ID A0A2H1ZE65_ARATH Unreviewed; 815 AA.
AC A0A2H1ZE65;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|RuleBase:RU362114};
DE Short=PARP {ECO:0000256|RuleBase:RU362114};
DE EC=2.4.2.- {ECO:0000256|RuleBase:RU362114};
GN Name=PARP3 {ECO:0000313|EMBL:AED93031.2, ECO:0000313|TAIR:AT5G22470};
GN Synonyms=AtPARP3 {ECO:0000313|EMBL:AED93031.2}, MQJ16.1
GN {ECO:0000313|EMBL:AED93031.2}, MQJ16_1 {ECO:0000313|EMBL:AED93031.2},
GN Poly(ADP-Ribose) Polymerase 3 {ECO:0000313|EMBL:AED93031.2};
GN OrderedLocusNames=At5g22470 {ECO:0000313|Araport:AT5G22470,
GN ECO:0000313|EMBL:AED93031.2};
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 {ECO:0000313|EMBL:AED93031.2, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:AED93031.2, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130714; DOI=10.1038/35048507;
RG Kazusa DNA Research Institute;
RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG European Union Arabidopsis Genome Sequencing Consortium;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D.,
RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B.,
RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H.,
RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S.,
RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J.,
RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
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).
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. {ECO:0000256|ARBA:ARBA00024945}.
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:0000256|ARBA:ARBA00000438};
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:0000256|ARBA:ARBA00000459};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR EMBL; CP002688; AED93031.2; -; Genomic_DNA.
DR RefSeq; NP_001318618.1; NM_001343735.1.
DR AlphaFoldDB; A0A2H1ZE65; -.
DR SMR; A0A2H1ZE65; -.
DR ProteomicsDB; 193879; -.
DR EnsemblPlants; AT5G22470.1; AT5G22470.1; AT5G22470.
DR GeneID; 832308; -.
DR Gramene; AT5G22470.1; AT5G22470.1; AT5G22470.
DR KEGG; ath:AT5G22470; -.
DR Araport; AT5G22470; -.
DR TAIR; AT5G22470; PARP3.
DR OMA; THQYWKK; -.
DR OrthoDB; 548995at2759; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; A0A2H1ZE65; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR CDD; cd17747; BRCT_PARP1; 1.
DR CDD; cd01437; parp_like; 1.
DR CDD; cd08001; WGR_PARP1_like; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 3.90.640.80; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR049296; PARP1-like_PADR1_N.
DR InterPro; IPR012982; PARP1-like_PADR1_Zn_ribbon.
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 PANTHER; PTHR10459; DNA LIGASE; 1.
DR PANTHER; PTHR10459:SF106; PROTEIN ADP-RIBOSYLTRANSFERASE PARP3; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF21728; PADR1_N; 1.
DR Pfam; PF08063; PADR1_Zn_ribbon; 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; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS52007; PADR1; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU362114};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A2H1ZE65,
KW ECO:0007829|ProteomicsDB:A0A2H1ZE65};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 183..275
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 323..423
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 450..569
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 578..809
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 91534 MW; 4B1B602057D46B60 CRC64;
MKVHETRSHA HMSGDEQKKG NLRKHKAEGK LPESEQSQKK AKPENDDGRS VNGAGDAASE
YNEFCKAVEE NLSIDQIKEV LEINGQDCSA PEETLLAQCQ DLLFYGALAK CPLCGGTLIC
DNEKRFVCGG EISEWCSCVF STKDPPRKEE PVKIPDSVMN SAISDLIKKH QDPKSRPKRE
LGSADKPFVG MMISLMGRLT RTHQYWKKKI ERNGGKVSNT VQGVTCLVVS PAERERGGTS
KMVEAMEQGL PVVSEAWLID SVEKHEAQPL EAYDVVSDLS VEGKGIPWDK QDPSEEAIES
FSAELKMYGK RGVYMDTKLQ ERGGKIFEKD GLLYNCAFSI CDLGKGRNEY CIMQLVTVPD
SNLNMYFKRG KVGDDPNAEE RLEEWEDEEA AIKEFARLFE EIAGNEFEPW EREKKIQKKP
HKFFPIDMDD GIEVRSGALG LRQLGIASAH CKLDSFVANF IKVLCGQEIY NYALMELGLD
PPDLPMGMLT DIHLKRCEEV LLEFVEKVKT TKETGQKAEA MWADFSSRWF SLMHSTRPMR
LHDVNELADH AASAFETVRD INTASRLIGD MRGDTLDDPL SDRYKKLGCK ISVVDKESED
YKMVVKYLET TYEPVKVSDV EYGVSVQNVF AVESDAIPSL DDIKKLPNKV LLWCGSRSSN
LLRHIYKGFL PAVCSLPVPG YMFGRAIVCS DAAAEAARYG FTAVDRPEGF LVLAVASLGE
EVTEFTSPPE DTKTLEDKKI GVKGLGRKKT EESEHFMWRD DIKVPCGRLV PSEHKDSPLE
YNEYAVYDPK QTSIRFLVEV KYEEKGTEIV DVEPE
//
