PRP2B_ORYSJ
ID PRP2B_ORYSJ Reviewed; 605 AA.
AC Q0JMY1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Poly [ADP-ribose] polymerase 2-B;
DE Short=PARP-2-B;
DE EC=2.4.2.30 {ECO:0000250|UniProtKB:P09874};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 2-B;
DE Short=ADPRT-2-B;
DE AltName: Full=Poly[ADP-ribose] synthase 2-B;
DE AltName: Full=Protein ADP-ribosyltransferase PARP2 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
GN Name=PARP2-B; OrderedLocusNames=Os01g0351100, LOC_Os01g24920;
GN ORFNames=B1051E10.53, P0463A02.23;
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=BAF04897.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP008207; BAF04897.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q0JMY1; -.
DR SMR; Q0JMY1; -.
DR STRING; 4530.OS01T0351100-00; -.
DR PaxDb; Q0JMY1; -.
DR PRIDE; Q0JMY1; -.
DR eggNOG; KOG1037; Eukaryota.
DR HOGENOM; CLU_004841_1_0_1; -.
DR InParanoid; Q0JMY1; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q0JMY1; 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 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; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
PE 3: Inferred from homology;
KW ADP-ribosylation; Glycosyltransferase; NAD; Nucleotidyltransferase;
KW Nucleus; Reference proteome; Transferase.
FT CHAIN 1..605
FT /note="Poly [ADP-ribose] polymerase 2-B"
FT /id="PRO_0000260507"
FT DOMAIN 153..260
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 250..370
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 378..605
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 96..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 67742 MW; 9B49D0305E3D124E CRC64;
MQMIGGEMWT AAGRRLHQQR DLHAILRTAH RRCCTRPIGG GLDAPAAPPG DLRTLSGVGM
LIHQFKALLA PKKIYPWRSS HLQSLEVRRL HTAPSNAAAA AAVTDGGDQD KTKSAKDDDG
DDKVQCKKEK IVTATKKGAA VLDQYIPDNI KTAYHVLQVG DEIYDATMNQ TNVGGNNNKF
YIIQALESDA GGNFMVYSRW GRVGTRDIHW SYRKGSHCYA HKYTWLEMDY GEADKETNKK
TSSITNQLEE TKLETRTASF ISLICDISMM KQQMVEIGYN ADKLPLGKLS KSTILKGYDV
LKRISNVISG ADTDRTQLEQ LTGEFYSVIP HDFGFKKMSE FIIDTPQKLK AKLEMVEALS
EIEIAIKLLE DDSSDQDHPL YARYKQFCCD FTPLEVDSEE YSMIKTYLTN THGKTHTGYT
VDIVQIFKVS RLGEMERFQK FASAGNRMLL WHGSRLTNWA GILSQGLRIA PPEAPISGFM
FGKGVYFADM FSKSANYCCA SEACKSGVML LCEVALGEMN ELLYGDFGAD NLPNGKLSTK
GVGQTEPNIA ESKITDDGMV IPLGKPEKVP SRRGSLMYNE YIVYNVDQIR MRYILNVNFN
FKRWG
