PARP1_ORYSJ
ID PARP1_ORYSJ Reviewed; 977 AA.
AC Q7EYV7; B9FWT2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Poly [ADP-ribose] polymerase 1;
DE Short=PARP-1;
DE EC=2.4.2.30;
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=Os07g0413700, LOC_Os07g23110;
GN ORFNames=OsJ_23951 {ECO:0000312|EMBL:EEE67019.1}, OSJNBa0077F02.113;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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 -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK103479; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP005247; BAC84104.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF21367.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT01136.1; -; Genomic_DNA.
DR EMBL; CM000144; EEE67019.1; -; Genomic_DNA.
DR EMBL; AK103479; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015647732.1; XM_015792246.1.
DR AlphaFoldDB; Q7EYV7; -.
DR SMR; Q7EYV7; -.
DR STRING; 4530.OS07T0413700-01; -.
DR PaxDb; Q7EYV7; -.
DR PRIDE; Q7EYV7; -.
DR EnsemblPlants; Os07t0413700-01; Os07t0413700-01; Os07g0413700.
DR GeneID; 4343013; -.
DR Gramene; Os07t0413700-01; Os07t0413700-01; Os07g0413700.
DR KEGG; osa:4343013; -.
DR eggNOG; KOG1037; Eukaryota.
DR HOGENOM; CLU_004841_0_1_1; -.
DR InParanoid; Q7EYV7; -.
DR OMA; RSAMMEF; -.
DR OrthoDB; 909382at2759; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q7EYV7; baseline and differential.
DR Genevisible; Q7EYV7; OS.
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; IBA:GO_Central.
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; IEA:EnsemblPlants.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblPlants.
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; IPR003034; SAP_dom.
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; PS50800; SAP; 1.
DR PROSITE; PS51977; WGR; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; DNA-binding; Glycosyltransferase; Metal-binding; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..977
FT /note="Poly [ADP-ribose] polymerase 1"
FT /id="PRO_0000260502"
FT DOMAIN 254..288
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 381..473
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 504..604
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 626..745
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 752..977
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 104..179
FT /note="PARP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT REGION 177..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 233
FT /note="S -> F (in Ref. 5; AK103479)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="G -> S (in Ref. 5; AK103479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 977 AA; 110156 MW; 0BBB8B57BFF9976B CRC64;
MAAPPKAWKA EYAKSGRSSC KSCRSPIGKD QLRLGKMVQA TQFDGLMPMW NHASCILSKK
NQIKSVDDVE GIDTLRWDDQ EKIRNYVGSA PATASSAAAI SDKCTIEVAK SARTSCRRCG
EKIKKGTVRV SSKLEGQGWY HASCFLEMSP AATVENFSGW EILSHEDKRA VLDLVKKDAP
SSGQTSSKGS KRKNNQNDIH DCKAPKIIRS ISEGTAEDKG KAVVSHDSNA NSSDLQEKLK
EQSDTLWKLK DELKKHVSTA ELRNMLEANG QDTSGPERHL LDRCADGMLF GALGTCPVCS
SFLYYHGGQY HCSGYVSEWS KCTYSTTEPV RSKKKWKIPD EMDNGYLTKW FKSQKAKKPE
RVLPPMSPEK SLCQSTQQNR SFLSEGLDKL RVSIVGQSKD VVDGWKQKLK DAGANFNATV
TKDSSCLVLC SELESENAEV KKARRLKIPI LREGYLGECI RKNRVLPFDL YKVEAALESS
KGGTMTVKVK GRSAVHESSG LQDTGHILED GKSIYNTTLN MSDLTRGVNS YYILQVIEED
NGSDCYVFRK WGRVGNEKIG GTKLEEMSKI HAIQEFRRLF LEKTGNPWEA WEQKTNFQKQ
PGKFYPLDID YGVRQGPKRK DIDKMKSSLP PQLLELMNML FNIETYRAAM LEFKINMSEM
PLGKLSKENI QKGFEALTEI QNLLGNTNNQ ELAVRESLIV AASNRFFTLI PSIHPHIIQD
EDDLMVKVKM LEALQDIEIA SKLVGFDSDN DESLDDKYKK LRCAITPLPH DCEDYKLVEK
YLLNTHAPTH KEWSLELEEV FSLDRDGEFS KYSRYKNNLH NKMLLWHGSR LTNYVGILSQ
GLRIAPPEAP VTGYMFGKGL YFADLVSKSA QYCYVDRKNP VGLMLLSEVA LGDMYELKKA
TSMDKPPRGK HSTKGLGKTV PLESEFAKWR DDVVVPCGKP VPASIKTSEL MYNEYIVYNT
SQVKMQYLLK VRFHHKR
