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Poly [ADP-ribose] polymerase (PARP) (EC 2.4.2.30) (NAD( ) ADP-ribosyltransferase) (ADPRT) (Poly[ADP-ribose] synthase)

 PARP_DROME              Reviewed;         994 AA.
P35875; A8Y590; Q7PLT6; Q8MSB5; Q8MU87; Q9W5Q5; Q9W5S1;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
23-MAY-2018, entry version 196.
RecName: Full=Poly [ADP-ribose] polymerase;
Short=PARP;
EC=2.4.2.30;
AltName: Full=NAD(+) ADP-ribosyltransferase;
Short=ADPRT;
AltName: Full=Poly[ADP-ribose] synthase;
Name=Parp; ORFNames=CG40411;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
TISSUE=Embryo;
PubMed=8475096; DOI=10.1073/pnas.90.8.3481;
Uchida K., Hanai S., Ishikawa K., Ozawa Y., Uchida M., Sugimura T.,
Miwa M.;
"Cloning of cDNA encoding Drosophila poly(ADP-ribose) polymerase:
leucine zipper in the auto-modification domain.";
Proc. Natl. Acad. Sci. U.S.A. 90:3481-3485(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS I
AND II), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Canton-S;
PubMed=9565614; DOI=10.1074/jbc.273.19.11881;
Hanai S., Uchida M., Kobayashi S., Miwa M., Uchida K.;
"Genomic organization of Drosophila poly(ADP-ribose) polymerase and
distribution of its mRNA during development.";
J. Biol. Chem. 273:11881-11886(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), FUNCTION, SUBCELLULAR
LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=12183365; DOI=10.1101/gad.1003902;
Tulin A., Stewart D., Spradling A.C.;
"The Drosophila heterochromatic gene encoding poly(ADP-ribose)
polymerase (PARP) is required to modulate chromatin structure during
development.";
Genes Dev. 16:2108-2119(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-994 (ISOFORM II).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
-!- FUNCTION: Poly[ADP-ribose] polymerase modifies various nuclear
proteins by poly(ADP-ribosyl)ation. The modification is dependent
on DNA and is involved in the regulation of various important
cellular processes such as differentiation, proliferation, and
tumor transformation and also in the regulation of the molecular
events involved in the recovery of cell from DNA damage. Plays a
fundamental role in organizing chromatin on a global scale;
isoform e autoregulates Parp transcription by influencing the
chromatin structure of its heterochromatic environment.
{ECO:0000269|PubMed:12183365}.
-!- CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor =
nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
{ECO:0000255|PROSITE-ProRule:PRU00397}.
-!- INTERACTION:
Q24368:Iswi; NbExp=4; IntAct=EBI-266172, EBI-367628;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00264, ECO:0000269|PubMed:12183365}. Nucleus, nucleolus
{ECO:0000269|PubMed:12183365}. Note=Highly enriched in nucleoli,
heterochromatic chromosomal regions, and diverse euchromatic sites
in the cells of most embryonic and adult tissues.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=II; Synonyms=B, Long;
IsoId=P35875-1; Sequence=Displayed;
Name=I; Synonyms=Short;
IsoId=P35875-2; Sequence=VSP_004536;
Name=E; Synonyms=Embryonic;
IsoId=P35875-3; Sequence=VSP_013203, VSP_013204;
-!- TISSUE SPECIFICITY: Expressed in adult female oocytes, anal plates
of stage 12 embryos and in cells around the central nervous system
in later embryos. {ECO:0000269|PubMed:9565614}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
embryos, pupae and adults. Expression is highest in embryos.
{ECO:0000269|PubMed:12183365, ECO:0000269|PubMed:9565614}.
-!- MISCELLANEOUS: The ADP-D-ribosyl group of NAD(+) is transferred to
an acceptor carboxyl group on a histone or the enzyme itself, and
further ADP-ribosyl groups are transferred to the 2'-position of
the terminal adenosine moiety, building up a polymer with an
average chain length of 20-30 units.
-!- SEQUENCE CAUTION:
Sequence=AAM50807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; D13806; BAA02964.1; -; mRNA.
EMBL; AF051548; AAC24518.1; -; Genomic_DNA.
EMBL; AF051544; AAC24518.1; JOINED; Genomic_DNA.
EMBL; AF051545; AAC24518.1; JOINED; Genomic_DNA.
EMBL; AF051546; AAC24518.1; JOINED; Genomic_DNA.
EMBL; AF051547; AAC24518.1; JOINED; Genomic_DNA.
EMBL; AF533701; AAM93435.1; -; mRNA.
EMBL; AE014297; EDP28045.1; -; Genomic_DNA.
EMBL; BT015238; AAT94467.1; -; mRNA.
EMBL; AY118947; AAM50807.1; ALT_INIT; mRNA.
PIR; A47474; A47474.
RefSeq; NP_001104452.1; NM_001110982.3. [P35875-1]
UniGene; Dm.7847; -.
ProteinModelPortal; P35875; -.
SMR; P35875; -.
BioGrid; 78234; 37.
DIP; DIP-23413N; -.
IntAct; P35875; 2.
STRING; 7227.FBpp0112608; -.
PaxDb; P35875; -.
PRIDE; P35875; -.
EnsemblMetazoa; FBtr0113885; FBpp0112608; FBgn0010247. [P35875-1]
GeneID; 3355109; -.
KEGG; dme:Dmel_CG40411; -.
CTD; 3355109; -.
FlyBase; FBgn0010247; Parp.
eggNOG; KOG1037; Eukaryota.
eggNOG; ENOG410XP18; LUCA.
GeneTree; ENSGT00390000017341; -.
InParanoid; P35875; -.
KO; K10798; -.
OMA; WNHASCI; -.
OrthoDB; EOG091G13H1; -.
PhylomeDB; P35875; -.
BRENDA; 2.4.2.30; 1994.
Reactome; R-DME-110362; POLB-Dependent Long Patch Base Excision Repair.
Reactome; R-DME-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-DME-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-DME-5696400; Dual Incision in GG-NER.
GenomeRNAi; 3355109; -.
PRO; PR:P35875; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0010247; -.
GO; GO:0015030; C:Cajal body; IDA:FlyBase.
GO; GO:0005694; C:chromosome; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0035363; C:histone locus body; IDA:FlyBase.
GO; GO:0005719; C:nuclear euchromatin; IDA:FlyBase.
GO; GO:0005730; C:nucleolus; IDA:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
GO; GO:0042393; F:histone binding; IPI:FlyBase.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:FlyBase.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030576; P:Cajal body organization; IMP:FlyBase.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0051276; P:chromosome organization; TAS:FlyBase.
GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central.
GO; GO:0008069; P:dorsal/ventral axis specification, ovarian follicular epithelium; IGI:FlyBase.
GO; GO:0035080; P:heat shock-mediated polytene chromosome puffing; IMP:FlyBase.
GO; GO:0045087; P:innate immune response; IMP:FlyBase.
GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:FlyBase.
GO; GO:0007552; P:metamorphosis; TAS:FlyBase.
GO; GO:0007000; P:nucleolus organization; IMP:FlyBase.
GO; GO:0035079; P:polytene chromosome puffing; TAS:FlyBase.
GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:CACAO.
GO; GO:0006471; P:protein ADP-ribosylation; IMP:FlyBase.
GO; GO:0043484; P:regulation of RNA splicing; IMP:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:FlyBase.
GO; GO:0009303; P:rRNA transcription; TAS:FlyBase.
CDD; cd00027; BRCT; 1.
Gene3D; 1.20.142.10; -; 1.
Gene3D; 2.20.140.10; -; 1.
Gene3D; 2.20.25.630; -; 1.
Gene3D; 3.30.1740.10; -; 2.
Gene3D; 3.40.50.10190; -; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR012982; PADR1.
InterPro; IPR038650; PADR1_dom_sf.
InterPro; IPR008288; PARP.
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; IPR036930; WGR_dom_sf.
InterPro; IPR008893; WGR_domain.
InterPro; IPR001510; Znf_PARP.
InterPro; IPR036957; Znf_PARP_sf.
Pfam; PF00533; BRCT; 1.
Pfam; PF08063; PADR1; 1.
Pfam; PF00644; PARP; 1.
Pfam; PF02877; PARP_reg; 1.
Pfam; PF05406; WGR; 1.
Pfam; PF00645; zf-PARP; 2.
PIRSF; PIRSF000489; NAD_ADPRT; 1.
SMART; SM00292; BRCT; 1.
SMART; SM01335; PADR1; 1.
SMART; SM00773; WGR; 1.
SMART; SM01336; zf-PARP; 2.
SUPFAM; SSF142921; SSF142921; 1.
SUPFAM; SSF47587; SSF47587; 1.
SUPFAM; SSF52113; SSF52113; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS51060; PARP_ALPHA_HD; 1.
PROSITE; PS51059; PARP_CATALYTIC; 1.
PROSITE; PS00347; PARP_ZN_FINGER_1; 1.
PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
1: Evidence at protein level;
ADP-ribosylation; Alternative splicing; Chromatin regulator;
Complete proteome; DNA-binding; Glycosyltransferase; Metal-binding;
NAD; Nucleus; Reference proteome; Repeat; Transferase; Zinc;
Zinc-finger.
CHAIN 1 994 Poly [ADP-ribose] polymerase.
/FTId=PRO_0000211325.
DOMAIN 380 471 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
DOMAIN 644 761 PARP alpha-helical. {ECO:0000255|PROSITE-
ProRule:PRU00398}.
DOMAIN 770 994 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
DNA_BIND 1 367
ZN_FING 7 89 PARP-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00264}.
ZN_FING 111 200 PARP-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00264}.
REGION 368 507 Automodification domain.
MOTIF 208 210 Nuclear localization signal.
MOTIF 223 228 Nuclear localization signal.
VAR_SEQ 376 565 Missing (in isoform I). {ECO:0000305}.
/FTId=VSP_004536.
VAR_SEQ 607 613 NEYEQRD -> MHFSEIH (in isoform E).
{ECO:0000303|PubMed:12183365}.
/FTId=VSP_013203.
VAR_SEQ 614 994 Missing (in isoform E).
{ECO:0000303|PubMed:12183365}.
/FTId=VSP_013204.
SEQUENCE 994 AA; 113792 MW; ACA85A270DD29E08 CRC64;
MDIELPYLAE YARTGRATCK GCKSTISKDT LRIAVMVQSA FHDAKVPNWF HKTCFFKNQR
PSSVGDIQNI GNLRFADQKE LTDLVENIQE VISAQLGKKR SKAFNLALKD FGIEYAKSSR
STCRGCEQKI NKDLVRLRKT VYDTEVGMKY GGQPLWHHLE CFAQLRSELG WFASGEDMPG
FQSLADDDQA KVKNAIPPIK SEELPDTKRA KMELSDTNEE GEKKQRLKDQ NDAYFRFRDD
IKNKMKKKDI DILLKFNNQQ PVTGDTEKLF DQTADLLTFG AIESCSECNS CQFIVNKSGY
ICNGNHSEWT KCNKLLKEPT RSACIVPKEL KALYNFLNTV KEIPSTRIFN NFPPNKSTFS
RSLLKTNKNN DVLVRPTIPR ISPPLYNLKF SIIGLKNQHK ELRKRIENLG GKFEVKISEN
TIAIISTELE IQKKSTRMKF AEELGIHIVP IEFLDFVEAD TEGAIKYINS TCICSWGTDP
KSRIPKETTK SLNSNSIYTK SMPVSRTFKV KDGLAVDPDS GLEDIAHVYV DSNNKYSVVL
GLTDIQRNKN SYYKVQLLKA DKKEKYWIFR SWGRIGTNIG NSKLEEFDTS ESAKRNFKEI
YADKTGNEYE QRDNFVKRTG RMYPIEIQYD DDQKLVKHES HFFTSKLEIS VQNLIKLIFD
IDSMNKTLME FHIDMDKMPL GKLSAHQIQS AYRVVKEIYN VLECGSNTAK LIDATNRFYT
LIPHNFGVQL PTLIETHQQI EDLRQMLDSL AEIEVAYSII KSEDVSDACN PLDNHYAQIK
TQLVALDKNS EEFSILSQYV KNTHASTHKS YDLKIVDVFK VSRQGEARRF KPFKKLHNRK
LLWHGSRLTN FVGILSHGLR IAPPEAPPTG YMFGKGIYFA DMVSKSANYC CTSQQNSTGL
MLLSEVALGD MMECTSAKYI NKLSNNKHSC FGRGRTMPDP TKSYIRSDGV EIPYGETITD
EHLKSSLLYN EYIVYDVAQV NIQYLFRMEF KYSY


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18-003-42429 Poly [ADP-ribose] polymerase 1 - EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.1 mg Protein A
18-003-42430 Poly [ADP-ribose] polymerase 2 - EC 2.4.2.30; PARP-2; NAD(+) ADP-ribosyltransferase 2; Poly[ADP-ribose] synthetase 2; pADPRT-2; hPARP-2 Polyclonal 0.05 mg Aff Pur
EIAAB29926 193 kDa vault protein,ADPRTL1,Homo sapiens,Human,KIAA0177,PARP4,PARP-4,PARPL,PARP-related_IalphaI-related H5_proline-rich,PH5P,Poly [ADP-ribose] polymerase 4,Vault poly(ADP-ribose) polymerase,VPARP
EIAAB29933 Homo sapiens,Human,PARP7,PARP-7,Poly [ADP-ribose] polymerase 7,TCDD-inducible poly [ADP-ribose] polymerase,TIPARP
20-272-190972 cleaved PARP - Mouse monoclonal [194C1439] to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Monoclonal 0.05 mg
18-272-197065 cleaved PARP - Rabbit polyclonal to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.05 mg
18-272-197066 cleaved PARP - Rabbit polyclonal to cleaved PARP; EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.05 mg


 

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