PARP3_ARATH
ID PARP3_ARATH Reviewed; 814 AA.
AC Q9FK91; F4K9W5; Q8GXP3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 136.
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=At5g22470; ORFNames=MQJ16_1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-814.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09119.1; 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; AB012244; BAB09119.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK118123; BAC42749.1; -; mRNA.
DR RefSeq; NP_001318618.1; NM_001343735.1.
DR AlphaFoldDB; Q9FK91; -.
DR SMR; Q9FK91; -.
DR STRING; 3702.AT5G22470.1; -.
DR PaxDb; Q9FK91; -.
DR PeptideAtlas; Q9FK91; -.
DR PRIDE; Q9FK91; -.
DR GeneID; 832308; -.
DR KEGG; ath:AT5G22470; -.
DR Araport; AT5G22470; -.
DR TAIR; locus:2171137; AT5G22470.
DR eggNOG; KOG1037; Eukaryota.
DR HOGENOM; CLU_004841_0_1_1; -.
DR InParanoid; Q9FK91; -.
DR OrthoDB; 909382at2759; -.
DR PRO; PR:Q9FK91; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK91; baseline and differential.
DR Genevisible; Q9FK91; AT.
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; Repeat; TPR repeat; Transferase.
FT CHAIN 1..814
FT /note="Protein ADP-ribosyltransferase PARP3"
FT /id="PRO_0000260498"
FT DOMAIN 182..274
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REPEAT 182..215
FT /note="TPR 1"
FT REPEAT 277..310
FT /note="TPR 2"
FT DOMAIN 322..422
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 449..568
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 577..808
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 444
FT /note="G -> V (in Ref. 3; BAC42749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 814 AA; 91406 MW; B68B75DF2A76692F CRC64;
MKVHETRSHA HMSGDEQKGN LRKHKAEGKL PESEQSQKKA KPENDDGRSV NGAGDAASEY
NEFCKAVEEN LSIDQIKEVL EINGQDCSAP EETLLAQCQD LLFYGALAKC PLCGGTLICD
NEKRFVCGGE ISEWCSCVFS TKDPPRKEEP VKIPDSVMNS AISDLIKKHQ DPKSRPKREL
GSADKPFVGM MISLMGRLTR THQYWKKKIE RNGGKVSNTV QGVTCLVVSP AERERGGTSK
MVEAMEQGLP VVSEAWLIDS VEKHEAQPLE AYDVVSDLSV EGKGIPWDKQ DPSEEAIESF
SAELKMYGKR GVYMDTKLQE RGGKIFEKDG LLYNCAFSIC DLGKGRNEYC IMQLVTVPDS
NLNMYFKRGK VGDDPNAEER LEEWEDEEAA IKEFARLFEE IAGNEFEPWE REKKIQKKPH
KFFPIDMDDG IEVRSGALGL RQLGIASAHC KLDSFVANFI KVLCGQEIYN YALMELGLDP
PDLPMGMLTD IHLKRCEEVL LEFVEKVKTT KETGQKAEAM WADFSSRWFS LMHSTRPMRL
HDVNELADHA ASAFETVRDI NTASRLIGDM RGDTLDDPLS DRYKKLGCKI SVVDKESEDY
KMVVKYLETT YEPVKVSDVE YGVSVQNVFA VESDAIPSLD DIKKLPNKVL LWCGSRSSNL
LRHIYKGFLP AVCSLPVPGY MFGRAIVCSD AAAEAARYGF TAVDRPEGFL VLAVASLGEE
VTEFTSPPED TKTLEDKKIG VKGLGRKKTE ESEHFMWRDD IKVPCGRLVP SEHKDSPLEY
NEYAVYDPKQ TSIRFLVEVK YEEKGTEIVD VEPE
