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Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.30)

 A0A1P8B7C8_ARATH        Unreviewed;       635 AA.
A0A1P8B7C8;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
18-JUL-2018, entry version 10.
RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|RuleBase:RU362114};
Short=PARP {ECO:0000256|RuleBase:RU362114};
EC=2.4.2.30 {ECO:0000256|RuleBase:RU362114};
Name=PARP2 {ECO:0000313|EMBL:ANM67480.1};
Synonyms=APP {ECO:0000313|EMBL:ANM67480.1},
ATPARP1 {ECO:0000313|EMBL:ANM67480.1},
PARP1 {ECO:0000313|EMBL:ANM67480.1},
POLY(ADP-RIBOSE) POLYMERASE {ECO:0000313|EMBL:ANM67480.1},
poly(ADP-ribose) polymerase {ECO:0000313|EMBL:ANM67480.1},
POLY(ADP-RIBOSE) POLYMERASE 1 {ECO:0000313|EMBL:ANM67480.1},
poly(ADP-ribose) polymerase 2 {ECO:0000313|EMBL:ANM67480.1},
PP {ECO:0000313|EMBL:ANM67480.1};
OrderedLocusNames=At4g02390 {ECO:0000313|EMBL:ANM67480.1};
ORFNames=T14P8.19 {ECO:0000313|EMBL:ANM67480.1},
T14P8_19 {ECO:0000313|EMBL:ANM67480.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000313|EMBL:ANM67480.1, ECO:0000313|Proteomes:UP000006548};
[1] {ECO:0000313|EMBL:ANM67480.1, ECO:0000313|Proteomes:UP000006548}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
PubMed=10617198; DOI=10.1038/47134;
EU;
CSHL and WU Arabidopsis Sequencing Project;
Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B.,
Ansorge W., Brandt P., Grivell L., Rieger M., Weichselgartner M.,
de Simone V., Obermaier B., Mache R., Muller M., Kreis M., Delseny M.,
Puigdomenech P., Watson M., Schmidtheini T., Reichert B.,
Portatelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P.,
Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.A.,
McCullagh B., Bilham L., Robben J., Van der Schueren J.,
Grymonprez B., Chuang Y.J., Vandenbussche F., Braeken M., Weltjens I.,
Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G.,
Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S.,
van Staveren M., Dirske W., Mooijman P., Klein Lankhorst R., Rose M.,
Hauf J., Kotter P., Berneiser S., Hempel S., Feldpausch M.,
Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J.,
Villarroel R., De Clercq R., Van Montagu M., Rogers J., Cronin A.,
Quail M., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M.,
Muller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K.,
Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R.,
Piravandi E., Massenet O., Quigley F., Clabauld G., Mundlein A.,
Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Montfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.W., Stocker S., Zaccaria P.,
Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L.,
Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sehkon M.,
Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T.,
Kalicki J., Graves T., Harmon G., Edwards J., Latreille P.,
Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P.,
Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J.,
Fulton L., Mardis E., Dante M., Pepin K., Hillier L., Nelson J.,
Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
O'Shaughnessy A., Rodriguez M., Hoffmann J., Till S., Granat S.,
Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E.,
Marra M., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2] {ECO:0000313|Proteomes:UP000006548}
GENOME REANNOTATION.
STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000256|RuleBase:RU362114}.
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EMBL; CP002687; ANM67480.1; -; Genomic_DNA.
RefSeq; NP_001329308.1; NM_001340373.1.
UniGene; At.92; -.
EnsemblPlants; AT4G02390.2; AT4G02390.2; AT4G02390.
GeneID; 828049; -.
Gramene; AT4G02390.2; AT4G02390.2; AT4G02390.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; A0A1P8B7C8; baseline and differential.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
Gene3D; 1.10.720.30; -; 2.
Gene3D; 1.20.142.10; -; 1.
Gene3D; 2.20.140.10; -; 1.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
InterPro; IPR003034; SAP_dom.
InterPro; IPR036361; SAP_dom_sf.
InterPro; IPR036930; WGR_dom_sf.
InterPro; IPR008893; WGR_domain.
Pfam; PF00644; PARP; 1.
Pfam; PF02877; PARP_reg; 1.
Pfam; PF02037; SAP; 2.
Pfam; PF05406; WGR; 1.
SMART; SM00513; SAP; 2.
SMART; SM00773; WGR; 1.
SUPFAM; SSF142921; SSF142921; 1.
SUPFAM; SSF47587; SSF47587; 1.
SUPFAM; SSF68906; SSF68906; 2.
PROSITE; PS51060; PARP_ALPHA_HD; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS50800; SAP; 2.
4: Predicted;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000006548};
Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
NAD {ECO:0000256|RuleBase:RU362114};
Reference proteome {ECO:0000313|Proteomes:UP000006548};
Transferase {ECO:0000256|RuleBase:RU362114}.
DOMAIN 2 36 SAP. {ECO:0000259|PROSITE:PS50800}.
DOMAIN 69 103 SAP. {ECO:0000259|PROSITE:PS50800}.
DOMAIN 284 402 PARP alpha-helical.
{ECO:0000259|PROSITE:PS51060}.
DOMAIN 410 635 PARP catalytic.
{ECO:0000259|PROSITE:PS51059}.
COILED 29 49 {ECO:0000256|SAM:Coils}.
COILED 115 135 {ECO:0000256|SAM:Coils}.
SEQUENCE 635 AA; 72018 MW; E3F1CBE4D367A377 CRC64;
MANKLKVDEL RLKLAERGLS TTGVKAVLVE RLEEAIAEDT KKEESKSKRK RNSSNDTYES
NKLIAIGEFR GMIVKELREE AIKRGLDTTG TKKDLLERLC NDANNVSNAP VKSSNDEAED
DNNGFEEEKK EEKIVTATKK GAAVLDQWIP DEIKSQYHVL QRGDDVYDAI LNQTNVRDNN
NKFFVLQVLE SDSKKTYMVY TRWGRVGVKG QSKLDGPYDS WDRAIEIFTN KFNDKTKNYW
SDRKEFIPHP KSYTWLEMDY GKEENDSPVN NDIPSSSSEV KPEQSKLDTR VAKFISLICN
VSMMAQHMME IGYNANKLPL GKISKSTISK GYEVLKRISE VIDRYDRTRL EELSGEFYTV
IPHDFGFKKM SQFVIDTPQK LKQKIEMVEA LGEIELATKL LSVDPGLQDD PLYYHYQQLN
CGLTPVGNDS EEFSMVANYM ENTHAKTHSG YTVEIAQLFR ASRAVEADRF QQFSSSKNRM
LLWHGSRLTN WAGILSQGLR IAPPEAPVTG YMFGKGVYFA DMFSKSANYC YANTGANDGV
LLLCEVALGD MNELLYSDYN ADNLPPGKLS TKGVGKTAPN PSEAQTLEDG VVVPLGKPVE
RSCSKGMLLY NEYIVYNVEQ IKMRYVIQVK FNYKH


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