PARP2_MAIZE
ID PARP2_MAIZE Reviewed; 653 AA.
AC O50017;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=PARP;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9778846; DOI=10.1046/j.1365-313x.1998.00240.x;
RA Babiychuk E., Cottrill P.B., Storozhenko S., Fuangthong M., Chen Y.,
RA O'Farrell M.K., Van Montagu M., Inze D., Kushnir S.;
RT "Higher plants possess two structurally different poly(ADP-ribose)
RT polymerases.";
RL Plant J. 15:635-645(1998).
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}.
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DR EMBL; AJ222588; CAA10888.1; -; mRNA.
DR PIR; T03656; T03656.
DR AlphaFoldDB; O50017; -.
DR SMR; O50017; -.
DR STRING; 4577.GRMZM2G099231_P01; -.
DR PaxDb; O50017; -.
DR PRIDE; O50017; -.
DR MaizeGDB; 403201; -.
DR eggNOG; KOG1037; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; O50017; baseline and differential.
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; -; 1.
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; 1.
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 2: Evidence at transcript level;
KW ADP-ribosylation; DNA-binding; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transferase.
FT CHAIN 1..653
FT /note="Poly [ADP-ribose] polymerase 2"
FT /id="PRO_0000260499"
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..276
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 301..419
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 427..653
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 64..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..72
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 653 AA; 72995 MW; 5FD01923C4ABCD1D CRC64;
MSARLRVADV RAELQRRGLD VSGTKPALVR RLDAAICEAE KAVVAAAPTS VANGYDVAVD
GKRNCGNNKR KRSGDGGEEG NGDTCTDVTK LEGMSYRELQ GLAKARGVAA NGGKKDVIQR
LLSATAGPAA VADGGPLGAK EVIKGGDEEV EVKKEKMVTA TKKGAAVLDQ HIPDHIKVNY
HVLQVGDEIY DATLNQTNVG DNNNKFYIIQ VLESDAGGSF MVYNRWGRVG VRGQDKLHGP
SPTRDQAIYE FEGKFHNKTN NHWSDRKNFK CYAKKYTWLE MDYGETEKEI EKGSITDQIK
ETKLETRIAQ FISLICNISM MKQRMVEIGY NAEKLPLGKL RKATILKGYH VLKRISDVIS
KADRRHLEQL TGEFYTVIPH DFGFRKMREF IIDTPQKLKA KLEMVEALGE IEIATKLLED
DSSDQDDPLY ARYKQLHCDF TPLEADSDEY SMIKSYLRNT HGKTHSGYTV DIVQIFKVSR
HGETERFQKF ASTRNRMLLW HGSRLSNWAG ILSQGLRIAP PEAPVTGYMF GKGVYFADMF
SKSANYCYAS EACRSGVLLL CEVALGDMNE LLNADYDANN LPKGKLRSKG VGQTAPNMVE
SKVADDGVVV PLGEPKQEPS KRGGLLYNEY IVYNVDQIRM RYVLHVNFNF KRR
