PARP3_SOYBN
ID PARP3_SOYBN Reviewed; 815 AA.
AC Q9SWB4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein ADP-ribosyltransferase PARP3 {ECO:0000250|UniProtKB:Q9Y6F1};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9Y6F1};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 3;
DE Short=ADPRT-3;
DE AltName: Full=Poly [ADP-ribose] polymerase 3;
DE Short=PARP-3;
DE AltName: Full=Poly[ADP-ribose] synthase 3;
GN Name=PARP3; Synonyms=PM38;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Shi-shi;
RA Chow T.Y., Lin T.Y., Lin T.Y., Liu S.M., Hsing Y.I.C.;
RT "Characterization of a soybean seed maturation protein, PM38.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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:Q9Y6F1}.
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:Q9Y6F1};
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:Q9Y6F1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AF169023; AAD51626.1; -; mRNA.
DR RefSeq; NP_001237586.1; NM_001250657.1.
DR AlphaFoldDB; Q9SWB4; -.
DR SMR; Q9SWB4; -.
DR STRING; 3847.GLYMA12G09390.1; -.
DR PRIDE; Q9SWB4; -.
DR EnsemblPlants; KRH25206; KRH25206; GLYMA_12G088300.
DR GeneID; 548024; -.
DR Gramene; KRH25206; KRH25206; GLYMA_12G088300.
DR KEGG; gmx:548024; -.
DR eggNOG; KOG1037; Eukaryota.
DR InParanoid; Q9SWB4; -.
DR OMA; TRPFIFR; -.
DR OrthoDB; 909382at2759; -.
DR Proteomes; UP000008827; Chromosome 12.
DR Genevisible; Q9SWB4; GM.
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; 1.20.142.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR012982; PADR1.
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; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08063; PADR1; 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; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51977; WGR; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; DNA-binding; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..815
FT /note="Protein ADP-ribosyltransferase PARP3"
FT /id="PRO_0000260506"
FT DOMAIN 69..103
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 182..274
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 322..422
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 449..568
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 577..808
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 91689 MW; 2795159D82B70D12 CRC64;
MKVQETRSHV HALGEEEKVM TRKQKAESKA HEVEHSPKKA KVEKEDGHIN GKSETGVAEE
YDEFCKATTE HLPLEQMRDI LEANGLDSSG SDLEITRRCQ DLLFYGALDK CSVCNGSLEF
DGRRYVCRGF YSEWASCTFS TRNPPRKQEP IKLPDSVQNS LASDLLKKYQ DPSHRPHRDL
GLAEKPFTGM MISLMGRLTR THHYWKTTIE KHGGKVANSI IGSTCLVASP AERERGGTSK
LAEAMERSIP VVREAWLIDS IEKQEPQPLE AYDLVSDLSV DGKGIPWDKQ DPGEEAIESL
SAELKLYGKR GVYKDTKLQE QGGKIFERDG ILYNCAFSVC DQGRGLNDYC VMQLIVVPEN
RLHLYFKKGR VGDDPNAEER LEEWDNVDGA LKEFVRLFEE ITGNEFEPWE REKKFQKKPL
KFYPIDMDDG IEVRHGALGL RQLGIAATHC KLEPLVANFM KVLCSQEIYK YALMEMGYDC
PDLPIGMVTN LHLKKCEDVL LEFIDKVKSL KETGPKAEAV WTDFSQRWFT LMHSTRPFNF
RDYQEIADHA AAALEGVRDI TQASHLIGDM TGSTIDDPLS ETYKKLGCSI SALDKSSDDY
EMIVKYLEKT YEPVKVGDIE YGVSVENIFA VQTGGCPSYE DIIKLPNKVL LWCGSRSSNL
LRHLQKGFLP AICSLPIPGY MFGKAIVCSD AAAEAARYGF TAVDRPEGFL VLAIASLGNE
ITELKTPPED ASSLEEKKVG VKGPGKKKTD ESEHFVWKDD IKVPCGKLVA SDHQDSPLEY
NEYAVYDKKR ARISYLVGVK YEEKEEKGAV IDTAE
