PRP2A_ORYSJ
ID PRP2A_ORYSJ Reviewed; 660 AA.
AC Q5Z8Q9; Q0JMY0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Poly [ADP-ribose] polymerase 2-A;
DE Short=PARP-2-A;
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 2-A;
DE Short=ADPRT-2-A;
DE AltName: Full=Poly[ADP-ribose] synthase 2-A;
DE AltName: Full=Protein ADP-ribosyltransferase PARP2 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
GN Name=PARP2-A; OrderedLocusNames=Os01g0351200, LOC_Os01g24940;
GN ORFNames=B1051E10.55, P0463A02.25;
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
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 [3]
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 [4]
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).
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:0000305}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD52929.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD53855.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF04898.2; 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; AP003258; BAD52929.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP003764; BAD53855.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008207; BAF04898.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q5Z8Q9; -.
DR SMR; Q5Z8Q9; -.
DR STRING; 4530.OS01T0351200-00; -.
DR PaxDb; Q5Z8Q9; -.
DR PRIDE; Q5Z8Q9; -.
DR eggNOG; KOG1037; Eukaryota.
DR HOGENOM; CLU_004841_2_1_1; -.
DR InParanoid; Q5Z8Q9; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q5Z8Q9; OS.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 1.10.720.30; -; 2.
DR Gene3D; 1.20.142.10; -; 1.
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; IPR036361; SAP_dom_sf.
DR InterPro; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF02037; SAP; 2.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00513; SAP; 2.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50800; SAP; 2.
DR PROSITE; PS51977; WGR; 1.
PE 3: Inferred from homology;
KW ADP-ribosylation; DNA-binding; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transferase.
FT CHAIN 1..660
FT /note="Poly [ADP-ribose] polymerase 2-A"
FT /id="PRO_0000260503"
FT DOMAIN 2..36
FT /note="SAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 91..125
FT /note="SAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 179..281
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 308..426
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 434..660
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 40..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..75
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 56..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 74297 MW; 94FA8F38B72470A9 CRC64;
MSARLRVEEL RAELQRRGLD ASGNKPVLVR RLDAAIRKEE EEEAAVSAAA KEEADAGGVV
DGEGNGEDKR KRKRRGDGED VDNSESDAAK LEGMSYRELQ ALAKSRGLAA NGSKKEVIER
LLCAPSDTDG GVQDKKKIAK GFADGDDRVE ECRKEKIVTA TRKGAAVLDQ HIPDHIKMTY
HVLQVWFLLK GDEIYDATMN QTNVGDNNNK FYIIQALESD AGGSFMVYNR WGRVGARGQD
KLHGPFSSRE QAIYEFEGKF HGKTNNHWSD RKSFECYARK YTWLEMDYGE ADRETNKKVS
PSTDQIKETK LETRIASFIS LICNISMMKQ QMVEIGYNSD KLPLGKLSKS TIFKGYDVLK
RISNVISRAD RRQLEQLTGE FYTVIPHDFG FKKMREFIID TPQKLKAKLE MVEALGEIEI
ATKLLEDDST DQDDPLYARY KQLSCDFTPL EVGSEEYSMI KTYLANTHGK THTSYTVDVV
QIFKVSRHGE MERFQKFATA GNRMLLWHGS RLTNWAGILS QGLRIAPPEA PVTGYMFGKG
VYFADMFSKS ANYCYASEAC RSGVLLLCEV ALGEMNELLN ADYDANNLPK GKLSTKGVGQ
TEPNTAESKI TDDGVVVPLG KPKAEPSKRG SLLYNEFIVY NVDQIRMRYV LHVSFNFKKR
