) with XRCC1; leading to inhibit PARP1
CC       ADP-ribosyltransferase activity. Interacts with SPINDOC; promoting
CC       PARP1 ADP-ribosyltransferase activity. Interacts with BANF1; leading to
CC       inhibit PARP1 ADP-ribosyltransferase activity in response to oxidative
CC       DNA damage. Interacts (when sumoylated and ubiquitinated) with VCP/p97;
CC       leading to its extraction from chromatin. Interacts with YARS1;
CC       promoting PARP1 ADP-ribosyltransferase activity. Interacts with PACMP
CC       micropeptide; Interacts with PACMP micropeptide; interaction (By
CC       similarity). Interacts (when poly-ADP-ribosylated) with isoform 1 of
CC       MACROH2A1; MACROH2A1 specifically binds to poly-ADP-ribose chains and
CC       inhibits PARP1 activity, limiting the consumption of nuclear NAD(+) (By
CC       similarity). Interacts with CARM1; promoting recruitment to replication
CC       forks (By similarity). Interacts with RECQL (By similarity). Interacts
CC       with ZNF32; the interaction reshapes ZNF432 interacting proteins (By
CC       similarity). {ECO:0000250|UniProtKB:P09874,
CC       ECO:0000250|UniProtKB:P11103, ECO:0000269|PubMed:25625556}.
CC   -!- SUBUNIT: [Poly [ADP-ribose] polymerase 1, processed C-terminus]:
CC       Interacts (when auto-poly-ADP-ribosylated) with AIFM1.
CC       {ECO:0000250|UniProtKB:P09874}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:P09874}.
CC       Nucleus {ECO:0000250|UniProtKB:P09874}. Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P09874}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P09874}. Note=Localizes to sites of DNA damage.
CC       Recognizes (via PARP-type zinc-fingers) and binds DNA strand breaks.
CC       Also binds normal/undamaged chromatin. Auto poly-ADP-ribosylation
CC       promotes dissociation from chromatin. Extracted from chromatin by
CC       VCP/p97 following sumoylation and ubiquitination. Translocates from the
CC       nucleus to the cytosol following phosphorylation by PRKDC. Recruited to
CC       replication forks following interaction with CARM1.
CC       {ECO:0000250|UniProtKB:P09874}.
CC   -!- SUBCELLULAR LOCATION: [Poly [ADP-ribose] polymerase 1, processed N-
CC       terminus]: Chromosome {ECO:0000250|UniProtKB:P09874}. Note=Following
CC       cleavage by caspase-3 (CASP3) and caspase-7 (CASP7) in response to
CC       apoptosis, this cleavage form irreversibly binds to DNA breaks.
CC       {ECO:0000250|UniProtKB:P09874}.
CC   -!- SUBCELLULAR LOCATION: [Poly [ADP-ribose] polymerase 1, processed C-
CC       terminus]: Cytoplasm {ECO:0000250|UniProtKB:P09874}. Note=Following
CC       cleavage by caspase-3 (CASP3) and caspase-7 (CASP7) in response to
CC       apoptosis, translocates into the cytoplasm, where the auto-poly-ADP-
CC       ribosylated form serves as a poly-ADP-ribose carrier to induce AIFM1-
CC       mediated apoptosis. {ECO:0000250|UniProtKB:P09874}.
CC   -!- DOMAIN: The two PARP-type zinc-fingers (also named Zn1 and Zn2)
CC       specifically recognize DNA strand breaks: PARP-type zinc-finger 1 binds
CC       PARP-type zinc-finger 2 from a separate PARP1 molecule to form a
CC       dimeric module that specifically recognizes DNA strand breaks.
CC       {ECO:0000250|UniProtKB:P09874}.
CC   -!- DOMAIN: The PADR1-type (also named Zn3) zinc-finger mediates an
CC       interdomain contact and is required for the ability of PARP1 to
CC       regulate chromatin structure. {ECO:0000250|UniProtKB:P09874}.
CC   -!- DOMAIN: The BRCT domain is able to bind intact DNA without activating
CC       the poly-ADP-ribosyltransferase activity. The BRCT domain mediates DNA
CC       intrastrand transfer (named 'monkey-bar mechanism') that allows rapid
CC       movements of PARP1 through the nucleus. {ECO:0000250|UniProtKB:P09874}.
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   -!- DOMAIN: The PARP alpha-helical domain (also named HD region) prevents
CC       effective NAD(+)-binding in absence of activation signal. Binding to
CC       damaged DNA unfolds the PARP alpha-helical domain, relieving
CC       autoinhibition. {ECO:0000250|UniProtKB:P09874}.
CC   -!- PTM: Poly-ADP-ribosylated on serine, glutamate and aspartate residues
CC       by autocatalysis. Auto-ADP-ribosylation on serine takes place following
CC       interaction with HPF1. Auto poly-ADP-ribosylation on serine residues
CC       promotes its dissociation from chromatin. Poly-ADP-ribosylated by
CC       PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA
CC       damage sites (By similarity). Mono-ADP-ribosylated at Lys-521 by SIRT6
CC       in response to oxidative stress, promoting recruitment to double-strand
CC       breaks (DSBs) sites (By similarity). {ECO:0000250|UniProtKB:P09874,
CC       ECO:0000250|UniProtKB:P11103}.
CC   -!- PTM: S-nitrosylated, leading to inhibit transcription regulation
CC       activity. {ECO:0000250|UniProtKB:P11103}.
CC   -!- PTM: Phosphorylated at Thr-594 by PRKDC in response to DNA damage
CC       following virus infection, promoting its translocation to the cytosol.
CC       Phosphorylated by TXK. {ECO:0000250|UniProtKB:P09874}.
CC   -!- PTM: Proteolytically cleaved by caspase-3 (CASP3) and caspase-7 (CASP7)
CC       in response to apoptosis to generate the Poly [ADP-ribose] polymerase
CC       1, processed N-terminus and Poly [ADP-ribose] polymerase 1, processed
CC       C-terminus forms. {ECO:0000250|UniProtKB:P09874}.
CC   -!- PTM: Sumoylated with SUMO1 or SUMO2 by PIAS4 following prolonged
CC       residence (trapping) to chromatin. Sumoylation promotes ubiquitination
CC       by RNF4 and removal from chromatin by VCP/p97.
CC       {ECO:0000250|UniProtKB:P09874}.
CC   -!- PTM: Ubiquitinated by RNF4 following sumoylation by PIAS4 in response
CC       to prolonged residence (trapping) to chromatin. Ubiquitination promotes
CC       removal from chromatin by VCP/p97. {ECO:0000250|UniProtKB:P09874}.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01351, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA46478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U94340; AAC53544.1; -; mRNA.
DR   EMBL; BC085765; AAH85765.1; -; mRNA.
DR   EMBL; X65496; CAA46477.1; -; Genomic_DNA.
DR   EMBL; X65497; CAA46478.1; ALT_INIT; Genomic_DNA.
DR   PIR; S21163; S21163.
DR   PIR; S26057; S26057.
DR   RefSeq; NP_037195.1; NM_013063.2.
DR   PDB; 2LE0; NMR; -; A=389-487.
DR   PDBsum; 2LE0; -.
DR   AlphaFoldDB; P27008; -.
DR   SMR; P27008; -.
DR   BioGRID; 247621; 19.
DR   IntAct; P27008; 1.
DR   MINT; P27008; -.
DR   STRING; 10116.ENSRNOP00000004232; -.
DR   BindingDB; P27008; -.
DR   ChEMBL; CHEMBL4664; -.
DR   CarbonylDB; P27008; -.
DR   iPTMnet; P27008; -.
DR   PhosphoSitePlus; P27008; -.
DR   jPOST; P27008; -.
DR   PaxDb; 10116-ENSRNOP00000004232; -.
DR   Ensembl; ENSRNOT00000004232.6; ENSRNOP00000004232.3; ENSRNOG00000003084.6.
DR   Ensembl; ENSRNOT00055021223; ENSRNOP00055017164; ENSRNOG00055012447.
DR   Ensembl; ENSRNOT00060011409; ENSRNOP00060008533; ENSRNOG00060006959.
DR   Ensembl; ENSRNOT00065041544; ENSRNOP00065033940; ENSRNOG00065024216.
DR   GeneID; 25591; -.
DR   KEGG; rno:25591; -.
DR   UCSC; RGD:2053; rat.
DR   AGR; RGD:2053; -.
DR   CTD; 142; -.
DR   RGD; 2053; Parp1.
DR   eggNOG; KOG1037; Eukaryota.
DR   GeneTree; ENSGT00940000156058; -.
DR   HOGENOM; CLU_004841_0_0_1; -.
DR   InParanoid; P27008; -.
DR   OMA; MNFKYKY; -.
DR   OrthoDB; 5481368at2759; -.
DR   PhylomeDB; P27008; -.
DR   TreeFam; TF316616; -.
DR   Reactome; R-RNO-110362; POLB-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-RNO-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-RNO-5685939; HDR through MMEJ (alt-NHEJ).
DR   Reactome; R-RNO-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-RNO-5696400; Dual Incision in GG-NER.
DR   PRO; PR:P27008; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003084; Expressed in heart and 19 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR   GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:RGD.
DR   GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0032993; C:protein-DNA complex; ISO:RGD.
DR   GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0051287; F:NAD binding; IDA:RGD.
DR   GO; GO:0140294; F:NAD DNA ADP-ribosyltransferase activity; ISO:RGD.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:RGD.
DR   GO; GO:0140806; F:NAD+- protein-aspartate ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0140822; F:NAD+-histone H2BE35 glutamate ADP-ribosyltransferase activity; ISO:RGD.
DR   GO; GO:0140816; F:NAD+-histone H2BS6 serine ADP-ribosyltransferase activity; ISO:RGD.
DR   GO; GO:0140817; F:NAD+-histone H3S10 serine ADP-ribosyltransferase activity; ISO:RGD.
DR   GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0140807; F:NAD+-protein-glutamate ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0140815; F:NAD+-protein-histidine ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0140805; F:NAD+-protein-serine ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0140808; F:NAD+-protein-tyrosine ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:RGD.
DR   GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016763; F:pentosyltransferase activity; NAS:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0140537; F:transcription regulator activator activity; IDA:ARUK-UCL.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
DR   GO; GO:0006284; P:base-excision repair; ISO:RGD.
DR   GO; GO:0048148; P:behavioral response to cocaine; ISO:RGD.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IDA:RGD.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IMP:RGD.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:RGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR   GO; GO:0071451; P:cellular response to superoxide; ISO:RGD.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR   GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR   GO; GO:0071294; P:cellular response to zinc ion; IEP:RGD.
DR   GO; GO:0046697; P:decidualization; ISS:UniProtKB.
DR   GO; GO:0030592; P:DNA ADP-ribosylation; ISS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; IDA:RGD.
DR   GO; GO:0006259; P:DNA metabolic process; ISO:RGD.
DR   GO; GO:0006281; P:DNA repair; ISO:RGD.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0032042; P:mitochondrial DNA metabolic process; ISO:RGD.
DR   GO; GO:0043504; P:mitochondrial DNA repair; ISO:RGD.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR   GO; GO:1904178; P:negative regulation of adipose tissue development; ISO:RGD.
DR   GO; GO:2001170; P:negative regulation of ATP biosynthetic process; ISO:RGD.
DR   GO; GO:0160049; P:negative regulation of cGAS/STING signaling pathway; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB.
DR   GO; GO:0032700; P:negative regulation of interleukin-17 production; ISO:RGD.
DR   GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0034244; P:negative regulation of transcription elongation by RNA polymerase II; ISO:RGD.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:RGD.
DR   GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:UniProtKB.
DR   GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISO:RGD.
DR   GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:RGD.
DR   GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IMP:RGD.
DR   GO; GO:1904762; P:positive regulation of myofibroblast differentiation; IMP:RGD.
DR   GO; GO:0060545; P:positive regulation of necroptotic process; ISS:UniProtKB.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:RGD.
DR   GO; GO:1903518; P:positive regulation of single strand break repair; ISO:RGD.
DR   GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IMP:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR   GO; GO:0016540; P:protein autoprocessing; IDA:RGD.
DR   GO; GO:0071168; P:protein localization to chromatin; ISO:RGD.
DR   GO; GO:0036211; P:protein modification process; ISO:RGD.
DR   GO; GO:0070212; P:protein poly-ADP-ribosylation; ISS:UniProtKB.
DR   GO; GO:1905051; P:regulation of base-excision repair; ISO:RGD.
DR   GO; GO:0045188; P:regulation of circadian sleep/wake cycle, non-REM sleep; ISS:UniProtKB.
DR   GO; GO:0044030; P:regulation of DNA methylation; IMP:RGD.
DR   GO; GO:0040009; P:regulation of growth rate; ISO:RGD.
DR   GO; GO:1903376; P:regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IMP:RGD.
DR   GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR   GO; GO:1903516; P:regulation of single strand break repair; ISO:RGD.
DR   GO; GO:0071932; P:replication fork reversal; ISS:UniProtKB.
DR   GO; GO:1904044; P:response to aldosterone; IEP:RGD.
DR   GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
DR   GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0000723; P:telomere maintenance; ISO:RGD.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0050882; P:voluntary musculoskeletal movement; ISO:RGD.
DR   CDD; cd17747; BRCT_PARP1; 1.
DR   CDD; cd01437; parp_like; 1.
DR   CDD; cd08001; WGR_PARP1_like; 1.
DR   Gene3D; 1.10.20.130; -; 1.
DR   Gene3D; 2.20.25.630; -; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR   Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 2.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR038650; PADR1_C_dom_sf.
DR   InterPro; IPR008288; PARP.
DR   InterPro; IPR049296; PARP1-like_PADR1_N.
DR   InterPro; IPR012982; PARP1-like_PADR1_Zn_ribbon.
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   PANTHER; PTHR10459; DNA LIGASE; 1.
DR   PANTHER; PTHR10459:SF112; POLY [ADP-RIBOSE] POLYMERASE 1; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF21728; PADR1_N; 1.
DR   Pfam; PF08063; PADR1_Zn_ribbon; 1.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF02877; PARP_reg; 1.
DR   Pfam; PF05406; WGR; 1.
DR   Pfam; PF00645; zf-PARP; 2.
DR   PIRSF; PIRSF000489; NAD_ADPRT; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM01335; PADR1; 1.
DR   SMART; SM00773; WGR; 1.
DR   SMART; SM01336; zf-PARP; 2.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   SUPFAM; SSF142921; WGR domain-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS52007; PADR1; 1.
DR   PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS51977; WGR; 1.
DR   PROSITE; PS00347; ZF_PARP_1; 2.
DR   PROSITE; PS50064; ZF_PARP_2; 2.
DR   Genevisible; P27008; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ADP-ribosylation; Allosteric enzyme; Apoptosis;
KW   Chromosome; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW   Glycosyltransferase; Immunity; Innate immunity; Isopeptide bond;
KW   Metal-binding; NAD; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CHAIN           2..1014
FT                   /note="Poly [ADP-ribose] polymerase 1"
FT                   /id="PRO_0000211321"
FT   CHAIN           2..214
FT                   /note="Poly [ADP-ribose] polymerase 1, processed N-
FT                   terminus"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT                   /id="PRO_0000456365"
FT   CHAIN           215..1014
FT                   /note="Poly [ADP-ribose] polymerase 1, processed C-
FT                   terminus"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT                   /id="PRO_0000456366"
FT   DOMAIN          225..360
FT                   /note="PADR1 zinc-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01351"
FT   DOMAIN          386..477
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          542..638
FT                   /note="WGR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT   DOMAIN          662..779
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT   DOMAIN          788..1014
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT   ZN_FING         9..93
FT                   /note="PARP-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   ZN_FING         113..203
FT                   /note="PARP-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   REGION          291..333
FT                   /note="Zinc ribbon"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01351"
FT   REGION          357..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..524
FT                   /note="Automodification domain"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   REGION          496..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           207..209
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOTIF           221..226
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   ACT_SITE        988
FT                   /note="For poly [ADP-ribose] polymerase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01351"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01351"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01351"
FT   BINDING         322
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01351"
FT   BINDING         862..864
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT   BINDING         871
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT   BINDING         878
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT   BINDING         904
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGN5"
FT   SITE            214..215
FT                   /note="Cleavage; by caspase-3 and caspase-7"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         41
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         97
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         105
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         131
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         388
FT                   /note="PolyADP-ribosyl aspartic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         408
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         414
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         436
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         438
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         445
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         446
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         457
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         485
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         489
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         492
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         500
FT                   /note="ADP-ribosylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         504
FT                   /note="ADP-ribosylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         507
FT                   /note="ADP-ribosylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         513
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         514
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         519
FT                   /note="ADP-ribosylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         520
FT                   /note="PolyADP-ribosyl glutamic acid"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         521
FT                   /note="N6-(ADP-ribosyl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         594
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         600
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         621
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         782
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   MOD_RES         786
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        192
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        203
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        203
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        250
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        468
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        487
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        487
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        512
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        528
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        748
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CROSSLNK        748
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P09874"
FT   CONFLICT        639
FT                   /note="Y -> H (in Ref. 5; CAA46478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        642
FT                   /note="E -> A (in Ref. 5; CAA46478)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        753
FT                   /note="N -> D (in Ref. 5; CAA46478)"
FT                   /evidence="ECO:0000305"
FT   STRAND          394..398
FT                   /evidence="ECO:0007829|PDB:2LE0"
FT   HELIX           406..416
FT                   /evidence="ECO:0007829|PDB:2LE0"
FT   STRAND          422..424
FT                   /evidence="ECO:0007829|PDB:2LE0"
FT   STRAND          427..431
FT                   /evidence="ECO:0007829|PDB:2LE0"
FT   HELIX           434..439
FT                   /evidence="ECO:0007829|PDB:2LE0"
FT   HELIX           442..449
FT                   /evidence="ECO:0007829|PDB:2LE0"
FT   STRAND          453..455
FT                   /evidence="ECO:0007829|PDB:2LE0"
FT   HELIX           458..465
FT                   /evidence="ECO:0007829|PDB:2LE0"
FT   HELIX           470..476
FT                   /evidence="ECO:0007829|PDB:2LE0"
SQ   SEQUENCE   1014 AA;  112660 MW;  BE1B6F2B29B887ED CRC64;
     MAEATERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV
     GHSIRQPDTE VDGFSELRWD DQQKVKKTAE AGGVAGKGQH GGGGKAEKTL GDFAAEYAKS
     NRSTCKGCME KIEKGQMRLS KKMLDPEKPQ LGMIDRWYHP TCFVKNRDEL GFRPEYSASQ
     LKGFSLLSAE DKEALKKQLP AVKSEGKRKC DEVDGIDEVA KKKSKKGKDK ESSKLEKALK
     AQNELVWNIK DELKKACSTN DLKELLIFNQ QQVPSGESAI LDRVADGMAF GALLPCKECS
     GQLVFKSDAY YCTGDVTAWT KCMVKTQNPS RKEWVTPKEF REISYLKKLK IKKQDRLFPP
     ESSAPAPPAP PVSITSAPTA VNSSAPADKP LSNMKILTLG KLSQNKDEAK AMIEKLGGKL
     TGSANKASLC ISTKKEVEKM SKKMEEVKAA NVRVVCEDFL QDVSASAKSL QELLSAHSLS
     SWGAEVKVEP GEVVVPKGKS AAPSKKSKGA VKEEGVNKSE KRMKLTLKGG AAVDPDSGLE
     HSAHVLEKGG KVFSATLGLV DIVKGTNSYY KLQLLESDKE SRYWIFRSWG RVGTVIGSNK
     LEQMPSKEDA VEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE AVKKLAVKPG
     TKSKLPKPVQ ELVGMIFDVE SMKKALVEYE IDLQKMPLGK LSRRQIQAAY SILSEVQQAV
     SQGSSESQIL DLSNRFYTLI PHDFGMKKPP LLNNTDSVQA KVEMLDNLLD IEVAYSLLRG
     GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEVIRKYVKN THATTHNAYD LEVIDIFKIE
     REGESQRYKP FRQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM
     VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTAPDPSA
     SITLDGVEVP LGTGIPSGVN DTCLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW
//