ID A0A3Q0E0Q9_CARSF Unreviewed; 568 AA.
AC A0A3Q0E0Q9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 08-OCT-2025, 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=PARP2 {ECO:0000313|RefSeq:XP_021569919.1};
OS Carlito syrichta (Philippine tarsier) (Tarsius syrichta).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC Carlito.
OX NCBI_TaxID=1868482 {ECO:0000313|Proteomes:UP000189704, ECO:0000313|RefSeq:XP_021569919.1};
RN [1] {ECO:0000313|RefSeq:XP_021569919.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
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:0000256|ARBA:ARBA00033987};
CC -!- SUBUNIT: Component of a base excision repair (BER) complex, containing
CC at least XRCC1, PARP1, POLB and LRIG3. Homo- and heterodimer with
CC PARP1. Interacts (via the PARP catalytic domain) with HPF1. Interacts
CC with core nucleosomes. {ECO:0000256|ARBA:ARBA00064631}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_021569919.1; XM_021714244.1.
DR AlphaFoldDB; A0A3Q0E0Q9; -.
DR STRING; 1868482.ENSTSYP00000003629; -.
DR GeneID; 103264038; -.
DR CTD; 10038; -.
DR OMA; QGENDRF; -.
DR Proteomes; UP000189704; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:TreeGrafter.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140294; F:NAD DNA ADP-ribosyltransferase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0003950; F:NAD+ poly-ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140806; F:NAD+-protein-aspartate ADP-ribosyltransferase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0140807; F:NAD+-protein-glutamate ADP-ribosyltransferase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0140805; F:NAD+-protein-serine ADP-ribosyltransferase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0031491; F:nucleosome binding; IEA:UniProtKB-ARBA.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0030592; P:DNA ADP-ribosylation; IEA:UniProtKB-ARBA.
DR GO; GO:0006302; P:double-strand break repair; IEA:TreeGrafter.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IEA:TreeGrafter.
DR CDD; cd22252; PARP2_NTR; 1.
DR CDD; cd01437; parp_like; 1.
DR CDD; cd08003; WGR_PARP2_like; 1.
DR FunFam; 1.20.142.10:FF:000003; Poly [ADP-ribose] polymerase; 1.
DR FunFam; 2.20.140.10:FF:000001; Poly [ADP-ribose] polymerase; 1.
DR FunFam; 3.90.228.10:FF:000002; Poly [ADP-ribose] polymerase; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR Gene3D; 2.20.140.10; WGR domain; 1.
DR InterPro; IPR050800; ARTD/PARP.
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:SF60; POLY [ADP-RIBOSE] POLYMERASE 2; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF142921; WGR domain-like; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU362114};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000189704};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 90..187
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 216..333
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 341..568
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..47
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 64422 MW; EF014876B8529C5C CRC64;
MAARKRRASG LRARALNETK RASNGNTASE DSNPTKKTRK CQRHGVKKMP VAGGKANKDK
TEDKQCESVK ALLLKGKAPV DPECTAKVGK AHVYCEGSDV YDVMLNQTNL QFNNNKYYLI
QLLEDDDQRN FSVWMRWGRV GKMGQHSLVA CSANLNKAKE IFQKKFLDKT KNNWEDREKF
EKVPGKYDML QMDYATNTQG EEKTKKESLK SSLKTESQLD LRVQELIKLI CNVQAMEEMM
IEMKYNTKKA PLGKLTVAQI KAGYQSLKKI EDCIRSGQHG RALMEACSEF YTRIPHDFGL
RTPPLIRTEK ELSEKVQLLE ALGDIEIAIK LVKTEQQSPE HPLDQHYRNL HCALCPLDHE
SYEFKVISQY LQSTHAPTHS DYTMTLLDVF EVEKEGEKEV FREDLHNRML LWHGSRLSNW
VGILSRGLRV APPEAPITGY MFGKGIYFAD MSSKSANYCF ASHLKNTGLL LLSEVALGQC
NELLEANPKA ESLLQGKHST KGLGKMAPSP SCFITLNGST VPLGPASDTG IVNPEGYTLN
YNEYIVYNPN QVRMRYLLKV QFNFLQLW
//
