PARP2_ARATH
ID PARP2_ARATH Reviewed; 637 AA.
AC Q11207; O81294;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Poly [ADP-ribose] polymerase 2;
DE Short=PARP-2;
DE EC=2.4.2.30;
DE AltName: Full=NAD(+) ADP-ribosyltransferase 2;
DE Short=ADPRT-2;
DE AltName: Full=Poly[ADP-ribose] synthase 2;
DE AltName: Full=Protein ADP-ribosyltransferase PARP2 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
GN Name=PARP2; Synonyms=APP; OrderedLocusNames=At4g02390; ORFNames=T14P8.19;
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 [MRNA].
RX PubMed=7750552; DOI=10.1016/0014-5793(95)00335-7;
RA Lepiniec L., Babiychuk E., Kushnir S., van Montagu M., Inze D.;
RT "Characterization of an Arabidopsis thaliana cDNA homologue to animal
RT poly(ADP-ribose) polymerase.";
RL FEBS Lett. 364:103-108(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP INDUCTION.
RX PubMed=11523787; DOI=10.1007/s004380100506;
RA Doucet-Chabeaud G., Godon C., Brutesco C., de Murcia G., Kazmaier M.;
RT "Ionising radiation induces the expression of PARP-1 and PARP-2 genes in
RT Arabidopsis.";
RL Mol. Genet. Genomics 265:954-963(2001).
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.
CC -!- INDUCTION: By ionising radiation (IR)-induced DNA damage, by
CC dehydration and after cadmium exposure. {ECO:0000269|PubMed:11523787}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC19283.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80732.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z48243; CAA88288.1; -; mRNA.
DR EMBL; AF069298; AAC19283.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161494; CAB80732.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82163.1; -; Genomic_DNA.
DR PIR; T01311; T01311.
DR RefSeq; NP_001329308.1; NM_001340373.1.
DR RefSeq; NP_192148.2; NM_116472.4.
DR AlphaFoldDB; Q11207; -.
DR SMR; Q11207; -.
DR BioGRID; 13340; 6.
DR STRING; 3702.AT4G02390.1; -.
DR iPTMnet; Q11207; -.
DR PaxDb; Q11207; -.
DR PRIDE; Q11207; -.
DR ProteomicsDB; 236327; -.
DR EnsemblPlants; AT4G02390.1; AT4G02390.1; AT4G02390.
DR GeneID; 828049; -.
DR Gramene; AT4G02390.1; AT4G02390.1; AT4G02390.
DR KEGG; ath:AT4G02390; -.
DR Araport; AT4G02390; -.
DR TAIR; locus:2005523; AT4G02390.
DR eggNOG; KOG1037; Eukaryota.
DR HOGENOM; CLU_004841_2_1_1; -.
DR InParanoid; Q11207; -.
DR OrthoDB; 909382at2759; -.
DR PhylomeDB; Q11207; -.
DR PRO; PR:Q11207; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q11207; baseline and differential.
DR Genevisible; Q11207; AT.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:TAIR.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0030592; P:DNA ADP-ribosylation; IDA:TAIR.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:TAIR.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:TAIR.
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; 2.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50800; SAP; 2.
DR PROSITE; PS51977; WGR; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; DNA-binding; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transferase.
FT CHAIN 1..637
FT /note="Poly [ADP-ribose] polymerase 2"
FT /id="PRO_0000211332"
FT DOMAIN 2..36
FT /note="SAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 69..103
FT /note="SAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 158..255
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 286..404
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 412..637
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT DNA_BIND 1..140
FT /evidence="ECO:0000255"
FT REGION 35..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..62
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 637 AA; 72176 MW; 527A8F464605D127 CRC64;
MANKLKVDEL RLKLAERGLS TTGVKAVLVE RLEEAIAEDT KKEESKSKRK RNSSNDTYES
NKLIAIGEFR GMIVKELREE AIKRGLDTTG TKKDLLERLC NDANNVSNAP VKSSNGTDEA
EDDNNGFEEE KKEEKIVTAT KKGAAVLDQW IPDEIKSQYH VLQRGDDVYD AILNQTNVRD
NNNKFFVLQV LESDSKKTYM VYTRWGRVGV KGQSKLDGPY DSWDRAIEIF TNKFNDKTKN
YWSDRKEFIP HPKSYTWLEM DYGKEENDSP VNNDIPSSSS EVKPEQSKLD TRVAKFISLI
CNVSMMAQHM MEIGYNANKL PLGKISKSTI SKGYEVLKRI SEVIDRYDRT RLEELSGEFY
TVIPHDFGFK KMSQFVIDTP QKLKQKIEMV EALGEIELAT KLLSVDPGLQ DDPLYYHYQQ
LNCGLTPVGN DSEEFSMVAN YMENTHAKTH SGYTVEIAQL FRASRAVEAD RFQQFSSSKN
RMLLWHGSRL TNWAGILSQG LRIAPPEAPV TGYMFGKGVY FADMFSKSAN YCYANTGAND
GVLLLCEVAL GDMNELLYSD YNADNLPPGK LSTKGVGKTA PNPSEAQTLE DGVVVPLGKP
VERSCSKGML LYNEYIVYNV EQIKMRYVIQ VKFNYKH
