P35875 (PARP_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly [ADP-ribose] polymerase
Short name=PARP
EC=2.4.2.30

Alternative name(s):
NAD(+) ADP-ribosyltransferase
Short name=ADPRT
Poly[ADP-ribose] synthase

Gene names

Name:	Parp
ORF Names:	CG40411

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	994 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

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.
Catalytic activity	NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
Subcellular location	Nucleus. Nucleus › nucleolus. Note: Highly enriched in nucleoli, heterochromatic chromosomal regions, and diverse euchromatic sites in the cells of most embryonic and adult tissues. Ref.3
Tissue specificity	Expressed in adult female oocytes, anal plates of stage 12 embryos and in cells around the central nervous system in later embryos. Ref.2
Developmental stage	Expressed both maternally and zygotically in embryos, pupae and adults. Expression is highest in embryos. Ref.2 Ref.3
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 similarities	Contains 1 BRCT domain. Contains 1 PARP alpha-helical domain. Contains 1 PARP catalytic domain. Contains 2 PARP-type zinc fingers.
Sequence caution	The sequence AAM50807.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding NAD Zinc
Molecular function	Chromatin regulator Glycosyltransferase Transferase
PTM	ADP-ribosylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW heat shock-mediated polytene chromosome puffing Inferred from expression pattern. Source: FlyBase innate immune response Inferred from mutant phenotype. Source: FlyBase maintenance of protein location in nucleus Inferred from mutant phenotype. Source: FlyBase metamorphosis Traceable author statement. Source: FlyBase nucleolus organization Inferred from mutant phenotype Ref.3. Source: FlyBase positive regulation of antibacterial peptide biosynthetic process Inferred from mutant phenotype. Source: FlyBase protein ADP-ribosylation Inferred from mutant phenotype Ref.3. Source: FlyBase rRNA transcription Traceable author statement. Source: FlyBase regulation of RNA splicing Inferred from mutant phenotype. Source: FlyBase regulation of transcription, DNA-dependent Traceable author statement. Source: FlyBase
Cellular component	nuclear euchromatin Inferred from direct assay. Source: FlyBase nucleolus Inferred from direct assay. Source: FlyBase polytene chromosome puff Inferred from direct assay. Source: FlyBase
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW NAD binding Inferred from electronic annotation. Source: InterPro NAD+ ADP-ribosyltransferase activity Inferred from direct assay. Source: FlyBase histone binding Inferred from physical interaction. Source: FlyBase zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform II (identifier: P35875-1)

Also known as: B; Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform I (identifier: P35875-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     376-565: Missing.

Isoform E (identifier: P35875-3)

Also known as: Embryonic;

The sequence of this isoform differs from the canonical sequence as follows:
     607-613: NEYEQRD → MHFSEIH
     614-994: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 994	994	Poly [ADP-ribose] polymerase		PRO_0000211325
Regions
	Domain	380 – 471	92	BRCT
	Domain	644 – 761	118	PARP alpha-helical
	Domain	770 – 994	225	PARP catalytic
	DNA binding	1 – 367	367
	Zinc finger	7 – 89	83	PARP-type 1
	Zinc finger	111 – 200	90	PARP-type 2
	Region	368 – 507	140	Automodification domain
	Motif	208 – 210	3	Nuclear localization signal
	Motif	223 – 228	6	Nuclear localization signal
Natural variations
	Alternative sequence	376 – 565	190	Missing in isoform I.		VSP_004536
	Alternative sequence	607 – 613	7	NEYEQRD → MHFSEIH in isoform E.		VSP_013203
	Alternative sequence	614 – 994	381	Missing in isoform E.		VSP_013204

Sequences

	Sequence		Length	Mass (Da)
	Isoform II (B) (Long) [UniParc]. Last modified June 1, 1994. Version 1. Checksum: ACA85A270DD29E08	FASTA	994	113,792
	10 20 30 40 50 60 MDIELPYLAE YARTGRATCK GCKSTISKDT LRIAVMVQSA FHDAKVPNWF HKTCFFKNQR 70 80 90 100 110 120 PSSVGDIQNI GNLRFADQKE LTDLVENIQE VISAQLGKKR SKAFNLALKD FGIEYAKSSR 130 140 150 160 170 180 STCRGCEQKI NKDLVRLRKT VYDTEVGMKY GGQPLWHHLE CFAQLRSELG WFASGEDMPG 190 200 210 220 230 240 FQSLADDDQA KVKNAIPPIK SEELPDTKRA KMELSDTNEE GEKKQRLKDQ NDAYFRFRDD 250 260 270 280 290 300 IKNKMKKKDI DILLKFNNQQ PVTGDTEKLF DQTADLLTFG AIESCSECNS CQFIVNKSGY 310 320 330 340 350 360 ICNGNHSEWT KCNKLLKEPT RSACIVPKEL KALYNFLNTV KEIPSTRIFN NFPPNKSTFS 370 380 390 400 410 420 RSLLKTNKNN DVLVRPTIPR ISPPLYNLKF SIIGLKNQHK ELRKRIENLG GKFEVKISEN 430 440 450 460 470 480 TIAIISTELE IQKKSTRMKF AEELGIHIVP IEFLDFVEAD TEGAIKYINS TCICSWGTDP 490 500 510 520 530 540 KSRIPKETTK SLNSNSIYTK SMPVSRTFKV KDGLAVDPDS GLEDIAHVYV DSNNKYSVVL 550 560 570 580 590 600 GLTDIQRNKN SYYKVQLLKA DKKEKYWIFR SWGRIGTNIG NSKLEEFDTS ESAKRNFKEI 610 620 630 640 650 660 YADKTGNEYE QRDNFVKRTG RMYPIEIQYD DDQKLVKHES HFFTSKLEIS VQNLIKLIFD 670 680 690 700 710 720 IDSMNKTLME FHIDMDKMPL GKLSAHQIQS AYRVVKEIYN VLECGSNTAK LIDATNRFYT 730 740 750 760 770 780 LIPHNFGVQL PTLIETHQQI EDLRQMLDSL AEIEVAYSII KSEDVSDACN PLDNHYAQIK 790 800 810 820 830 840 TQLVALDKNS EEFSILSQYV KNTHASTHKS YDLKIVDVFK VSRQGEARRF KPFKKLHNRK 850 860 870 880 890 900 LLWHGSRLTN FVGILSHGLR IAPPEAPPTG YMFGKGIYFA DMVSKSANYC CTSQQNSTGL 910 920 930 940 950 960 MLLSEVALGD MMECTSAKYI NKLSNNKHSC FGRGRTMPDP TKSYIRSDGV EIPYGETITD 970 980 990 EHLKSSLLYN EYIVYDVAQV NIQYLFRMEF KYSY
	Isoform I (Short) [UniParc]. Checksum: 52719FF12193871F	FASTA	804	92,303
	10 20 30 40 50 60 MDIELPYLAE YARTGRATCK GCKSTISKDT LRIAVMVQSA FHDAKVPNWF HKTCFFKNQR 70 80 90 100 110 120 PSSVGDIQNI GNLRFADQKE LTDLVENIQE VISAQLGKKR SKAFNLALKD FGIEYAKSSR 130 140 150 160 170 180 STCRGCEQKI NKDLVRLRKT VYDTEVGMKY GGQPLWHHLE CFAQLRSELG WFASGEDMPG 190 200 210 220 230 240 FQSLADDDQA KVKNAIPPIK SEELPDTKRA KMELSDTNEE GEKKQRLKDQ NDAYFRFRDD 250 260 270 280 290 300 IKNKMKKKDI DILLKFNNQQ PVTGDTEKLF DQTADLLTFG AIESCSECNS CQFIVNKSGY 310 320 330 340 350 360 ICNGNHSEWT KCNKLLKEPT RSACIVPKEL KALYNFLNTV KEIPSTRIFN NFPPNKSTFS 370 380 390 400 410 420 RSLLKTNKNN DVLVRYWIFR SWGRIGTNIG NSKLEEFDTS ESAKRNFKEI YADKTGNEYE 430 440 450 460 470 480 QRDNFVKRTG RMYPIEIQYD DDQKLVKHES HFFTSKLEIS VQNLIKLIFD IDSMNKTLME 490 500 510 520 530 540 FHIDMDKMPL GKLSAHQIQS AYRVVKEIYN VLECGSNTAK LIDATNRFYT LIPHNFGVQL 550 560 570 580 590 600 PTLIETHQQI EDLRQMLDSL AEIEVAYSII KSEDVSDACN PLDNHYAQIK TQLVALDKNS 610 620 630 640 650 660 EEFSILSQYV KNTHASTHKS YDLKIVDVFK VSRQGEARRF KPFKKLHNRK LLWHGSRLTN 670 680 690 700 710 720 FVGILSHGLR IAPPEAPPTG YMFGKGIYFA DMVSKSANYC CTSQQNSTGL MLLSEVALGD 730 740 750 760 770 780 MMECTSAKYI NKLSNNKHSC FGRGRTMPDP TKSYIRSDGV EIPYGETITD EHLKSSLLYN 790 800 EYIVYDVAQV NIQYLFRMEF KYSY
	Isoform E (Embryonic) [UniParc]. Checksum: B82605E1E3804868	FASTA	613	69,956
	10 20 30 40 50 60 MDIELPYLAE YARTGRATCK GCKSTISKDT LRIAVMVQSA FHDAKVPNWF HKTCFFKNQR 70 80 90 100 110 120 PSSVGDIQNI GNLRFADQKE LTDLVENIQE VISAQLGKKR SKAFNLALKD FGIEYAKSSR 130 140 150 160 170 180 STCRGCEQKI NKDLVRLRKT VYDTEVGMKY GGQPLWHHLE CFAQLRSELG WFASGEDMPG 190 200 210 220 230 240 FQSLADDDQA KVKNAIPPIK SEELPDTKRA KMELSDTNEE GEKKQRLKDQ NDAYFRFRDD 250 260 270 280 290 300 IKNKMKKKDI DILLKFNNQQ PVTGDTEKLF DQTADLLTFG AIESCSECNS CQFIVNKSGY 310 320 330 340 350 360 ICNGNHSEWT KCNKLLKEPT RSACIVPKEL KALYNFLNTV KEIPSTRIFN NFPPNKSTFS 370 380 390 400 410 420 RSLLKTNKNN DVLVRPTIPR ISPPLYNLKF SIIGLKNQHK ELRKRIENLG GKFEVKISEN 430 440 450 460 470 480 TIAIISTELE IQKKSTRMKF AEELGIHIVP IEFLDFVEAD TEGAIKYINS TCICSWGTDP 490 500 510 520 530 540 KSRIPKETTK SLNSNSIYTK SMPVSRTFKV KDGLAVDPDS GLEDIAHVYV DSNNKYSVVL 550 560 570 580 590 600 GLTDIQRNKN SYYKVQLLKA DKKEKYWIFR SWGRIGTNIG NSKLEEFDTS ESAKRNFKEI 610 YADKTGMHFS EIH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of cDNA encoding Drosophila poly(ADP-ribose) polymerase: leucine zipper in the auto-modification domain." Uchida K., Hanai S., Ishikawa K., Ozawa Y., Uchida M., Sugimura T., Miwa M. Proc. Natl. Acad. Sci. U.S.A. 90:3481-3485(1993) [PubMed: 8475096] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II). Tissue: Embryo.
[2]	"Genomic organization of Drosophila poly(ADP-ribose) polymerase and distribution of its mRNA during development." Hanai S., Uchida M., Kobayashi S., Miwa M., Uchida K. J. Biol. Chem. 273:11881-11886(1998) [PubMed: 9565614] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS I AND II), DEVELOPMENTAL STAGE, TISSUE SPECIFICITY. Strain: Canton-S.
[3]	"The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development." Tulin A., Stewart D., Spradling A.C. Genes Dev. 16:2108-2119(2002) [PubMed: 12183365] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[4]	"The genome sequence of Drosophila melanogaster." 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. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[5]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[6]	"Heterochromatic sequences in a Drosophila whole-genome shotgun assembly." Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., Karpen G.H. Genome Biol. 3:RESEARCH0085.1-RESEARCH0085.16(2002) [PubMed: 12537574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II). Strain: Berkeley. Tissue: Embryo.
[8]	"A Drosophila full-length cDNA resource." 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. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-994 (ISOFORM II). Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D13806 mRNA. Translation: BAA02964.1. AF051548 , AF051544, AF051545, AF051546, AF051547 Genomic DNA. Translation: AAC24518.1. AF533701 mRNA. Translation: AAM93435.1. CM000459 Genomic DNA. Translation: EDP28045.1. BT015238 mRNA. Translation: AAT94467.1. AY118947 mRNA. Translation: AAM50807.1. Different initiation.
PIR	A47474.
RefSeq	NP_001104452.1. NM_001110982.2.
UniGene	Dm.7847.
3D structure databases
ProteinModelPortal	P35875.
SMR	P35875. Positions 3-93, 100-202, 217-350, 378-482, 498-632, 644-993.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-23413N.
MINT	MINT-836001.
STRING	P35875.
Proteomic databases
PRIDE	P35875.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0113885; FBpp0112608; FBgn0010247.
GeneID	3355109.
KEGG	dme:Dmel_CG40411.
NMPDR	fig|7227.3.peg.15795.
Organism-specific databases
CTD	3355109.
FlyBase	FBgn0010247. Parp.
Phylogenomic databases
eggNOG	inNOG04880.
GeneTree	EMGT00050000000757.
InParanoid	P35875.
OMA	EYSASQL.
OrthoDB	EOG4JM64P.
PhylomeDB	P35875.
Gene expression databases
Bgee	P35875.
GermOnline	CG40411. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001357. BRCT. IPR008288. NAD_ADPRT. IPR012982. PADR1. IPR012317. Poly(ADP-ribose)pol_cat_dom. IPR004102. Poly(ADP-ribose)pol_reg_dom. IPR008893. WGR_domain. IPR001510. Znf_PARP. [Graphical view]
Gene3D	G3DSA:2.20.140.10. G3DSA:2.20.140.10. 1 hit. G3DSA:1.20.142.10. PARP_reg. 1 hit. G3DSA:3.30.1740.10. Znf_PARP. 2 hits.
KO	K10798.
Pfam	PF00533. BRCT. 1 hit. PF08063. PADR1. 1 hit. PF00644. PARP. 1 hit. PF02877. PARP_reg. 1 hit. PF05406. WGR. 1 hit. PF00645. zf-PARP. 2 hits. [Graphical view]
PIRSF	PIRSF000489. NAD_ADPRT. 1 hit.
SMART	SM00292. BRCT. 1 hit. SM00773. WGR. 1 hit. [Graphical view]
SUPFAM	SSF52113. BRCT. 1 hit. SSF47587. PARP_reg. 1 hit. SSF142921. SSF142921. 1 hit.
PROSITE	PS50172. BRCT. 1 hit. PS51060. PARP_ALPHA_HD. 1 hit. PS51059. PARP_CATALYTIC. 1 hit. PS00347. PARP_ZN_FINGER_1. 1 hit. PS50064. PARP_ZN_FINGER_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	850624.

Entry information

Entry name

PARP_DROME

Accession

Primary (citable) accession number: P35875
Secondary accession number(s): A8Y590 , Q7PLT6, Q8MSB5, Q8MU87, Q9W5Q5, Q9W5S1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	January 25, 2012
This is version 132 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project