PARP3_ORYSJ
ID PARP3_ORYSJ Reviewed; 831 AA.
AC Q0E0Q3; B7ETH1; Q6H750;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein ADP-ribosyltransferase PARP3 {ECO:0000250|UniProtKB:Q9Y6F1};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9Y6F1};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 3;
DE Short=ADPRT-3;
DE AltName: Full=Poly [ADP-ribose] polymerase 3;
DE Short=PARP-3;
DE AltName: Full=Poly[ADP-ribose] synthase 3;
GN Name=PARP3; OrderedLocusNames=Os02g0530600, LOC_Os02g32860;
GN ORFNames=OsJ_06997 {ECO:0000312|EMBL:EEE57119.1}, P0476H10.38;
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).
RN [6]
RP INDUCTION BY HEAVY ION IRRADIATION.
RX PubMed=27462908; DOI=10.1371/journal.pone.0160061;
RA Ishii K., Kazama Y., Morita R., Hirano T., Ikeda T., Usuda S., Hayashi Y.,
RA Ohbu S., Motoyama R., Nagamura Y., Abe T.;
RT "Linear energy transfer-dependent change in rice gene expression profile
RT after heavy-ion beam irradiation.";
RL PLoS ONE 11:E0160061-E0160061(2016).
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:Q9Y6F1}.
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:Q9Y6F1};
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:Q9Y6F1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: Induced by heavy ion irradiation.
CC {ECO:0000269|PubMed:27462908}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD25449.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP004790; BAD25449.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008208; BAF08935.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS79031.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE57119.1; -; Genomic_DNA.
DR EMBL; AK102681; BAG95668.1; -; mRNA.
DR RefSeq; XP_015623193.1; XM_015767707.1.
DR RefSeq; XP_015623194.1; XM_015767708.1.
DR AlphaFoldDB; Q0E0Q3; -.
DR SMR; Q0E0Q3; -.
DR STRING; 4530.OS02T0530600-01; -.
DR PaxDb; Q0E0Q3; -.
DR PRIDE; Q0E0Q3; -.
DR EnsemblPlants; Os02t0530600-01; Os02t0530600-01; Os02g0530600.
DR GeneID; 4329546; -.
DR Gramene; Os02t0530600-01; Os02t0530600-01; Os02g0530600.
DR KEGG; osa:4329546; -.
DR eggNOG; KOG1037; Eukaryota.
DR HOGENOM; CLU_004841_0_1_1; -.
DR InParanoid; Q0E0Q3; -.
DR OMA; TRPFIFR; -.
DR OrthoDB; 909382at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q0E0Q3; baseline and differential.
DR Genevisible; Q0E0Q3; OS.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IBA:GO_Central.
DR Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR012982; PADR1.
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 Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF08063; PADR1; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
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; PS51977; WGR; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Glycosyltransferase; NAD; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Transferase.
FT CHAIN 1..831
FT /note="Protein ADP-ribosyltransferase PARP3"
FT /id="PRO_0000260505"
FT DOMAIN 198..290
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 338..439
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 466..585
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 594..827
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 92404 MW; 448C932D3F97173E CRC64;
MVHETRSRTL AASQEEGKAA PKKQKTESKE QEGGQQAPSK NKKTADNEEH DGEQEPSKNK
KLKAEESDLN GKATAVKEFS EFCKAIREHL TIEDMRKILQ GNEQDASGSE DAVVPRCEDV
MFYGPLDKCP VCGGQLECKG LKYNCTGTHS EWACCSFSTN NPSRRGGPIK VPDDVKNDFV
RKWLKQQEGN KYPKRNLDDE GIFSGMMIAL SGRMSRSHGY FKEQIMKHGG KVNNSVIGVT
CVVASPAERH QGGSGGFAEA LERGTPVVSE NWIIDSVQKK EKQPLAAYDI ASDVVPEGRG
LPLGNLDPTE EAIETLAAEL KLAGKRAVHK DSKLEKDGGH IYEKDGIIYN CAFSVCDLGG
DINQLCIMQL IMVPENHLHL YYKKGPIGHD QMAEERVEDF GSRFNDAIKE FVRLFEEVTG
NEFEPWEREK KFKKKCMKMY PLDMDDGVDV RHGGVALRQL GAAAAHCKLD PSVTFIMKQL
CSQEIYRYAL TEMGHDVPDL PIGMLTDLHL KRGEETLLEW KQDVESAPES GPAADAFWME
ISNKWFTLFP TTRPYTMKGY EQIADNVASG LETVRDINVA SRLIGDVFGS TLDDPLSQCY
KKLGCSINRV VEDSEDYKMI LKYLEKTYEP VKVGDVVYSA TVERIYAVES SALPSYDEIK
KLPNKVLLWC GTRSSNLLRH LRDGFVPAVC HIPVPGYMFG KAIVCSDAAA EAALYGFTAV
DRPEGYLVLA VASLGKEIQE ITGTPGSEDV KRMEEKKMGV KGVGRKTTDP SEHFTWRDGV
TVPCGKLVPS TNKDGPLEYN EYAVYDPKQV SIAFLVGVKY EEQNMEVVPD E