ID   PARP1_ARATH             Reviewed;         983 AA.
AC   Q9ZP54; Q9SJW4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 2.
DT   02-SEP-2026, entry version 178.
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=NAD(+) ADP-ribosyltransferase 1;
DE            Short=ADPRT-1;
DE   AltName: Full=Poly[ADP-ribose] synthase 1;
DE   AltName: Full=Protein ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874};
DE            EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
GN   Name=PARP1; OrderedLocusNames=At2g31320; ORFNames=F16D14.16;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=11523787; DOI=10.1007/s004380100506;
RA   Doucet-Chabeaud G., Godon C., Brutesco C., de Murcia G., Kazmaier M.;
RT   "Ionising radiation induces the expression of PARP-1 and PARP-2 genes in
RT   Arabidopsis.";
RL   Mol. Genet. Genomics 265:954-963(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   STRUCTURE BY NMR OF 5-105.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the first Zn-finger domain of poly(ADP-ribose)
RT   polymerase-1.";
RL   Submitted (FEB-2005) to the PDB data bank.
CC   -!- FUNCTION: Involved in the base excision repair (BER) pathway, by
CC       catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor
CC       proteins involved in chromatin architecture and in DNA metabolism. This
CC       modification follows DNA damages and appears as an obligatory step in a
CC       detection/signaling pathway leading to the reparation of DNA strand
CC       breaks (By similarity). {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-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   -!- 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00264}.
CC   -!- INDUCTION: By ionising radiation (IR)-induced DNA damage.
CC       {ECO:0000269|PubMed:11523787}.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01351, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD20677.1; Type=Erroneous gene model prediction; Evidence={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; AJ131705; CAA10482.1; -; mRNA.
DR   EMBL; AC006593; AAD20677.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC08527.1; -; Genomic_DNA.
DR   EMBL; OZ408684; CAO7037021.1; -; Genomic_DNA.
DR   EMBL; AY091061; AAM13882.1; -; mRNA.
DR   EMBL; AY150460; AAN12901.1; -; mRNA.
DR   PIR; C84719; C84719.
DR   PIR; T51353; T51353.
DR   RefSeq; NP_850165.1; NM_179834.2.
DR   PDB; 1V9X; NMR; -; A=5-105.
DR   AlphaFoldDB; Q9ZP54; -.
DR   SMR; Q9ZP54; -.
DR   BioGRID; 3038; 6.
DR   FunCoup; Q9ZP54; 2228.
DR   STRING; 3702.Q9ZP54; -.
DR   iPTMnet; Q9ZP54; -.
DR   PaxDb; 3702-Q9ZP54; -.
DR   ProteomicsDB; 236282; -.
DR   GeneID; 817690; -.
DR   KEGG; ath:AT2G31320; -.
DR   Araport; AT2G31320; -.
DR   TAIR; AT2G31320; PARP1.
DR   eggNOG; KOG1037; Eukaryota.
DR   HOGENOM; CLU_004841_0_1_1; -.
DR   InParanoid; Q9ZP54; -.
DR   OMA; MNFKYKY; -.
DR   PhylomeDB; Q9ZP54; -.
DR   EvolutionaryTrace; Q9ZP54; -.
DR   PRO; PR:Q9ZP54; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISM:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0003950; F:NAD+ poly-ADP-ribosyltransferase activity; IDA:TAIR.
DR   GO; GO:1990404; F:NAD+-protein mono-ADP-ribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0140806; F:NAD+-protein-aspartate ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0140807; F:NAD+-protein-glutamate ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030592; P:DNA ADP-ribosylation; IDA:TAIR.
DR   GO; GO:0006281; P:DNA repair; IEP:TAIR.
DR   GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:TAIR.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR   CDD; cd01437; parp_like; 1.
DR   CDD; cd08001; WGR_PARP1_like; 1.
DR   FunFam; 1.10.20.130:FF:000001; Poly [ADP-ribose] polymerase; 1.
DR   FunFam; 1.20.142.10:FF:000002; Poly [ADP-ribose] polymerase; 1.
DR   FunFam; 2.20.25.630:FF:000001; Poly [ADP-ribose] polymerase; 1.
DR   FunFam; 3.30.1740.10:FF:000004; Poly [ADP-ribose] polymerase; 1.
DR   FunFam; 3.30.1740.10:FF:000005; Poly [ADP-ribose] polymerase; 1.
DR   FunFam; 3.40.50.10190:FF:000051; Poly [ADP-ribose] polymerase; 1.
DR   FunFam; 3.90.228.10:FF:000002; Poly [ADP-ribose] polymerase; 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; IPR050800; ARTD/PARP.
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:SF80; POLY [ADP-RIBOSE] POLYMERASE 1; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF21728; PADR1_N; 1.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF02877; PARP_reg; 1.
DR   Pfam; PF05406; WGR; 1.
DR   Pfam; PF00645; zf-PARP; 2.
DR   Pfam; PF08063; Zn_ribbon_PADR1; 1.
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; PS50064; ZF_PARP_2; 2.
DR   PDBsum; 1V9X; -.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; DNA-binding; Glycosyltransferase;
KW   Metal-binding; NAD; Nucleotidyltransferase; Nucleus; Reference proteome;
KW   Repeat; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..983
FT                   /note="Poly [ADP-ribose] polymerase 1"
FT                   /id="PRO_0000211331"
FT   DOMAIN          236..375
FT                   /note="PADR1 zinc-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01351"
FT   DOMAIN          394..484
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          511..611
FT                   /note="WGR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT   DOMAIN          633..751
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT   DOMAIN          758..983
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT   ZN_FING         8..91
FT                   /note="PARP-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   ZN_FING         114..194
FT                   /note="PARP-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   REGION          197..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..345
FT                   /note="Zinc ribbon"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01351"
FT   REGION          369..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT   BINDING         156
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         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01351"
FT   BINDING         309
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         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01351"
FT   STRAND          7..12
FT                   /evidence="ECO:0007829|PDB:1V9X"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:1V9X"
FT   STRAND          29..36
FT                   /evidence="ECO:0007829|PDB:1V9X"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:1V9X"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:1V9X"
FT   HELIX           53..57
FT                   /evidence="ECO:0007829|PDB:1V9X"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:1V9X"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:1V9X"
FT   TURN            71..74
FT                   /evidence="ECO:0007829|PDB:1V9X"
FT   HELIX           77..87
FT                   /evidence="ECO:0007829|PDB:1V9X"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:1V9X"
SQ   SEQUENCE   983 AA;  111233 MW;  468E12A8EF1B6F4F CRC64;
     MASPHKPWRA EYAKSSRSSC KTCKSVINKE NFRLGKLVQS THFDGIMPMW NHASCILKKT
     KQIKSVDDVE GIESLRWEDQ QKIRKYVESG AGSNTSTSTG TSTSSTANNA KLEYGIEVSQ
     TSRAGCRKCS EKILKGEVRI FSKPEGPGNK GLMWHHAKCF LEMSSSTELE SLSGWRSIPD
     SDQEALLPLV KKALPAAKTE TAEARQTNSR AGTKRKNDSV DNEKSKLAKS SFDMSTSGAL
     QPCSKEKEME AQTKELWDLK DDLKKYVTSA ELREMLEVNE QSTRGSELDL RDKCADGMMF
     GPLALCPMCS GHLSFSGGLY RCHGYISEWS KCSHSTLDPD RIKGKWKIPD ETENQFLLKW
     NKSQKSVKPK RILRPVLSGE TSQGQGSKDA TDSSRSERLA DLKVSIAGNT KERQPWKKRI
     EEAGAEFHAN VKKGTSCLVV CGLTDIRDAE MRKARRMKVA IVREDYLVDC FKKQRKLPFD
     KYKIEDTSES LVTVKVKGRS AVHEASGLQE HCHILEDGNS IYNTTLSMSD LSTGINSYYI
     LQIIQEDKGS DCYVFRKWGR VGNEKIGGNK VEEMSKSDAV HEFKRLFLEK TGNTWESWEQ
     KTNFQKQPGK FLPLDIDYGV NKQVAKKEPF QTSSNLAPSL IELMKMLFDV ETYRSAMMEF
     EINMSEMPLG KLSKHNIQKG FEALTEIQRL LTESDPQPTM KESLLVDASN RFFTMIPSIH
     PHIIRDEDDF KSKVKMLEAL QDIEIASRIV GFDVDSTESL DDKYKKLHCD ISPLPHDSED
     YRLIEKYLNT THAPTHTEWS LELEEVFALE REGEFDKYAP HREKLGNKML LWHGSRLTNF
     VGILNQGLRI APPEAPATGY MFGKGIYFAD LVSKSAQYCY TCKKNPVGLM LLSEVALGEI
     HELTKAKYMD KPPRGKHSTK GLGKKVPQDS EFAKWRGDVT VPCGKPVSSK VKASELMYNE
     YIVYDTAQVK LQFLLKVRFK HKR
//