PARP1_ARATH
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 03-AUG-2022, entry version 159.
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 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 [5]
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:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20677.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ131705; CAA10482.1; -; mRNA.
DR EMBL; AC006593; AAD20677.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08527.1; -; 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 PDBsum; 1V9X; -.
DR AlphaFoldDB; Q9ZP54; -.
DR SMR; Q9ZP54; -.
DR BioGRID; 3038; 6.
DR STRING; 3702.AT2G31320.1; -.
DR PaxDb; Q9ZP54; -.
DR PRIDE; Q9ZP54; -.
DR ProteomicsDB; 236282; -.
DR EnsemblPlants; AT2G31320.1; AT2G31320.1; AT2G31320.
DR GeneID; 817690; -.
DR Gramene; AT2G31320.1; AT2G31320.1; AT2G31320.
DR KEGG; ath:AT2G31320; -.
DR Araport; AT2G31320; -.
DR TAIR; locus:2042511; AT2G31320.
DR eggNOG; KOG1037; Eukaryota.
DR HOGENOM; CLU_004841_0_1_1; -.
DR InParanoid; Q9ZP54; -.
DR OMA; RSAMMEF; -.
DR OrthoDB; 909382at2759; -.
DR PhylomeDB; Q9ZP54; -.
DR EvolutionaryTrace; Q9ZP54; -.
DR PRO; PR:Q9ZP54; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZP54; baseline and differential.
DR Genevisible; Q9ZP54; AT.
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:TAIR.
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:0030592; P:DNA ADP-ribosylation; IDA:TAIR.
DR GO; GO:0006281; P:DNA repair; IEP:TAIR.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA: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 Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.30.1740.10; -; 2.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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; PF00533; BRCT; 1.
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; 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; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
DR PROSITE; PS51977; WGR; 1.
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 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 369..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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
